ID NEUA_MOUSE Reviewed; 432 AA. AC Q99KK2; O88719; Q8C330; Q8K2G7; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 27-NOV-2024, entry version 153. DE RecName: Full=N-acylneuraminate cytidylyltransferase; DE EC=2.7.7.43; DE AltName: Full=CMP-N-acetylneuraminic acid synthase; DE Short=CMP-NeuNAc synthase; GN Name=Cmas; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9689047; DOI=10.1073/pnas.95.16.9140; RA Muenster A.-K., Eckhardt M., Potvin B., Muehlenhoff M., Stanley P., RA Gerardy-Schahn R.; RT "Mammalian cytidine 5-prime-monophosphate N-acetylneuraminic acid RT synthetase: a nuclear protein with evolutionarily conserved structural RT motifs."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9140-9145(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION, ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-198; ARG-199; RP PRO-200; ARG-201; ARG-202; GLN-203 AND ASP-204. RX PubMed=11893746; DOI=10.1074/jbc.m201093200; RA Muenster A.-K., Weinhold B., Gotza B., Muehlenhoff M., Frosch M., RA Gerardy-Schahn R.; RT "Nuclear localization signal of murine CMP-Neu5Ac synthetase includes RT residues required for both nuclear targeting and enzymatic activity."; RL J. Biol. Chem. 277:19688-19696(2002). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Liver, and Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-35 AND ARG-50, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 40-268 IN COMPLEX WITH CMP-NEUNAC, RP AND SUBUNIT. RX PubMed=14636592; DOI=10.1016/j.jmb.2003.09.080; RA Krapp S., Muenster-Kuehnel A.-K., Kaiser J.T., Huber R., Tiralongo J., RA Gerardy-Schahn R., Jacob U.; RT "The crystal structure of murine CMP-5-N-acetylneuraminic acid RT synthetase."; RL J. Mol. Biol. 334:625-637(2003). CC -!- FUNCTION: Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) CC to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a CC substrate required for the addition of sialic acid. Has some activity CC toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D- CC glycero-D-galacto-nononic acid (KDN). {ECO:0000269|PubMed:9689047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate + CC diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43; CC Evidence={ECO:0000269|PubMed:11893746, ECO:0000269|PubMed:9689047}; CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate metabolism. CC -!- SUBUNIT: Homotetramer; the active enzyme is formed by a dimer of CC dimers. {ECO:0000269|PubMed:14636592}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11893746, CC ECO:0000269|PubMed:9689047}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99KK2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99KK2-2; Sequence=VSP_012765; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and heart, and at CC intermediate level muscle and liver. {ECO:0000269|PubMed:9689047}. CC -!- DOMAIN: The BC2 (basic cluster 2) motif is necessary and sufficient for CC the nuclear localization and contains the catalytic active site. The CC localization in the nucleus is however not required for the enzyme CC activity. CC -!- MISCELLANEOUS: [Isoform 2]: Inactive. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ006215; CAA06915.1; -; mRNA. DR EMBL; AK087150; BAC39813.1; -; mRNA. DR EMBL; BC004606; AAH04606.1; -; mRNA. DR EMBL; BC031500; AAH31500.1; -; mRNA. DR EMBL; BC063776; AAH63776.1; -; mRNA. DR CCDS; CCDS20687.1; -. [Q99KK2-1] DR RefSeq; NP_034038.2; NM_009908.2. DR PDB; 1QWJ; X-ray; 2.80 A; A/B/C/D=40-268. DR PDB; 3EWI; X-ray; 1.90 A; A/B=267-432. DR PDBsum; 1QWJ; -. DR PDBsum; 3EWI; -. DR AlphaFoldDB; Q99KK2; -. DR SMR; Q99KK2; -. DR BioGRID; 198764; 4. DR STRING; 10090.ENSMUSP00000032419; -. DR ChEMBL; CHEMBL4523436; -. DR GlyGen; Q99KK2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99KK2; -. DR PhosphoSitePlus; Q99KK2; -. DR SwissPalm; Q99KK2; -. DR PaxDb; 10090-ENSMUSP00000032419; -. DR PeptideAtlas; Q99KK2; -. DR ProteomicsDB; 252823; -. [Q99KK2-1] DR ProteomicsDB; 252824; -. [Q99KK2-2] DR Pumba; Q99KK2; -. DR DNASU; 12764; -. DR GeneID; 12764; -. DR KEGG; mmu:12764; -. DR UCSC; uc009eps.2; mouse. [Q99KK2-1] DR AGR; MGI:1337124; -. DR CTD; 55907; -. DR MGI; MGI:1337124; Cmas. DR eggNOG; ENOG502QQH3; Eukaryota. DR InParanoid; Q99KK2; -. DR OrthoDB; 5486419at2759; -. DR PhylomeDB; Q99KK2; -. DR TreeFam; TF324840; -. DR BioCyc; MetaCyc:MONOMER-14521; -. DR BRENDA; 2.7.7.43; 3474. DR BRENDA; 2.7.7.92; 3474. DR Reactome; R-MMU-4085001; Sialic acid metabolism. DR SABIO-RK; Q99KK2; -. DR UniPathway; UPA00628; -. DR BioGRID-ORCS; 12764; 23 hits in 80 CRISPR screens. DR ChiTaRS; Cmas; mouse. DR EvolutionaryTrace; Q99KK2; -. DR PRO; PR:Q99KK2; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q99KK2; protein. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; ISO:MGI. DR GO; GO:0006055; P:CMP-N-acetylneuraminate biosynthetic process; ISO:MGI. DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd02513; CMP-NeuAc_Synthase; 1. DR CDD; cd01630; HAD_KDO-like; 1. DR FunFam; 3.40.50.1000:FF:000082; N-acylneuraminate cytidylyltransferase A; 1. DR FunFam; 3.90.550.10:FF:000074; N-acylneuraminate cytidylyltransferase A; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR050793; CMP-NeuNAc_synthase. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR21485; HAD SUPERFAMILY MEMBERS CMAS AND KDSC; 1. DR PANTHER; PTHR21485:SF3; N-ACYLNEURAMINATE CYTIDYLYLTRANSFERASE; 1. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Methylation; KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase. FT CHAIN 1..432 FT /note="N-acylneuraminate cytidylyltransferase" FT /id="PRO_0000213200" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 15..31 FT /note="BC1 motif" FT MOTIF 198..204 FT /note="BC2 motif" FT MOTIF 267..274 FT /note="BC3 motif" FT ACT_SITE 199 FT BINDING 50 FT /ligand="substrate" FT BINDING 60 FT /ligand="substrate" FT BINDING 109 FT /ligand="substrate" FT BINDING 118 FT /ligand="substrate" FT BINDING 120 FT /ligand="substrate" FT BINDING 141 FT /ligand="substrate" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q8NFW8" FT MOD_RES 35 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 50 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 1..232 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012765" FT MUTAGEN 196 FT /note="P->A: Does not affect the nuclear localization." FT MUTAGEN 198 FT /note="K->A: Abolishes the nuclear localization but does FT not affect the enzyme activity; when associated with FT A-201." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 199 FT /note="R->A: Abolishes both the nuclear localization and FT the enzyme activity." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 200 FT /note="P->A: Does not affect neither the nuclear FT localization nor the enzyme activity." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 201 FT /note="R->A: Abolishes the nuclear localization but does FT not affect the enzyme activity; when associated with FT A-198." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 202 FT /note="R->A: Does not strongly affect the nuclear FT localization but strongly affects the enzyme activity." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 203 FT /note="Q->A: Does not affect the nuclear localization but FT affects the enzyme activity." FT /evidence="ECO:0000269|PubMed:11893746" FT MUTAGEN 204 FT /note="D->A: Does not affect the nuclear localization." FT /evidence="ECO:0000269|PubMed:11893746" FT CONFLICT 9 FT /note="V -> A (in Ref. 3; AAH31500/AAH63776)" FT /evidence="ECO:0000305" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:1QWJ" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 69..80 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 93..101 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 120..128 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 149..160 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 165..173 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 191..195 FT /evidence="ECO:0007829|PDB:1QWJ" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 208..219 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 220..224 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:1QWJ" FT HELIX 252..262 FT /evidence="ECO:0007829|PDB:1QWJ" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:3EWI" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 303..314 FT /evidence="ECO:0007829|PDB:3EWI" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 329..333 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:3EWI" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 376..381 FT /evidence="ECO:0007829|PDB:3EWI" FT STRAND 382..387 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 393..396 FT /evidence="ECO:0007829|PDB:3EWI" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:3EWI" FT TURN 407..410 FT /evidence="ECO:0007829|PDB:3EWI" FT HELIX 411..426 FT /evidence="ECO:0007829|PDB:3EWI" SQ SEQUENCE 432 AA; 48058 MW; BF7295535E7F6CE5 CRC64; MDALEKGAVT SGPAPRGRPS RGRPPKLQRS RGAGRGLEKP PHLAALVLAR GGSKGIPLKN IKRLAGVPLI GWVLRAALDA GVFQSVWVST DHDEIENVAK QFGAQVHRRS SETSKDSSTS LDAIVEFLNY HNEVDIVGNI QATSPCLHPT DLQKVAEMIR EEGYDSVFSV VRRHQFRWSE IQKGVREVTE PLNLNPAKRP RRQDWDGELY ENGSFYFAKR HLIEMGYLQG GKMAYYEMRA EHSVDIDVDI DWPIAEQRVL RFGYFGKEKL KEIKLLVCNI DGCLTNGHIY VSGDQKEIIS YDVKDAIGIS LLKKSGIEVR LISERACSKQ TLSALKLDCK TEVSVSDKLA TVDEWRKEMG LCWKEVAYLG NEVSDEECLK RVGLSAVPAD ACSGAQKAVG YICKCSGGRG AIREFAEHIF LLIEKVNNSC QK // ID TBG_GIAIC Reviewed; 472 AA. AC A0A644F0Y1; A8BQF3; DT 24-JAN-2024, integrated into UniProtKB/Swiss-Prot. DT 22-APR-2020, sequence version 1. DT 02-OCT-2024, entry version 17. DE RecName: Full=Tubulin gamma chain {ECO:0000255|RuleBase:RU000352, ECO:0000305}; DE AltName: Full=Gamma-tubulin {ECO:0000303|PubMed:10928459, ECO:0000303|PubMed:30318753}; DE AltName: Full=Glgamma-tubulin {ECO:0000303|PubMed:30318753}; GN ORFNames=GL50803_00114218 {ECO:0000312|EMBL:KAE8302020.1}, GN GL50803_114218 {ECO:0000312|EMBL:EDO77838.1}; OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia). OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia. OX NCBI_TaxID=184922 {ECO:0000312|EMBL:KAE8302020.1, ECO:0000312|Proteomes:UP000001548}; RN [1] {ECO:0000312|EMBL:EDO77838.1, ECO:0000312|EMBL:KAE8302020.1, ECO:0000312|Proteomes:UP000001548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000312|Proteomes:UP000001548}; RX PubMed=17901334; DOI=10.1126/science.1143837; RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D., RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J., RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U., RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D., RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J., RA Svard S.G., Sogin M.L.; RT "Genomic minimalism in the early diverging intestinal parasite Giardia RT lamblia."; RL Science 317:1921-1926(2007). RN [2] RP SUBCELLULAR LOCATION. RC STRAIN=Portland-1 {ECO:0000303|PubMed:10928459}; RX PubMed=10928459; DOI=10.1078/0171-9335-00066; RA Nohynkova E., Draber P., Reischig J., Kulda J.; RT "Localization of gamma-tubulin in interphase and mitotic cells of a RT unicellular eukaryote, Giardia intestinalis."; RL Eur. J. Cell Biol. 79:438-445(2000). RN [3] RP FUNCTION, SUBUNIT, INTERACTION WITH EB1; GCP2 AND GCP3, SUBCELLULAR RP LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 30957 / WB {ECO:0000303|PubMed:30318753}; RX PubMed=30318753; DOI=10.1002/mbo3.748; RA Kim J., Park S.J.; RT "Roles of end-binding 1 protein and gamma-tubulin small complex in RT cytokinesis and flagella formation of Giardia lamblia."; RL MicrobiologyOpen 8:e00748-e00748(2019). CC -!- FUNCTION: Tubulin is the major constituent of microtubules (Potential). CC The gamma chain is found at microtubule organizing centers (MTOC) such CC as the centrosome (PubMed:30318753). Component of the gamma-tubulin CC small complex (gamma-TuSC) involved in microtubule nucleation for the CC formation of median bodies and in the biogenesis of flagella CC (PubMed:30318753). Gamma-TuSC may be required for the correct CC positioning of EB1 within the trophozoites (PubMed:30318753). CC {ECO:0000255|RuleBase:RU000352, ECO:0000269|PubMed:30318753}. CC -!- SUBUNIT: Component of the gamma-tubulin small complex (gamma-TuSC) CC composed of tubulin gamma chain, gamma-tubulin complex protein 2 (GCP2) CC and gamma-tubulin complex protein 3 (GCP3) (PubMed:30318753). Interacts CC with GCP2 and GCP3 (PubMed:30318753). Interacts with EB1 CC (PubMed:30318753). {ECO:0000269|PubMed:30318753}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme CC {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal CC body {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10928459, CC ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, microtubule CC organizing center {ECO:0000269|PubMed:30318753}. Note=Localizes mainly CC to basal bodies of trophozoites during interface (PubMed:30318753). CC Localizes as four dots at the basis of posterolateral and ventral CC flagellar pairs in interphase (PubMed:10928459). Localizes also to CC axonemes and median body in over half of the interphase cells CC (PubMed:30318753). Colocalizes with microtubules in the median bodies CC of the interphase cells (PubMed:30318753). Localizes to basal bodies CC and median bodies in dividing stages of the trophozoites CC (PubMed:30318753). The four dots are absent in late prophase and early CC metaphase, but reappear as tiny dots at the perikinetosomal areas of CC the separated parent flagella in anaphase (PubMed:10928459). Localizes CC transiently to the centers of the mitotic spindles in anaphase CC (PubMed:30318753). The four dots localize at the basal body regions of CC each daughter karyomastigont in telophase (PubMed:10928459). CC Colocalizes with centrin outside the two nuclei in telophase CC (PubMed:30318753). Localizes to basal bodies and axonemes of the two CC daughter cells during cytokinesis (PubMed:30318753). Does not localize CC at the spindle poles of the dividing nuclei (PubMed:10928459). CC {ECO:0000269|PubMed:10928459, ECO:0000269|PubMed:30318753}. CC -!- DISRUPTION PHENOTYPE: Knockdown of expression by morpholino results in CC an arrest of cytokinesis, leading to reduced growth rate and increased CC number of cells with four nuclei. Knockdown has various defects CC including increased number of disorganized cells impertinent for CC cytokinesis and increased number of cells without furrow. However, CC knockdown does not have an effect on the number of cells defective in CC cytokinesis or abscission. Knockdown has reduced formation and volume CC of median bodies, increased number of posterolateral and ventral CC axonemes without central pair of flagellar microtubules (MTs), and CC reduced length of the caudal flagella. Knockdown does not affect CC central pair of flagellar MTs in anterior and caudal axonemes. CC {ECO:0000269|PubMed:30318753}. CC -!- SIMILARITY: Belongs to the tubulin family. CC {ECO:0000255|RuleBase:RU000352}. CC -!- SEQUENCE CAUTION: CC Sequence=EDO77838.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AACB02000033; EDO77838.1; ALT_INIT; Genomic_DNA. DR EMBL; AACB03000004; KAE8302020.1; -; Genomic_DNA. DR RefSeq; XP_001705512.1; XM_001705460.1. DR AlphaFoldDB; A0A644F0Y1; -. DR SMR; A0A644F0Y1; -. DR STRING; 184922.A0A644F0Y1; -. DR EnsemblProtists; EDO77838; EDO77838; GL50803_114218. DR GeneID; 5698417; -. DR KEGG; gla:GL50803_00114218; -. DR VEuPathDB; GiardiaDB:GL50803_114218; -. DR HOGENOM; CLU_015718_1_0_1; -. DR InParanoid; A0A644F0Y1; -. DR OMA; HRYISIL; -. DR Proteomes; UP000001548; Chromosome 2. DR GO; GO:0097729; C:9+2 motile cilium; IDA:UniProtKB. DR GO; GO:0005930; C:axoneme; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central. DR GO; GO:0008275; C:gamma-tubulin small complex; IDA:UniProtKB. DR GO; GO:0097556; C:left posteriolateral flagellum; IDA:UniProtKB. DR GO; GO:0097558; C:left ventral flagellum; IDA:UniProtKB. DR GO; GO:0097568; C:median body; IDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0097557; C:right posteriolateral flagellum; IDA:UniProtKB. DR GO; GO:0097559; C:right ventral flagellum; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB. DR GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central. DR GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB. DR GO; GO:1903673; P:mitotic cleavage furrow formation; IMP:UniProtKB. DR GO; GO:1902410; P:mitotic cytokinetic process; IMP:UniProtKB. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central. DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central. DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB. DR CDD; cd02188; gamma_tubulin; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR002454; Gamma_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR037103; Tubulin/FtsZ-like_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR023123; Tubulin_C. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01164; GAMMATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 1: Evidence at protein level; KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum; GTP-binding; KW Microtubule; Nucleotide-binding; Reference proteome. FT CHAIN 1..472 FT /note="Tubulin gamma chain" FT /id="PRO_0000459116" FT BINDING 142..148 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" SQ SEQUENCE 472 AA; 51870 MW; B5D2977F0EA7F4B3 CRC64; MPREVITIQC GQCGNQIGEV FWNRLCTEHG INPDGTLRPE AYTFNDRKDV FFYQSDDEHY VPRAILLDTE PGVISHIRNG PIKELINPEN VYIDSTGGGA GNIWTKGFQC GEAGFEKIVE IIDREADGAD SLAGFSLTHS IAGGTGSGMG SFLLDRLSDR YPKALLQTYS VFPNTTADII VQPYNSILTL QRLALCADAV VVLDNTALDR IITNHIPNEL LTNPFEHVNS LVSTVMAAST STLRLPGFMS NDLLSLVSSL VPTPRLHFLM SSYTPITSSS LNVKEHTKDQ EAGSGAVAGA AAGATRRQVH TDSIVQLVKR LLHPTNGMVS CGRDGKYISL LNIVQGEAES NQLYKSLQQI KEGRDVKFID WGPSNMQMAL SKRSPFTNEA HKVSGLMLAN HTAIRKIFDN INNTFTQLFS KRAYLQNYID SMVTGGEPEI LEQFTDAQAV CTSLSKEYEA AESKDYLEYI GM // ID CAN1_CANGA Reviewed; 597 AA. AC Q6FNY1; DT 13-SEP-2023, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-NOV-2024, entry version 112. DE RecName: Full=Arginine permease CAN1 {ECO:0000305}; GN Name=CAN1 {ECO:0000303|PubMed:37005249}; GN OrderedLocusNames=CAGL0J08162g {ECO:0000312|CGD:CAL0132774}; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593; RN [1] {ECO:0000312|Proteomes:UP000002428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). RN [2] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=KUE100 {ECO:0000303|PubMed:37005249}; RX PubMed=37005249; DOI=10.2323/jgam.2023.03.003; RA Nishimura A., Tanahashi R., Nakagami K., Morioka Y., Takagi H.; RT "Identification of an arginine transporter in Candida glabrata."; RL J. Gen. Appl. Microbiol. 68:2023.03.003-2023.03.003(2023). CC -!- FUNCTION: High-affinity permease for arginine (PubMed:37005249). May CC also transport other basic amino acids (By similarity). CC {ECO:0000250|UniProtKB:A0A1D8PPI5, ECO:0000269|PubMed:37005249}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:37005249}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- DISRUPTION PHENOTYPE: Resistance to canavanine. CC {ECO:0000269|PubMed:37005249}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR380956; CAG61014.1; -; Genomic_DNA. DR RefSeq; XP_448063.1; XM_448063.1. DR AlphaFoldDB; Q6FNY1; -. DR SMR; Q6FNY1; -. DR STRING; 284593.Q6FNY1; -. DR EnsemblFungi; CAGL0J08162g-T; CAGL0J08162g-T-p1; CAGL0J08162g. DR GeneID; 2889920; -. DR KEGG; cgr:2889920; -. DR CGD; CAL0132774; CAN1. DR VEuPathDB; FungiDB:CAGL0J08162g; -. DR eggNOG; KOG1286; Eukaryota. DR HOGENOM; CLU_007946_12_1_1; -. DR InParanoid; Q6FNY1; -. DR OMA; LFKALWY; -. DR Proteomes; UP000002428; Chromosome J. DR GO; GO:0032126; C:eisosome; IEA:EnsemblFungi. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB. DR FunFam; 1.20.1740.10:FF:000006; General amino acid permease; 1. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR004841; AA-permease/SLC12A_dom. DR InterPro; IPR004762; Amino_acid_permease_fungi. DR InterPro; IPR004840; Amoino_acid_permease_CS. DR InterPro; IPR050524; APC_YAT. DR NCBIfam; TIGR00913; 2A0310; 1. DR PANTHER; PTHR43341; AMINO ACID PERMEASE; 1. DR PANTHER; PTHR43341:SF19; LYSINE-SPECIFIC PERMEASE; 1. DR Pfam; PF00324; AA_permease; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell membrane; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..597 FT /note="Arginine permease CAN1" FT /id="PRO_0000458462" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 124..144 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 179..199 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 331..351 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 384..404 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 428..448 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 459..479 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 501..521 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 534..554 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 597 AA; 66348 MW; 905E6C468BA2E09A CRC64; MKFRNILKNE KNEKNEASAS TSHASEDIEI IPSRYDNEKF YSATEATHKK KTGSTGFDDT ISLTHTLSRS RIPTSMEDED AEEAEVHDTR VKRALKQRHI GMIALGGTIG TGLFVGISTP LSNSGPVGAL IAYIFMGTII YFVTQSLGEM ATFIPVTSSI TVFSKRFLSP AFGVANGYMY WFNWAITYAV EVSVIGQVIQ YWTFKVPLAA WIGIFWVLIT LMNFFPVKIY GEFEFWVASI KVIAIVGYLI YALIIVCGGS HQGPIGFRYW RNPGAMGAGI ISSDLGEARF LGWVSSLINA AFTYQGTELV GITAGEAANP RKSVPRAINK VVFRIVLFYI MSLFFVGLLV PYNDPRLSAS SAVIASSPFV ISIQNAGTKV LPDIFNAVVL VTVISAANSN VYVGSRVLYA LAQSGNAPKQ FAYVTRHGVP YLGVICTALL GLLAFLVVNH NANTAFNWLI NISTLAGLCA WLFISLAHIR FMQALKFRGI SRDDLPFKAK FMPWGAYYAS FFVTVIIFIQ GFQAFAPKFD VSEFFTAYIS LILLVVLFAG CQLYYRCRFL WKLEDIDIDS DRREIDAIVW EDDEPQNLWE KFWAAVA // ID T238L_HUMAN Reviewed; 79 AA. AC A6NJY4; A0A1B0GVL6; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 07-APR-2021, sequence version 3. DT 02-OCT-2024, entry version 54. DE RecName: Full=Transmembrane protein 238-like {ECO:0000305}; DE AltName: Full=FOXA1-regulated conserved small protein {ECO:0000303|PubMed:33112233}; DE Short=FORCP {ECO:0000303|PubMed:33112233}; GN Name=TMEM238L {ECO:0000312|HGNC:HGNC:44356}; GN Synonyms=FORCP {ECO:0000303|PubMed:33112233}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16344560; DOI=10.1101/gr.4039406; RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K., RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., RA Sugano S.; RT "Diversification of transcriptional modulation: large-scale identification RT and characterization of putative alternative promoters of human genes."; RL Genome Res. 16:55-65(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRI3BP, AND INDUCTION. RX PubMed=33112233; DOI=10.7554/elife.53734; RA Li X.L., Pongor L., Tang W., Das S., Muys B.R., Jones M.F., Lazar S.B., RA Dangelmaier E.A., Hartford C.C., Grammatikakis I., Hao Q., Sun Q., RA Schetter A., Martindale J.L., Tang B., Jenkins L.M., Robles A.I., RA Walker R.L., Ambs S., Chari R., Shabalina S.A., Gorospe M., Hussain S.P., RA Harris C.C., Meltzer P.S., Prasanth K.V., Aladjem M.I., Andresson T., RA Lal A.; RT "A small protein encoded by a putative lncRNA regulates apoptosis and RT tumorigenicity in human colorectal cancer cells."; RL Elife 9:0-0(2020). RN [6] RP MISCELLANEOUS. RX PubMed=35274990; DOI=10.1128/mcb.00505-21; RA Dangelmaier E.A., Li X.L., Hartford C.C.R., King J.C., Zibitt M.S., RA Chari R., Grammatikakis I., Lal A.; RT "An Evolutionarily Conserved AU-Rich Element in the 3' Untranslated Region RT of a Transcript Misannotated as a Long Noncoding RNA Regulates RNA RT Stability."; RL Mol. Cell. Biol. 42:e0050521-e0050521(2022). CC -!- FUNCTION: May play a role in inducing apoptosis during endoplasmic CC reticulum (ER) stress and in the inhibition of proliferation and CC tumorigenicity. {ECO:0000269|PubMed:33112233}. CC -!- SUBUNIT: Interacts with BRI3BP. {ECO:0000269|PubMed:33112233}. CC -!- INTERACTION: CC A6NJY4; Q8WY22: BRI3BP; NbExp=2; IntAct=EBI-40200763, EBI-359348; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:33112233}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- INDUCTION: Induced by FOXA1 in well-differentiated colorectal cancer CC (CRC) cells. {ECO:0000269|PubMed:33112233}. CC -!- MISCELLANEOUS: The TMEM238L transcript is unstable, and this CC instability is partly mediated through a conserved region containing CC AU-rich sequences in the TMEM238L 3'UTR (PubMed:35274990). Cancer cells CC lacking this conserved region display decreased proliferation and CC clonogenicity (PubMed:35274990). {ECO:0000269|PubMed:35274990, CC ECO:0000305|PubMed:35274990}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DB010820; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC015908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW89991.1; -; Genomic_DNA. DR EMBL; BC015790; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC041634; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS92258.1; -. DR AlphaFoldDB; A6NJY4; -. DR SMR; A6NJY4; -. DR IntAct; A6NJY4; 7. DR STRING; 9606.ENSP00000490566; -. DR BioMuta; -; -. DR BioMuta; TMEM238L; -. DR PeptideAtlas; A6NJY4; -. DR Ensembl; ENST00000581851.2; ENSP00000490566.1; ENSG00000263429.4. DR MANE-Select; ENST00000581851.2; ENSP00000490566.1; NM_001388428.1; NP_001375357.1. DR AGR; HGNC:44356; -. DR GeneCards; TMEM238L; -. DR HGNC; HGNC:44356; TMEM238L. DR HPA; ENSG00000263429; Group enriched (intestine, stomach, urinary bladder). DR neXtProt; NX_A6NJY4; -. DR OpenTargets; ENSG00000263429; -. DR VEuPathDB; HostDB:ENSG00000263429; -. DR GeneTree; ENSGT00940000164189; -. DR InParanoid; A6NJY4; -. DR OMA; LLFWIIW; -. DR Pharos; A6NJY4; Tdark. DR PRO; PR:A6NJY4; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; A6NJY4; protein. DR Bgee; ENSG00000263429; Expressed in mucosa of transverse colon and 68 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB. DR InterPro; IPR029365; TMEM238. DR PANTHER; PTHR28613; SI:CH211-232M10.4-RELATED; 1. DR PANTHER; PTHR28613:SF2; TRANSMEMBRANE PROTEIN 238-LIKE; 1. DR Pfam; PF15125; TMEM238; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..79 FT /note="Transmembrane protein 238-like" FT /id="PRO_0000345409" FT TRANSMEM 17..37 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT CONFLICT 14 FT /note="R -> C (in Ref. 1; DB010820 and 4; FT BC015790/BC041634)" SQ SEQUENCE 79 AA; 8766 MW; 47D1B3C0D9F8B638 CRC64; MLLGSLWGRC HPGRCALFLI LALLLDAVGL VLLLLGILAP LSSWDFFIYT GALILALSLL LWIIWYSLNI EVSPEKLDL // ID PPR29_MOUSE Reviewed; 823 AA. AC Q68FM6; Q69Z72; Q8CCW8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-NOV-2024, entry version 154. DE RecName: Full=Protein phosphatase 1 regulatory subunit 29; DE AltName: Full=Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2; DE AltName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 6; DE AltName: Full=Leucine-rich repeat-containing protein 62; DE Flags: Precursor; GN Name=Elfn2; Synonyms=Kiaa1904, Lrrc62, Ppp1r29; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 339-823. RC TISSUE=Fetal brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622; SER-671 AND SER-675, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) CC complexes. {ECO:0000250}. CC -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK031970; BAC27630.1; -; mRNA. DR EMBL; BC079588; AAH79588.1; -; mRNA. DR EMBL; BC094219; AAH94219.1; -; mRNA. DR EMBL; AK173294; BAD32572.1; -; mRNA. DR CCDS; CCDS27621.1; -. DR RefSeq; NP_898964.2; NM_183141.2. DR RefSeq; XP_006520741.1; XM_006520678.3. DR RefSeq; XP_017172014.1; XM_017316525.1. DR RefSeq; XP_017172015.1; XM_017316526.1. DR RefSeq; XP_017172017.1; XM_017316528.1. DR AlphaFoldDB; Q68FM6; -. DR SMR; Q68FM6; -. DR BioGRID; 228897; 6. DR IntAct; Q68FM6; 1. DR MINT; Q68FM6; -. DR STRING; 10090.ENSMUSP00000155111; -. DR GlyConnect; 2641; 5 N-Linked glycans (1 site). DR GlyCosmos; Q68FM6; 7 sites, 5 glycans. DR GlyGen; Q68FM6; 8 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q68FM6; -. DR PhosphoSitePlus; Q68FM6; -. DR SwissPalm; Q68FM6; -. DR PaxDb; 10090-ENSMUSP00000085960; -. DR PeptideAtlas; Q68FM6; -. DR ProteomicsDB; 291727; -. DR Antibodypedia; 274; 61 antibodies from 15 providers. DR DNASU; 207393; -. DR Ensembl; ENSMUST00000088592.6; ENSMUSP00000085960.5; ENSMUSG00000043460.8. DR Ensembl; ENSMUST00000229441.2; ENSMUSP00000155111.2; ENSMUSG00000043460.8. DR GeneID; 207393; -. DR KEGG; mmu:207393; -. DR UCSC; uc007wrf.1; mouse. DR AGR; MGI:3608416; -. DR CTD; 114794; -. DR MGI; MGI:3608416; Elfn2. DR VEuPathDB; HostDB:ENSMUSG00000043460; -. DR eggNOG; ENOG502QVFI; Eukaryota. DR GeneTree; ENSGT00940000159737; -. DR HOGENOM; CLU_018770_0_0_1; -. DR InParanoid; Q68FM6; -. DR OMA; TIPHPYS; -. DR OrthoDB; 4176548at2759; -. DR PhylomeDB; Q68FM6; -. DR TreeFam; TF332887; -. DR BioGRID-ORCS; 207393; 5 hits in 79 CRISPR screens. DR ChiTaRS; Elfn2; mouse. DR PRO; PR:Q68FM6; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q68FM6; protein. DR Bgee; ENSMUSG00000043460; Expressed in subiculum and 101 other cell types or tissues. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO. DR FunFam; 3.80.10.10:FF:000047; protein phosphatase 1 regulatory subunit 29; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR055106; ELFN_Fn3. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR050541; LRR_TM_domain-containing. DR PANTHER; PTHR24369; ANTIGEN BSP, PUTATIVE-RELATED; 1. DR PANTHER; PTHR24369:SF204; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 29-RELATED; 1. DR Pfam; PF22986; ELFN_Fn3; 1. DR Pfam; PF13855; LRR_8; 1. DR SMART; SM00369; LRR_TYP; 4. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 4. PE 1: Evidence at protein level; KW Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein; KW Protein phosphatase inhibitor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..823 FT /note="Protein phosphatase 1 regulatory subunit 29" FT /id="PRO_0000256139" FT TOPO_DOM 23..397 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 398..418 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 419..823 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 56..77 FT /note="LRR 1" FT REPEAT 80..101 FT /note="LRR 2" FT REPEAT 104..125 FT /note="LRR 3" FT REPEAT 128..149 FT /note="LRR 4" FT REPEAT 152..173 FT /note="LRR 5" FT DOMAIN 185..247 FT /note="LRRCT" FT DOMAIN 292..379 FT /note="Fibronectin type-III" FT REGION 249..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 590..624 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 622 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 80 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 85 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 117 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 247 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 749 FT /note="L -> P (in Ref. 1; BAC27630)" FT /evidence="ECO:0000305" SQ SEQUENCE 823 AA; 90029 MW; B8CC92E32D1AC4D7 CRC64; MLRLGLCAAA LLCVCQPGAV RADCWLIEGD KGYVWLAICS QNQPPYETIP QHINSTVHDL RLNENKLKAV LYSSLNRFGN LTDLNLTKNE ISYIEDGAFL GQTSLQVLQL GYNRLSNLTE GMLRGMSRLQ FLFVQHNLIE VVTPTAFSEC PSLISIDLSS NRLSRLDGAT FASLASLMVC ELAGNPFNCE CDLFGFLAWL VVFNNVTKNY DRLQCESPRE FAGYPLLVPR PYHSLNAITV LQAKCRNGSM PARPVSHPTP YSTDAQREPD ENSGFNPDEI LSVEPPASST TDASAGPAIK LHQVTFTSAT LVVIIPHPYS KMYVLVQYNN SYFSDVMTLK NKKEIVTLDK LRAHTEYTFC VTSLRNSRRF NHTCLTFTTR DLVPGDLAPS TSTTTHYIMT ILGCLFGMVI VLGAVYYCLR KRRMQEEKQK SVNVKKTILE MRYGADVDAG SIVHAAQKLG EPPVLPVARM SSIPSMVGEK LPASKGLEAG LDTPKVATKG NYIEVRTGAA GDSLARPEEE LPEIENGQGS AAEISTIAKE VDKVNQIINN CIDALKLDSA SFLGGGGGGG GGGDSDLAFE CQSLPAAPAA SSAATPGALE RPSFLSPPYK ESSHHPLQRQ LSADAAVSRK TCSVSSSGSI KSAKVFSLDV PDHPTPTGLA KSDSKYIEKG SPLNSPLDRL PLVPTGSSGS SGGGGGIHHL EVKPAYHCSE HRHSFPALYY EEGADSLSQR VSFLKPLTRS KRDSTYSQLS PRHYYSGYSS SPEYSSESTH KIWERFRPYK KHHREEVYMA AGHALRKKVQ FAKDEDLHDI LDYWKGVSAQ QKL // ID MNARL_HUMAN Reviewed; 190 AA. AC P59773; H3BM78; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2013, sequence version 2. DT 27-NOV-2024, entry version 116. DE RecName: Full=Major intrinsically disordered NOTCH2-binding receptor 1-like {ECO:0000305}; DE AltName: Full=Major intrinsically disordered NOTCH2-associated receptor 2 {ECO:0000303|PubMed:32954300}; DE AltName: Full=Membrane integral NOTCH2-associated receptor 2 {ECO:0000312|HGNC:HGNC:33914}; GN Name=MINAR2 {ECO:0000312|HGNC:HGNC:33914}; GN Synonyms=KIAA1024L {ECO:0000312|HGNC:HGNC:33914}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP INTERACTION WITH NOTCH2, AND SUBCELLULAR LOCATION. RX PubMed=32954300; DOI=10.1093/braincomms/fcaa047; RA Ho R.X., Amraei R., De La Cena K.O.C., Sutherland E.G., Mortazavi F., RA Stein T., Chitalia V., Rahimi N.; RT "Loss of MINAR2 impairs motor function and causes Parkinson's disease-like RT symptoms in mice."; RL Brain Commun. 2:fcaa047-fcaa047(2020). RN [4] RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF TRP-112 AND TYR-117. RX PubMed=36317962; DOI=10.7554/elife.80865; RA Gao G., Guo S., Zhang Q., Zhang H., Zhang C., Peng G.; RT "Kiaa1024L/Minar2 is essential for hearing by regulating cholesterol RT distribution in hair bundles."; RL Elife 11:0-0(2022). RN [5] RP FUNCTION, VARIANT DFNB120 48-TRP--THR-190 DEL, AND CHARACTERIZATION OF RP VARIANT DFNB120 48-TRP--THR-190 DEL. RX PubMed=35727972; DOI=10.1073/pnas.2204084119; RA Bademci G., Lachgar-Ruiz M., Deokar M., Zafeer M.F., Abad C., RA Yildirim Baylan M., Ingham N.J., Chen J., Sineni C.J., Vadgama N., RA Karakikes I., Guo S., Duman D., Singh N., Harlalka G., Jain S.P., RA Chioza B.A., Walz K., Steel K.P., Nasir J., Tekin M.; RT "Mutations in MINAR2 encoding membrane integral NOTCH2-associated receptor RT 2 cause deafness in humans and mice."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2204084119-e2204084119(2022). CC -!- FUNCTION: Binds cholesterol and may regulate the distribution and CC homeostasis of cholesterol in hair cells (PubMed:36317962). May play a CC role in angiogenesis (PubMed:35727972). {ECO:0000269|PubMed:35727972, CC ECO:0000269|PubMed:36317962}. CC -!- SUBUNIT: Interacts with NOTCH2. {ECO:0000269|PubMed:32954300}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:F1QEA1}; CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum CC membrane {ECO:0000305|PubMed:32954300}; Single-pass membrane protein CC {ECO:0000255}. Note=Localizes to the stereocilia and the apical region CC of hair cell, apparently around and just below the cuticular plate (By CC similarity). Co-localized with cholesterol in the stereocilia (By CC similarity). {ECO:0000250|UniProtKB:F1QEA1}. CC -!- TISSUE SPECIFICITY: Highly expressed in the auditory hair cells. CC {ECO:0000269|PubMed:36317962}. CC -!- DISEASE: Deafness, autosomal recessive, 120 (DFNB120) [MIM:620238]: A CC form of non-syndromic deafness characterized by congenital or CC prelingual onset of severe to profound sensorineural hearing loss. CC Sensorineural hearing loss results from damage to the neural receptors CC of the inner ear, the nerve pathways to the brain, or the area of the CC brain that receives sound information. {ECO:0000269|PubMed:35727972}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the MINAR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC008591; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW62380.1; -; Genomic_DNA. DR CCDS; CCDS58966.1; -. DR RefSeq; NP_001244237.1; NM_001257308.1. DR AlphaFoldDB; P59773; -. DR STRING; 9606.ENSP00000454268; -. DR GlyGen; P59773; 2 sites. DR iPTMnet; P59773; -. DR PhosphoSitePlus; P59773; -. DR BioMuta; KIAA1024L; -. DR DMDM; 519668667; -. DR MassIVE; P59773; -. DR PaxDb; 9606-ENSP00000454268; -. DR PeptideAtlas; P59773; -. DR Antibodypedia; 2707; 6 antibodies from 6 providers. DR DNASU; 100127206; -. DR Ensembl; ENST00000564719.2; ENSP00000454268.1; ENSG00000186367.7. DR GeneID; 100127206; -. DR KEGG; hsa:100127206; -. DR MANE-Select; ENST00000564719.2; ENSP00000454268.1; NM_001257308.2; NP_001244237.1. DR UCSC; uc031skx.2; human. DR AGR; HGNC:33914; -. DR CTD; 100127206; -. DR DisGeNET; 100127206; -. DR GeneCards; MINAR2; -. DR HGNC; HGNC:33914; MINAR2. DR HPA; ENSG00000186367; Tissue enriched (skeletal). DR MalaCards; MINAR2; -. DR MIM; 620215; gene. DR MIM; 620238; phenotype. DR neXtProt; NX_P59773; -. DR OpenTargets; ENSG00000186367; -. DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB. DR VEuPathDB; HostDB:ENSG00000186367; -. DR eggNOG; ENOG502RZQB; Eukaryota. DR GeneTree; ENSGT00530000063851; -. DR HOGENOM; CLU_120056_0_0_1; -. DR InParanoid; P59773; -. DR OMA; ATHGMFQ; -. DR OrthoDB; 5355182at2759; -. DR PathwayCommons; P59773; -. DR BioGRID-ORCS; 100127206; 12 hits in 1131 CRISPR screens. DR ChiTaRS; KIAA1024L; human. DR Pharos; P59773; Tdark. DR PRO; PR:P59773; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P59773; protein. DR Bgee; ENSG00000186367; Expressed in primordial germ cell in gonad and 18 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0032420; C:stereocilium; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB. DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB. DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IEA:Ensembl. DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR GO; GO:0090659; P:walking behavior; IEA:Ensembl. DR InterPro; IPR039706; MINAR1-like. DR InterPro; IPR009626; MINAR1-like_C. DR PANTHER; PTHR31530; MAJOR INTRINSICALLY DISORDERED NOTCH2-BINDING RECEPTOR 1 MINAR1 FAMILY MEMBER; 1. DR PANTHER; PTHR31530:SF4; MAJOR INTRINSICALLY DISORDERED NOTCH2-BINDING RECEPTOR 1-LIKE; 1. DR Pfam; PF06789; MINAR1_C; 1. PE 1: Evidence at protein level; KW Deafness; Disease variant; Endoplasmic reticulum; Glycoprotein; Lysosome; KW Membrane; Non-syndromic deafness; Phosphoprotein; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..190 FT /note="Major intrinsically disordered NOTCH2-binding FT receptor 1-like" FT /id="PRO_0000157135" FT TRANSMEM 169..189 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C4X7" FT CARBOHYD 109 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 125 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 48..190 FT /note="Missing (in DFNB120; enhances angiogenesis; enhances FT MAPK signaling pathway)" FT /evidence="ECO:0000269|PubMed:35727972" FT /id="VAR_087627" FT MUTAGEN 112 FT /note="W->A: Compromises cholesterol recruitment to the FT perinuclear region; when associated with A-117." FT /evidence="ECO:0000269|PubMed:36317962" FT MUTAGEN 117 FT /note="Y->A: Compromises cholesterol recruitment to the FT perinuclear region; when associated with A-112." FT /evidence="ECO:0000269|PubMed:36317962" SQ SEQUENCE 190 AA; 21573 MW; 3BC483841BB66CA5 CRC64; MDLSVLPNNN HPDKFLQLDV KSLTRSSALL QASLVRFPGG NYPAAQHWQN LVYSQREKKN IAAQRIRGSS ADSLVTADSP PPSMSSVMKN NPLYGDLSLE EAMEERKKNP SWTIEEYDKH SLHTNLSGHL KENPNDLRFW LGDMYTPGFD TLLKKEEKQE KHSKFCRMGL ILLVVISILV TIVTIITFFT // ID AMPP_PLAF7 Reviewed; 777 AA. AC A0A144A2H0; DT 03-MAY-2023, integrated into UniProtKB/Swiss-Prot. DT 08-JUN-2016, sequence version 1. DT 27-NOV-2024, entry version 41. DE RecName: Full=Aminopeptidase P {ECO:0000303|PubMed:17895246}; DE Short=PfAPP {ECO:0000303|PubMed:17895246}; DE EC=3.4.11.9 {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122}; DE AltName: Full=Xaa-Pro aminopeptidase {ECO:0000305}; DE Flags: Precursor; GN Name=APP {ECO:0000303|PubMed:17895246}; GN ORFNames=PF14_0517, PF3D7_1454400 {ECO:0000312|EMBL:CZU00239.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450}; RN [1] {ECO:0000312|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450}; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX PubMed=17895246; DOI=10.1074/jbc.m703643200; RA Dalal S., Klemba M.; RT "Roles for two aminopeptidases in vacuolar hemoglobin catabolism in RT Plasmodium falciparum."; RL J. Biol. Chem. 282:35978-35987(2007). RN [3] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL RP STAGE, AND PROTEOLYTIC CLEAVAGE. RX PubMed=19574214; DOI=10.1074/jbc.m109.018424; RA Ragheb D., Bompiani K., Dalal S., Klemba M.; RT "Evidence for catalytic roles for Plasmodium falciparum aminopeptidase P in RT the food vacuole and cytosol."; RL J. Biol. Chem. 284:24806-24815(2009). RN [4] {ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 108-764 IN COMPLEX WITH MANGANESE RP AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY RP REGULATION. RX PubMed=27462122; DOI=10.1042/bcj20160550; RA Drinkwater N., Sivaraman K.K., Bamert R.S., Rut W., Mohamed K., Vinh N.B., RA Scammells P.J., Drag M., McGowan S.; RT "Structure and substrate fingerprint of aminopeptidase P from Plasmodium RT falciparum."; RL Biochem. J. 473:3189-3204(2016). CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from CC the N-termini of peptides (PubMed:17895246, PubMed:19574214, CC PubMed:27462122). In the food vacuole, involved in the final step of CC host hemoglobin catabolism, by cleaving hemoglobin-derived CC oligopeptides (PubMed:17895246, PubMed:19574214). In the cytoplasm, may CC be involved in the last steps of the turnover of ubiquitinated proteins CC (Probable). {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214, CC ECO:0000269|PubMed:27462122, ECO:0000305|PubMed:19574214}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of any N-terminal amino acid, including proline, that CC is linked to proline, even from a dipeptide or tripeptide.; CC EC=3.4.11.9; Evidence={ECO:0000269|PubMed:17895246, CC ECO:0000269|PubMed:19574214, ECO:0000269|PubMed:27462122}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:19574214}; CC Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:27462122}; CC -!- ACTIVITY REGULATION: Partially activated by Co(2+) and Mg(2+) has no CC effect (PubMed:19574214). Inhibited by 1 mM Zn(2+), Ni(2+), or Cu(2+) CC (PubMed:19574214). Inhibited by apstatin, a non-hydrolysable peptide CC analog (PubMed:27462122). {ECO:0000269|PubMed:19574214, CC ECO:0000269|PubMed:27462122}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.51 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and CC 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; CC KM=0.86 mM for human hemoglobin peptide HbPep1 (FPHFD) (at pH 5.5 and CC 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; CC KM=1.4 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 7.5 and CC 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; CC KM=1.8 mM for human hemoglobin peptide HbPep2 (YPWTQ) (at pH 5.5 and CC 37 degrees Celsius) {ECO:0000269|PubMed:19574214}; CC Note=kcat is 8.6 sec(-1) with for human hemoglobin peptide HbPep1 CC (FPHFD) as substrate (at pH 7.5 and 37 degrees Celsius) CC (PubMed:19574214). kcat is 5.4 sec(-1) with for human hemoglobin CC peptide HbPep1 (FPHFD) as substrate (at pH 5.5 and 37 degrees CC Celsius) (PubMed:19574214). kcat is 1500 sec(-1) with for human CC hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 7.5 and 37 CC degrees Celsius) (PubMed:19574214). kcat is 12 sec(-1) with for human CC hemoglobin peptide HbPep2 (YPWTQ) as substrate (at pH 5.5 and 37 CC degrees Celsius) (PubMed:19574214). {ECO:0000269|PubMed:19574214}; CC pH dependence: CC Optimum pH is 7.5 (PubMed:19574214). Active at pH 5.5-7.5 CC (PubMed:19574214). {ECO:0000269|PubMed:19574214}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19574214}. CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:17895246, CC ECO:0000269|PubMed:19574214}. Cytoplasm {ECO:0000269|PubMed:17895246, CC ECO:0000269|PubMed:19574214}. Note=Localizes to the digestive (or food) CC vacuole, an acidic vacuole where host hemoglobin is digested. CC {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage including CC in rings, trophozoites and schizonts (at protein level). CC {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:19574214}. CC -!- PTM: The N-terminus may be proteolytically cleaved to generate a 73-kDa CC mature form. {ECO:0000269|PubMed:19574214}. CC -!- SIMILARITY: Belongs to the peptidase M24B family. CC {ECO:0000255|RuleBase:RU000590}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LN999946; CZU00239.1; -; Genomic_DNA. DR RefSeq; XP_001348691.1; XM_001348655.1. DR PDB; 5JQK; X-ray; 2.35 A; A/B=129-775. DR PDB; 5JR6; X-ray; 2.30 A; A/B=129-775. DR PDBsum; 5JQK; -. DR PDBsum; 5JR6; -. DR AlphaFoldDB; A0A144A2H0; -. DR SMR; A0A144A2H0; -. DR STRING; 36329.A0A144A2H0; -. DR PaxDb; 5833-PF14_0517; -. DR EnsemblProtists; CZU00239; CZU00239; PF3D7_1454400. DR GeneID; 812099; -. DR KEGG; pfa:PF3D7_1454400; -. DR VEuPathDB; PlasmoDB:PF3D7_1454400; -. DR InParanoid; A0A144A2H0; -. DR PhylomeDB; A0A144A2H0; -. DR BRENDA; 3.4.11.9; 4889. DR Proteomes; UP000001450; Chromosome 14. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0020020; C:food vacuole; IDA:UniProtKB. DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:UniProtKB. DR GO; GO:0042540; P:hemoglobin catabolic process; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR CDD; cd01085; APP; 1. DR FunFam; 3.90.230.10:FF:000009; xaa-Pro aminopeptidase 2; 1. DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1. DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR000587; Creatinase_N. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR033740; Pept_M24B. DR InterPro; IPR032416; Peptidase_M24_C. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR InterPro; IPR050422; X-Pro_aminopeptidase_P. DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1. DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1. DR Pfam; PF01321; Creatinase_N; 1. DR Pfam; PF16189; Creatinase_N_2; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF16188; Peptidase_M24_C; 1. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Manganese; KW Metal-binding; Protease; Reference proteome; Signal; Vacuole. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT PROPEP 18..? FT /evidence="ECO:0000305|PubMed:19574214" FT /id="PRO_0000457772" FT CHAIN ?..777 FT /note="Aminopeptidase P" FT /evidence="ECO:0000255" FT /id="PRO_5007516016" FT BINDING 551 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:27462122, FT ECO:0007744|PDB:5JR6" FT BINDING 570 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 581 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 581 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 640 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:27462122, FT ECO:0007744|PDB:5JR6" FT BINDING 644 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 653 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:27462122, FT ECO:0007744|PDB:5JR6" FT BINDING 676 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 690 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT BINDING 690 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:27462122, FT ECO:0007744|PDB:5JQK, ECO:0007744|PDB:5JR6" FT HELIX 132..145 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 180..186 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:5JQK" FT STRAND 192..196 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 200..206 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 219..223 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 246..259 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 314..317 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 321..334 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 338..344 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 347..354 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 369..376 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 381..389 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 396..400 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 404..406 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 408..411 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 415..421 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 424..426 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 440..444 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 450..454 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 467..473 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 477..507 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 509..512 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 515..527 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 532..537 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 540..543 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 544..548 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 556..558 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 564..571 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 573..575 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 582..589 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 593..611 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 620..632 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 633..635 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 642..645 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 652..659 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 661..663 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 671..675 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 678..681 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 682..684 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 685..688 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 690..700 FT /evidence="ECO:0007829|PDB:5JR6" FT STRAND 705..711 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 719..721 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 729..751 FT /evidence="ECO:0007829|PDB:5JR6" FT TURN 754..756 FT /evidence="ECO:0007829|PDB:5JR6" FT HELIX 759..768 FT /evidence="ECO:0007829|PDB:5JR6" SQ SEQUENCE 777 AA; 90130 MW; 96DD8BF540EA3104 CRC64; MQLNFLLFVF IFLMVFHLNI FNKGKRQNLV SAYLNHFKKS YFSGVTSGSD CVNKSEVSSD NNNNNNNNNN KIAHNFFSKK YQRNFENNNL SENQENNKNI IYSGSNIFKN IYNTEMMSNN NTVDVNMMDN NPAARLEELR TIMKKNKIDV YILINSDEHN SEIINEKDKK IVKITNYSGA DGILIVTKDK PILYVNALYE LQAMNELDQN LFTLRISRID NRDEIFETIS SLEFNTIAFD GKNTSVVFYE KLRKALLNAY PKKKIVEKII YNNNFDDVNK KDDENVLNFL VLEKSLVEIK DYPVNNKTLY IHDRKYNGAC AGEKIDKLKQ SLMYDIKNVD NLLLSELDEI AYLLNLRGYD YQYSPLFYSY LLFQFDREEQ DFSKIVFFTT VKNLPADVKN LLEINKVIVK EYEEIVPYLR DVVIPSIPKH NDDNPDFKKY DISLSPYINL MIYKLFDRKN VLLQNSPVVK MKAVKNDVEI DNMKQAHILD GLALLQFFHW CEQKRKTKEL FNETEMSLRH KVDYFRSTKK NFIFPSFSTI SASGPNAAVI HYECTDKTNA TIKPAIYLLD SGGQYLHGTT DVTRTTHFGE PTAEEKRIYT LVLKGHLRLR KVIFASYTNS SALDFIAREN LFNNFMDYNH GTGHGVGLTL NVHEGGCSIG PVGGAPLKKN MVLSNEPGYY MKDKFGVRIE NMQYVISKEI TDTTEYLSFD DLTMYPYEKK LLDFSLLTNQ EIKELNEYHT TIRNTLLPLV KQSPQEYGES VEKYLIEITE PIAIHNN // ID TM260_HUMAN Reviewed; 707 AA. AC Q9NX78; A8KAN4; B3KPF5; Q0VAA1; Q86XE1; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-NOV-2024, entry version 149. DE RecName: Full=Protein O-mannosyl-transferase TMEM260 {ECO:0000305}; DE EC=2.4.1.109 {ECO:0000269|PubMed:37186866}; DE AltName: Full=Transmembrane protein 260 {ECO:0000305}; GN Name=TMEM260 {ECO:0000303|PubMed:28318500, GN ECO:0000312|HGNC:HGNC:20185}; GN Synonyms=C14orf101 {ECO:0000312|HGNC:HGNC:20185}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ileal mucosa, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP SER-245. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TISSUE SPECIFICITY (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1 AND RP 3), INVOLVEMENT IN SHDRA, VARIANT SHDRA 465-GLN--VAL-707 DEL, AND RP CHARACTERIZATION OF VARIANT SHDRA 465-GLN--VAL-707 DEL. RX PubMed=28318500; DOI=10.1016/j.ajhg.2017.02.007; RA Ta-Shma A., Khan T.N., Vivante A., Willer J.R., Matak P., Jalas C., RA Pode-Shakked B., Salem Y., Anikster Y., Hildebrandt F., Katsanis N., RA Elpeleg O., Davis E.E.; RT "Mutations in TMEM260 cause a pediatric neurodevelopmental, cardiac, and RT renal syndrome."; RL Am. J. Hum. Genet. 100:666-675(2017). RN [5] RP VARIANTS SHDRA LYS-115; 465-GLN--VAL-707 DEL; 470-TYR--VAL-707 DEL AND RP GLN-582. RX PubMed=34612517; DOI=10.1111/cge.14071; RG Genomics England Research Consortium; RA Pagnamenta A.T., Jackson A., Perveen R., Beaman G., Petts G., Gupta A., RA Hyder Z., Chung B.H., Kan A.S., Cheung K.W., Kerstjens-Frederikse W.S., RA Abbott K.M., Elpeleg O., Taylor J.C., Banka S., Ta-Shma A.; RT "Biallelic TMEM260 variants cause truncus arteriosus, with or without renal RT defects."; RL Clin. Genet. 101:127-133(2022). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION RP AT ASN-568, VARIANTS SHDRA TYR-98; ARG-453 AND 465-GLN--VAL-707 DEL, RP CHARACTERIZATION OF VARIANTS SHDRA TYR-98; ARG-453 AND 465-GLN--VAL-707 RP DEL, AND MUTAGENESIS OF ASP-52. RX PubMed=37186866; DOI=10.1073/pnas.2302584120; RA Larsen I.S.B., Povolo L., Zhou L., Tian W., Mygind K.J., Hintze J., RA Jiang C., Hartill V., Prescott K., Johnson C.A., Mullegama S.V., RA McConkie-Rosell A., McDonald M., Hansen L., Vakhrushev S.Y., RA Schjoldager K.T., Clausen H., Worzfeld T., Joshi H.J., Halim A.; RT "The SHDRA syndrome-associated geDne TMEM260 encodes a protein-specific O- RT mannosyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 120:e2302584120-e2302584120(2023). CC -!- FUNCTION: O-mannosyl-transferase that transfers mannosyl residues to CC the hydroxyl group of serine or threonine residues of proteins CC (PubMed:37186866). Specifically glycosylates the IPT/TIG domain of CC target proteins, such as MET and MST1R/RON (PubMed:37186866). TMEM260- CC mediated O-mannosylated residues are composed of single mannose glycans CC that are not elongated or modified (PubMed:37186866). CC {ECO:0000269|PubMed:37186866}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L- CC seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di- CC trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498, CC Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; CC EC=2.4.1.109; Evidence={ECO:0000269|PubMed:37186866}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17378; CC Evidence={ECO:0000269|PubMed:37186866}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L- CC threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a CC di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498, CC Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; CC EC=2.4.1.109; Evidence={ECO:0000269|PubMed:37186866}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53397; CC Evidence={ECO:0000269|PubMed:37186866}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:37186866}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane CC {ECO:0000269|PubMed:28318500}. Note=Shows perinuclear localization. CC {ECO:0000269|PubMed:28318500}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Long; CC IsoId=Q9NX78-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NX78-2; Sequence=VSP_008621; CC Name=3; Synonyms=Short; CC IsoId=Q9NX78-3; Sequence=VSP_058993, VSP_058994; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in brain, heart, kidney, CC liver, lung, pancreas and placenta but are not detected in skeletal CC muscle. {ECO:0000269|PubMed:28318500}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in brain, heart, kidney, CC liver, lung, pancreas and placenta but are not detected in skeletal CC muscle. {ECO:0000269|PubMed:28318500}. CC -!- DISEASE: Structural heart defects and renal anomalies syndrome (SHDRA) CC [MIM:617478]: An autosomal recessive syndrome characterized by central CC nervous system, cardiac, renal, and digit abnormalities. Clinical CC features include ventricular and atrial septal defects, truncus CC arteriosus, tetralogy of Fallot, partial anomalous pulmonary venous CC return, renal cysts, renal failure, and generalized edema. Some CC patients show partial agenesis of corpus callosum. CC {ECO:0000269|PubMed:28318500, ECO:0000269|PubMed:34612517, CC ECO:0000269|PubMed:37186866}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glycosyltransferase 117 (GT117) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91139.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BC045556; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK000399; BAA91139.1; ALT_INIT; mRNA. DR EMBL; AK293099; BAF85788.1; -; mRNA. DR EMBL; AK056291; BAG51667.1; -; mRNA. DR EMBL; AL161757; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355103; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359234; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455900; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC045556; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC121163; AAI21164.1; -; mRNA. DR CCDS; CCDS9727.2; -. [Q9NX78-1] DR RefSeq; NP_060269.3; NM_017799.3. [Q9NX78-1] DR AlphaFoldDB; Q9NX78; -. DR SMR; Q9NX78; -. DR BioGRID; 120258; 12. DR IntAct; Q9NX78; 10. DR STRING; 9606.ENSP00000261556; -. DR GlyGen; Q9NX78; 3 sites, 2 N-linked glycans (1 site). DR iPTMnet; Q9NX78; -. DR PhosphoSitePlus; Q9NX78; -. DR SwissPalm; Q9NX78; -. DR BioMuta; TMEM260; -. DR DMDM; 296439393; -. DR jPOST; Q9NX78; -. DR MassIVE; Q9NX78; -. DR PaxDb; 9606-ENSP00000261556; -. DR PeptideAtlas; Q9NX78; -. DR ProteomicsDB; 58786; -. DR ProteomicsDB; 83054; -. [Q9NX78-1] DR Antibodypedia; 185; 45 antibodies from 16 providers. DR DNASU; 54916; -. DR Ensembl; ENST00000261556.11; ENSP00000261556.6; ENSG00000070269.14. [Q9NX78-1] DR Ensembl; ENST00000538838.5; ENSP00000441934.1; ENSG00000070269.14. [Q9NX78-3] DR GeneID; 54916; -. DR KEGG; hsa:54916; -. DR MANE-Select; ENST00000261556.11; ENSP00000261556.6; NM_017799.4; NP_060269.3. DR UCSC; uc001xcm.4; human. [Q9NX78-1] DR UCSC; uc059bva.1; human. DR AGR; HGNC:20185; -. DR CTD; 54916; -. DR DisGeNET; 54916; -. DR GeneCards; TMEM260; -. DR HGNC; HGNC:20185; TMEM260. DR HPA; ENSG00000070269; Tissue enhanced (cervix). DR MalaCards; TMEM260; -. DR MIM; 617449; gene. DR MIM; 617478; phenotype. DR neXtProt; NX_Q9NX78; -. DR OpenTargets; ENSG00000070269; -. DR PharmGKB; PA134894829; -. DR VEuPathDB; HostDB:ENSG00000070269; -. DR eggNOG; ENOG502QSIA; Eukaryota. DR GeneTree; ENSGT00390000013544; -. DR HOGENOM; CLU_019631_1_0_1; -. DR InParanoid; Q9NX78; -. DR OMA; HSVNLMC; -. DR OrthoDB; 51906at2759; -. DR PhylomeDB; Q9NX78; -. DR TreeFam; TF329604; -. DR PathwayCommons; Q9NX78; -. DR SignaLink; Q9NX78; -. DR BioGRID-ORCS; 54916; 11 hits in 1162 CRISPR screens. DR ChiTaRS; TMEM260; human. DR GenomeRNAi; 54916; -. DR Pharos; Q9NX78; Tdark. DR PRO; PR:Q9NX78; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9NX78; protein. DR Bgee; ENSG00000070269; Expressed in corpus epididymis and 187 other cell types or tissues. DR ExpressionAtlas; Q9NX78; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:UniProtKB. DR GO; GO:0051604; P:protein maturation; IDA:UniProtKB. DR InterPro; IPR052724; GT117_domain-containing. DR InterPro; IPR021280; TMEM260-like. DR PANTHER; PTHR16214; TRANSMEMBRANE PROTEIN 260; 1. DR PANTHER; PTHR16214:SF3; TRANSMEMBRANE PROTEIN 260; 1. DR Pfam; PF11028; TMEM260-like; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein; KW Glycosyltransferase; Membrane; Proteomics identification; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..707 FT /note="Protein O-mannosyl-transferase TMEM260" FT /id="PRO_0000089905" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 94..114 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 141..161 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 318..338 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 356..376 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 377..707 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:37186866" FT CARBOHYD 407 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 535 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 568 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:37186866" FT VAR_SEQ 287..707 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008621" FT VAR_SEQ 409 FT /note="S -> R (in isoform 3)" FT /evidence="ECO:0000305|PubMed:15489334" FT /id="VSP_058993" FT VAR_SEQ 410..707 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305|PubMed:15489334" FT /id="VSP_058994" FT VARIANT 98 FT /note="C -> Y (in SHDRA; decreased stability; FT dbSNP:rs1170968257)" FT /evidence="ECO:0000269|PubMed:37186866" FT /id="VAR_088292" FT VARIANT 115 FT /note="R -> K (in SHDRA; uncertain significance; FT dbSNP:rs747632686)" FT /evidence="ECO:0000269|PubMed:34612517" FT /id="VAR_088293" FT VARIANT 245 FT /note="A -> S (in dbSNP:rs17776256)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_057823" FT VARIANT 453 FT /note="C -> R (in SHDRA; decreased stability; FT dbSNP:rs752523485)" FT /evidence="ECO:0000269|PubMed:37186866" FT /id="VAR_088294" FT VARIANT 465..707 FT /note="Missing (in SHDRA; reduced expression of isoform 1 FT due to nonsense-mediated decay in patient-derived cells)" FT /evidence="ECO:0000269|PubMed:28318500, FT ECO:0000269|PubMed:34612517, ECO:0000269|PubMed:37186866" FT /id="VAR_078766" FT VARIANT 470..707 FT /note="Missing (in SHDRA)" FT /evidence="ECO:0000269|PubMed:34612517" FT /id="VAR_088295" FT VARIANT 565 FT /note="S -> N (in dbSNP:rs1041316)" FT /id="VAR_057824" FT VARIANT 582 FT /note="E -> Q (in SHDRA; uncertain significance; FT dbSNP:rs761443112)" FT /evidence="ECO:0000269|PubMed:34612517" FT /id="VAR_088296" FT MUTAGEN 52 FT /note="D->A: Abolished O-mannosyltransferase activity." FT /evidence="ECO:0000269|PubMed:37186866" FT CONFLICT 3 FT /note="P -> H (in Ref. 3; BC045556)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="I -> T (in Ref. 1; BAF85788)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="F -> V (in Ref. 1; BAA91139)" FT /evidence="ECO:0000305" FT CONFLICT 680 FT /note="N -> S (in Ref. 1; BAF85788/BAG51667)" FT /evidence="ECO:0000305" SQ SEQUENCE 707 AA; 79536 MW; F3EAB7ED42B77489 CRC64; MSPHGDGRGQ AQGRAVRVGL RRSGGIRGGV AVFAAVAAVF TFTLPPSVPG GDSGELITAA HELGVAHPPG YPLFTLVAKL AITLFPFGSI AYRVNLLCGL FGAVAASLLF FTVFRLSGSS AGGILAAGVF SFSRLTWQWS IAAEVFSLNN LFVGLLMALT VHFEEAATAK ERSKVAKIGA FCCGLSLCNQ HTIILYVLCI IPWILFQLLK KKELSLGSLL KLSLYFSAGL LPYVHLPISS YLNHARWTWG DQTTLQGFLT HFLREEYGTF SLAKSEIGSS MSEILLSQVT NMRTELSFNI QALAVCANIC LATKDRQNPS LVWLFTGMFC IYSLFFAWRA NLDISKPLFM GVVERFWMQS NAVVAVLAGI GLAAVVSETN RVLNSNGLQC LEWLSATLFV VYQIYSNYSV CDQRTNYVID KFAKNLLTSM PHDAIILLRG DLPGNSLRYM HYCEGLRPDI SLVDQEMMTY EWYLPKMAKH LPGVNFPGNR WNPVEGILPS GMVTFNLYHF LEVNKQKETF VCIGIHEGDP TWKKNYSLWP WGSCDKLVPL EIVFNPEEWI KLTKSIYNWT EEYGRFDPSS WESVANEEMW QARMKTPFFI FNLAETAHMP SKVKAQLYAQ AYDLYKEIVY LQKEHPVNWH KNYAIACERM LRLQARDADP EVLLSETIRH FRLYSQKAPN DPQQADILGA LKHLRKELQS LRNRKNV // ID SIR5_FUSO4 Reviewed; 326 AA. AC A0A0J9UVG7; A0A0D2XPP4; DT 03-MAY-2023, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2015, sequence version 1. DT 27-NOV-2024, entry version 35. DE RecName: Full=NAD-dependent protein deacylase SIR5 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9NXA8}; DE AltName: Full=FoSIR5 {ECO:0000303|PubMed:34927582}; DE AltName: Full=NAD-dependent protein deacetylase SIR5 {ECO:0000305}; DE EC=2.3.1.286 {ECO:0000255}; DE AltName: Full=Protein decrotonylase SIR5 {ECO:0000303|PubMed:34927582}; DE EC=2.3.1.- {ECO:0000269|PubMed:34927582}; DE Flags: Precursor; GN Name=SIR5 {ECO:0000303|PubMed:34927582}; GN ORFNames=FOXG_05932 {ECO:0000312|EMBL:KNB03449.1}; OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 OS / NRRL 34936) (Fusarium vascular wilt of tomato). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium oxysporum species complex. OX NCBI_TaxID=426428 {ECO:0000312|EMBL:KNB03449.1}; RN [1] {ECO:0000312|EMBL:KNB03449.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936 RC {ECO:0000312|EMBL:KNB03449.1}; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W., RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.; RT "Comparative genomics reveals mobile pathogenicity chromosomes in RT Fusarium."; RL Nature 464:367-373(2010). RN [2] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH LAT1, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=34927582; DOI=10.7554/elife.75583; RA Zhang N., Song L., Xu Y., Pei X., Luisi B.F., Liang W.; RT "The decrotonylase FoSir5 facilitates mitochondrial metabolic state RT switching in conidial germination of Fusarium oxysporum."; RL Elife 10:e75583-e75583(2021). CC -!- FUNCTION: NAD-dependent protein-lysine deacylase that decrotonylates CC the PDC (pyruvate dehydrogenase complex) subunit LAT1 at 'Lys-148' to CC inhibit PDC activity and consequently ATP production (PubMed:34927582). CC Also decrotonylates histone H3 crotonylated at 'Lys-18' (H3K18cr), to CC repress the expression of genes involved in aerobic respiration CC (PubMed:34927582). May also act as a NAD-dependent deacetylase (By CC similarity). Does not mediate desuccinylation, demalonylation, or CC deglutarylation of LAT1 (PubMed:34927582). CC {ECO:0000250|UniProtKB:P06700, ECO:0000269|PubMed:34927582}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-acetyl- CC ADP-D-ribose + nicotinamide + L-lysyl-[protein]; CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-(2E)-butenoyl-L-lysyl-[protein] + H2O = (2E)-2-butenoate CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; CC Evidence={ECO:0000269|PubMed:34927582}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q9NXA8}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8}; CC -!- SUBUNIT: Interacts with LAT1; the interaction is direct. CC {ECO:0000269|PubMed:34927582}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34927582}. CC Cytoplasm, cytosol {ECO:0000269|PubMed:34927582}. Nucleus CC {ECO:0000269|PubMed:34927582}. Chromosome CC {ECO:0000269|PubMed:34927582}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in conidia, decreases during CC germination, and increases again in the mycelium. CC {ECO:0000269|PubMed:34927582}. CC -!- DISRUPTION PHENOTYPE: Increases crotonylation of LAT1 CC (PubMed:34927582). Accelerates conidial germination (PubMed:34927582). CC Increases virulence in tomato (PubMed:34927582). CC {ECO:0000269|PubMed:34927582}. CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS231701; KNB03449.1; -; Genomic_DNA. DR RefSeq; XP_018241494.1; XM_018384418.1. DR AlphaFoldDB; A0A0J9UVG7; -. DR SMR; A0A0J9UVG7; -. DR STRING; 426428.A0A0D2XPP4; -. DR GeneID; 28947871; -. DR KEGG; fox:FOXG_05932; -. DR VEuPathDB; FungiDB:FOXG_05932; -. DR Proteomes; UP000009097; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IEA:TreeGrafter. DR GO; GO:0160012; F:NAD-dependent histone decrotonylase activity; IMP:UniProtKB. DR GO; GO:0160011; F:NAD-dependent protein decrotonylase activity; IDA:UniProtKB. DR GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IEA:InterPro. DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:InterPro. DR GO; GO:1901856; P:negative regulation of cellular respiration; IMP:UniProtKB. DR CDD; cd01412; SIRT5_Af1_CobB; 1. DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR050134; NAD-dep_sirtuin_deacylases. DR InterPro; IPR003000; Sirtuin. DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf. DR InterPro; IPR027546; Sirtuin_class_III. DR InterPro; IPR026590; Ssirtuin_cat_dom. DR PANTHER; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1. DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF02146; SIR2; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR PROSITE; PS50305; SIRTUIN; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Chromosome; Cytoplasm; Metal-binding; Mitochondrion; KW NAD; Nucleus; Reference proteome; Transferase; Transit peptide; Zinc. FT TRANSIT 1..26 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 27..326 FT /note="NAD-dependent protein deacylase SIR5" FT /evidence="ECO:0000255" FT /id="PRO_0000457717" FT DOMAIN 28..324 FT /note="Deacetylase sirtuin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" FT ACT_SITE 151 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" FT BINDING 53..72 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q9NXA8" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03160" FT BINDING 159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" FT BINDING 211 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" FT BINDING 214 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236" SQ SEQUENCE 326 AA; 36006 MW; B3A5B4958E9A3397 CRC64; MRLLRPTPRL SSIFSSKTAT SNLRFFTAMA PHNDVGAFHE ALRSSKRILA LCGAGLSASS GLPTFRGAGG LWRNHDATSL ATLSAFKNDP GLVWLFYNYR RHMCLRAEPN PAHYALAALA EKNKDFLCLT QNVDNLSQQA GHPQDQLRTL HGSLFDIKCT NCDWIQRGNY DDPFCPALAP ASVDVEPGKP FPLLDASLPL DPISPDDIPK CPQCKIGFQR PGVVWFGENL DEVMMMGITN WLLEDKVDLM LVIGTSAQVY PAAGYIDKAK RKGARIAVIN PEAENEEEMY KVKPGDFAFG KDAAEYLPLL LEPVIGKLET DKKERS // ID NP24_SOLLC Reviewed; 247 AA. AC P12670; A0A3Q7HVV0; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 27-NOV-2024, entry version 134. DE RecName: Full=Osmotin-like protein NP24-I {ECO:0000303|PubMed:1859873, ECO:0000303|PubMed:22660326, ECO:0000303|Ref.1}; DE AltName: Full=Endo-beta-1,3-D-glucanase NP24-I {ECO:0000303|PubMed:10504569}; DE EC=3.2.1.6 {ECO:0000269|PubMed:10504569}; DE AltName: Full=Pathogenesis-related protein PR P23 {ECO:0000303|PubMed:1859873}; DE AltName: Full=Salt-induced protein NP24-I {ECO:0000303|Ref.3}; DE Flags: Precursor; GN Name=NP24-I {ECO:0000303|PubMed:1859873, ECO:0000303|PubMed:22660326, GN ECO:0000303|Ref.1}; OrderedLocusNames=Solyc08g080650 {ECO:0000305}; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; OC Solanum subgen. Lycopersicon. OX NCBI_TaxID=4081; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Ailsa Craig; RA Martin G.B., Jia Y.; RT "Rapid transcript accumulation of pathogenesis-related genes during an RT incompatible interaction in bacterial speck disease resistant tomato RT plants."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Heinz 1706; RX PubMed=22660326; DOI=10.1038/nature11119; RG Tomato Genome Consortium; RT "The tomato genome sequence provides insights into fleshy fruit RT evolution."; RL Nature 485:635-641(2012). RN [3] RP NUCLEOTIDE SEQUENCE OF 9-247, PARTIAL PROTEIN SEQUENCE, INDUCTION BY SALT, RP AND SUBCELLULAR LOCATION. RC STRAIN=cv. VFNT Cherry; TISSUE=Root; RX AGRICOLA=IND92000607; DOI=10.1007/BF00014946; RA King G.J., Turner V.A., Hussey C.E. Jr., Wurtele E.S., Lee S.M.; RT "Isolation and characterization of a tomato cDNA clone which codes for a RT salt-induced protein."; RL Plant Mol. Biol. 10:401-412(1988). RN [4] RP PARTIAL PROTEIN SEQUENCE, AND INDUCTION BY VIROIDS. RC STRAIN=cv. Rutgers; TISSUE=Leaf; RX PubMed=1859873; DOI=10.1007/bf00015088; RA Rodrigo I., Vera P., Frank R., Conejero V.; RT "Identification of the viroid-induced tomato pathogenesis-related (PR) RT protein P23 as the thaumatin-like tomato protein NP24 associated with RT osmotic stress."; RL Plant Mol. Biol. 16:931-934(1991). RN [5] RP PROTEIN SEQUENCE OF 22-46, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, AND VARIANTS NP24 II PHE-24 AND PHE-38. RC STRAIN=cv. Better Boy; TISSUE=Pericarp; RX PubMed=9115696; DOI=10.1016/s0031-9422(96)00667-x; RA Pressey R.; RT "Two isoforms of NP24: a thaumatin-like protein in tomato fruit."; RL Phytochemistry 44:1241-1245(1997). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=10504569; DOI=10.1046/j.1365-313x.1999.00551.x; RA Grenier J., Potvin C., Trudel J., Asselin A.; RT "Some thaumatin-like proteins hydrolyse polymeric beta-1,3-glucans."; RL Plant J. 19:473-480(1999). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-228, DISULFIDE BONDS, AND RP FUNCTION. RC TISSUE=Fruit; RX PubMed=18651170; DOI=10.1007/s00425-008-0790-5; RA Ghosh R., Chakrabarti C.; RT "Crystal structure analysis of NP24-I: a thaumatin-like protein."; RL Planta 228:883-890(2008). CC -!- FUNCTION: Has antifungal activity against P.betae and F.dahliae CC (PubMed:9115696). May be involved in disease resistance in tomatoes CC and/or have a possible role in fruit development and ripening CC (PubMed:9115696). Binds to beta-glucans and exhibits beta-1,3-D- CC glucanase activity (Probable) (PubMed:10504569). CC {ECO:0000269|PubMed:10504569, ECO:0000269|PubMed:9115696, CC ECO:0000305|PubMed:18651170}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans CC when the glucose residue whose reducing group is involved in the CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6; CC Evidence={ECO:0000269|PubMed:10504569}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.3}. Vacuole CC {ECO:0000303|PubMed:10504569}. Note=Or soluble fractions of cytoplasmic CC organelles, except mitochondria and plastids. {ECO:0000269|Ref.3}. CC -!- TISSUE SPECIFICITY: Highest levels of both isoforms found in the outer CC pericarp, with smaller amounts in the inner pericarp. CC {ECO:0000269|PubMed:9115696}. CC -!- DEVELOPMENTAL STAGE: NP24 I is low in green tomatoes and it increased CC substantially during ripening, with the largest increase occurring CC between the pink and red stages. NP24 II is relatively high in green CC tomatoes and it increased somewhat as the fruit turned pink, but not CC during further ripening. {ECO:0000269|PubMed:9115696}. CC -!- INDUCTION: By salt stress or by viroids (at protein level). CC {ECO:0000269|PubMed:1859873, ECO:0000269|Ref.3}. CC -!- ALLERGEN: Probably allergenic. {ECO:0000305|PubMed:18651170}. CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE- CC ProRule:PRU00699}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF093743; AAC64171.1; -; Genomic_DNA. DR EMBL; M21346; AAA34175.1; -; mRNA. DR PIR; S07406; S07406. DR PIR; S16264; S16264. DR RefSeq; NP_001292922.1; NM_001305993.1. DR PDB; 2I0W; X-ray; 2.50 A; A=22-228. DR PDBsum; 2I0W; -. DR AlphaFoldDB; P12670; -. DR SMR; P12670; -. DR STRING; 4081.P12670; -. DR Allergome; 9063; Sola l TLP. DR PaxDb; 4081-Solyc08g080640.1.1; -. DR GeneID; 543979; -. DR KEGG; sly:543979; -. DR eggNOG; ENOG502QV4N; Eukaryota. DR HOGENOM; CLU_043181_5_0_1; -. DR InParanoid; P12670; -. DR OMA; RTKGGCN; -. DR OrthoDB; 979137at2759; -. DR PhylomeDB; P12670; -. DR EvolutionaryTrace; P12670; -. DR Proteomes; UP000004994; Chromosome 8. DR ExpressionAtlas; P12670; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005773; C:vacuole; IDA:UniProtKB. DR GO; GO:0052736; F:beta-glucanase activity; IDA:UniProtKB. DR GO; GO:0061760; P:antifungal innate immune response; IDA:UniProtKB. DR GO; GO:0006952; P:defense response; IBA:GO_Central. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR CDD; cd09217; TLP-P; 1. DR FunFam; 2.60.110.10:FF:000003; Thaumatin I; 1. DR Gene3D; 2.60.110.10; Thaumatin; 1. DR InterPro; IPR037176; Osmotin/thaumatin-like_sf. DR InterPro; IPR001938; Thaumatin. DR InterPro; IPR017949; Thaumatin_CS. DR PANTHER; PTHR31048; OS03G0233200 PROTEIN; 1. DR PANTHER; PTHR31048:SF206; PROTEIN NP24; 1. DR Pfam; PF00314; Thaumatin; 1. DR PIRSF; PIRSF002703; Thaumatin; 1. DR PRINTS; PR00347; THAUMATIN. DR SMART; SM00205; THN; 1. DR SUPFAM; SSF49870; Osmotin, thaumatin-like protein; 1. DR PROSITE; PS00316; THAUMATIN_1; 1. DR PROSITE; PS51367; THAUMATIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Antimicrobial; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Fungicide; Glycosidase; KW Hydrolase; Pathogenesis-related protein; Plant defense; Reference proteome; KW Signal; Stress response; Vacuole. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:9115696" FT CHAIN 22..247 FT /note="Osmotin-like protein NP24-I" FT /id="PRO_0000034044" FT DISULFID 30..225 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 72..82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 87..93 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 141..213 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 146..196 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 154..164 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 168..177 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT DISULFID 178..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:18651170, ECO:0007744|PDB:2I0W" FT VARIANT 24 FT /note="I -> F (in strain: cv. Rutgers and NP24 II)" FT /evidence="ECO:0000269|PubMed:9115696" FT VARIANT 38 FT /note="S -> F (in NP24 II)" FT /evidence="ECO:0000269|PubMed:9115696" FT STRAND 23..28 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:2I0W" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 63..71 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:2I0W" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 103..109 FT /evidence="ECO:0007829|PDB:2I0W" FT TURN 110..113 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 114..120 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:2I0W" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:2I0W" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:2I0W" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:2I0W" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:2I0W" FT HELIX 189..195 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:2I0W" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:2I0W" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:2I0W" SQ SEQUENCE 247 AA; 26646 MW; 942E56E2531031B4 CRC64; MGYLTSSFVL FFLLCVTYTY AATIEVRNNC PYTVWAASTP IGGGRRLNRG QTWVINAPRG TKMARIWGRT GCNFNAAGRG TCQTGDCGGV LQCTGWGKPP NTLAEYALDQ FSNLDFWDIS LVDGFNIPMT FAPTKPSGGK CHAIHCTANI NGECPRALKV PGGCNNPCTT FGGQQYCCTQ GPCGPTELSK FFKKRCPDAY SYPQDDPTST FTCPGGSTNY RVVFCPNGVA DPNFPLEMPA STDEVAK //