ID OCA6_YEAST Reviewed; 224 AA. AC Q12454; D6VS53; Q6Q559; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Putative tyrosine-protein phosphatase OCA6; DE EC=3.1.3.48; DE AltName: Full=Oxidant-induced cell-cycle arrest protein 6; GN Name=OCA6; OrderedLocusNames=YDR067C; ORFNames=D4264; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8789263; RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u; RA Brandt P., Ramlow S., Otto B., Bloecker H.; RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of RT Saccharomyces cerevisiae chromosome IV."; RL Yeast 12:85-90(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP FUNCTION. RX PubMed=14671320; DOI=10.1073/pnas.2536857100; RA Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., RA Ahlquist P.; RT "Systematic, genome-wide identification of host genes affecting replication RT of a positive-strand RNA virus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:15764-15769(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). CC -!- FUNCTION: Required for replication of Brome mosaic virus (BMV). CC {ECO:0000269|PubMed:14671320}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. 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; X84162; CAA58983.1; -; Genomic_DNA. DR EMBL; Z49209; CAA89096.1; -; Genomic_DNA. DR EMBL; Z74363; CAA98885.1; -; Genomic_DNA. DR EMBL; AY558491; AAS56817.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11913.1; -; Genomic_DNA. DR PIR; S54051; S54051. DR RefSeq; NP_010352.1; NM_001180375.1. DR AlphaFoldDB; Q12454; -. DR SMR; Q12454; -. DR BioGRID; 32122; 235. DR DIP; DIP-5466N; -. DR IntAct; Q12454; 3. DR STRING; 4932.YDR067C; -. DR iPTMnet; Q12454; -. DR MaxQB; Q12454; -. DR PaxDb; 4932-YDR067C; -. DR PeptideAtlas; Q12454; -. DR TopDownProteomics; Q12454; -. DR EnsemblFungi; YDR067C_mRNA; YDR067C; YDR067C. DR GeneID; 851639; -. DR KEGG; sce:YDR067C; -. DR AGR; SGD:S000002474; -. DR SGD; S000002474; OCA6. DR VEuPathDB; FungiDB:YDR067C; -. DR eggNOG; KOG1572; Eukaryota. DR GeneTree; ENSGT00940000176301; -. DR HOGENOM; CLU_047845_4_0_1; -. DR InParanoid; Q12454; -. DR OMA; HYPCYIH; -. DR OrthoDB; 119040at2759; -. DR BioCyc; YEAST:G3O-29674-MONOMER; -. DR BioGRID-ORCS; 851639; 0 hits in 10 CRISPR screens. DR PRO; PR:Q12454; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q12454; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd17663; PFA-DSP_Oca6; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR004861; Siw14-like. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR31126:SF14; TYROSINE-PROTEIN PHOSPHATASE OCA6-RELATED; 1. DR Pfam; PF03162; Y_phosphatase2; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase; KW Reference proteome. FT CHAIN 1..224 FT /note="Putative tyrosine-protein phosphatase OCA6" FT /id="PRO_0000244442" FT DOMAIN 8..170 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 114 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOD_RES 2 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT CONFLICT 208 FT /note="R -> G (in Ref. 2; AAS56817)" FT /evidence="ECO:0000305" SQ SEQUENCE 224 AA; 26024 MW; FFF222994B196F86 CRC64; MTLVTPLQFS TVQPNLYRGS YPREINLPFL RTLRLKYILS LTPEPLSTDP LMVKFCEENN IKTIHIKCQS ERKADKTKPK IKRKKKTVPI EYDVVVRCVK FLIDKGHYPC YMHCTNGELI ISLVVACMRK FSYWSTVSIL NEFLVYNSSI NIHERNFIEN FNSEIEVDDL DIKDKVPWIT VRYIARTATE SKDELRVDDA NASEKVARVS SVSNSLPKLK FHSM //