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OCA6_YEAST
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   03-AUG-2022, entry version 155.
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}.
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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; 231.
DR   DIP; DIP-5466N; -.
DR   IntAct; Q12454; 3.
DR   STRING; 4932.YDR067C; -.
DR   iPTMnet; Q12454; -.
DR   MaxQB; Q12454; -.
DR   PaxDb; Q12454; -.
DR   PRIDE; Q12454; -.
DR   TopDownProteomics; Q12454; -.
DR   EnsemblFungi; YDR067C_mRNA; YDR067C; YDR067C.
DR   GeneID; 851639; -.
DR   KEGG; sce:YDR067C; -.
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   BioCyc; YEAST:G3O-29674-MON; -.
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   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR004861; Siw14-like.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF03162; Y_phosphatase2; 1.
DR   SUPFAM; SSF52799; SSF52799; 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
 
 
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