ID   OCA1_YEAST              Reviewed;         238 AA.
AC   P50946; D6W180; Q45U02;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 169.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
DE   AltName: Full=Oxidant-induced cell-cycle arrest protein 1;
GN   Name=OCA1; OrderedLocusNames=YNL099C; ORFNames=N2194;
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], AND VARIANT CYS-66.
RC   STRAIN=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8701612;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4%3c403::aid-yea923%3e3.0.co;2-h;
RA   Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT   "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT   chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT   frames.";
RL   Yeast 12:403-409(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   DOMAIN.
RX   PubMed=9757831; DOI=10.1016/s0968-0004(98)01241-9;
RA   Wishart M.J., Dixon J.E.;
RT   "Gathering STYX: phosphatase-like form predicts functions for unique
RT   protein-interaction domains.";
RL   Trends Biochem. Sci. 23:301-306(1998).
RN   [6]
RP   FUNCTION.
RX   PubMed=11408586; DOI=10.1091/mbc.12.6.1801;
RA   Alic N., Higgins V.J., Dawes I.W.;
RT   "Identification of a Saccharomyces cerevisiae gene that is required for G1
RT   arrest in response to the lipid oxidation product linoleic acid
RT   hydroperoxide.";
RL   Mol. Biol. Cell 12:1801-1810(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12912987; DOI=10.1074/jbc.m307760200;
RA   Alic N., Higgins V.J., Pichova A., Breitenbach M., Dawes I.W.;
RT   "Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p
RT   in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 278:41849-41855(2003).
RN   [8]
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   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   INTERACTION WITH OCA2; OCA4; OCA5 AND SIW14.
RX   PubMed=16429126; DOI=10.1038/nature04532;
RA   Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
RA   Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
RA   Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.-M.,
RA   Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A.,
RA   Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B.,
RA   Bork P., Russell R.B., Superti-Furga G.;
RT   "Proteome survey reveals modularity of the yeast cell machinery.";
RL   Nature 440:631-636(2006).
RN   [11]
RP   FUNCTION.
RX   PubMed=18205808; DOI=10.1111/j.1567-1364.2007.00349.x;
RA   Fong C.S., Temple M.D., Alic N., Chiu J., Durchdewald M., Thorpe G.W.,
RA   Higgins V.J., Dawes I.W.;
RT   "Oxidant-induced cell-cycle delay in Saccharomyces cerevisiae: the
RT   involvement of the SWI6 transcription factor.";
RL   FEMS Yeast Res. 8:386-399(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Putative tyrosine-protein phosphatase required for protection
CC       against superoxide stress. Involved in cell-cycle delay in response to
CC       linoleic acid hydroperoxide (LoaOOH). {ECO:0000269|PubMed:11408586,
CC       ECO:0000269|PubMed:12912987, ECO:0000269|PubMed:18205808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; EC=3.1.3.48;
CC   -!- INTERACTION:
CC       P50946; P53949: OCA2; NbExp=5; IntAct=EBI-28814, EBI-28725;
CC       P50946; P25366: OCA4; NbExp=3; IntAct=EBI-28814, EBI-22021;
CC       P50946; P53965: SIW14; NbExp=5; IntAct=EBI-28814, EBI-28668;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ115393; AAZ22508.1; -; Genomic_DNA.
DR   EMBL; Z50161; CAA90527.1; -; Genomic_DNA.
DR   EMBL; Z71375; CAA95975.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10446.1; -; Genomic_DNA.
DR   PIR; S58253; S58253.
DR   RefSeq; NP_014300.3; NM_001182937.3.
DR   AlphaFoldDB; P50946; -.
DR   SMR; P50946; -.
DR   BioGRID; 35724; 274.
DR   DIP; DIP-1991N; -.
DR   FunCoup; P50946; 61.
DR   IntAct; P50946; 6.
DR   MINT; P50946; -.
DR   STRING; 4932.YNL099C; -.
DR   iPTMnet; P50946; -.
DR   PaxDb; 4932-YNL099C; -.
DR   PeptideAtlas; P50946; -.
DR   EnsemblFungi; YNL099C_mRNA; YNL099C; YNL099C.
DR   GeneID; 855624; -.
DR   KEGG; sce:YNL099C; -.
DR   AGR; SGD:S000005043; -.
DR   SGD; S000005043; OCA1.
DR   VEuPathDB; FungiDB:YNL099C; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_2_0_1; -.
DR   InParanoid; P50946; -.
DR   OMA; PWNPISE; -.
DR   OrthoDB; 6375174at2759; -.
DR   BioCyc; YEAST:G3O-33127-MONOMER; -.
DR   BioGRID-ORCS; 855624; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P50946; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P50946; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0016791; F:phosphatase activity; IDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   CDD; cd14531; PFA-DSP_Oca1; 1.
DR   FunFam; 3.90.190.10:FF:000035; Tyrosine phosphatase, putative; 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:SF8; TYROSINE-PROTEIN PHOSPHATASE OCA1-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   Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..238
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000203439"
FT   DOMAIN          72..230
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   VARIANT         66
FT                   /note="R -> C (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
SQ   SEQUENCE   238 AA;  27205 MW;  114DD87CBA2FAEBF CRC64;
     MTSKVGEYED VPEDESRLTE ENVSVPEEEV EDEDEEEDDD DDHIYINEET ESGREKVLVS
     HAPQERIVPP LNFCPVERYL YRSGQPSPVN FPFLLNLKLK TIIWLSNEEP QDTLLEFCDT
     HRINLQFAAI NPDAGEDDNP WDGLTEHSII NVLQTIVTQE NYPLLVCCGM GRHRTGTVIG
     CLRRIMGWNL ASVSEEYRRF TGSRGGRILV ELLIEAFDTN LVKIDKNKAP SWLLTALE
//