OCA2_YEAST
ID OCA2_YEAST Reviewed; 197 AA.
AC P53949; D6W1C2; Q6B2U7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tyrosine-protein phosphatase-like protein OCA2;
DE AltName: Full=Oxidant-induced cell-cycle arrest protein 2;
GN Name=OCA2; OrderedLocusNames=YNL056W; ORFNames=N2439, YNL2439W;
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].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [2]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
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 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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, 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).
CC -!- FUNCTION: Required for normal growth in the presence of linoleic acid
CC hydroperoxide (LoaOOH).
CC -!- INTERACTION:
CC P53949; P50946: OCA1; NbExp=5; IntAct=EBI-28725, EBI-28814;
CC P53949; P53965: SIW14; NbExp=3; IntAct=EBI-28725, EBI-28668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4530 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; U12141; AAA99655.1; -; Genomic_DNA.
DR EMBL; Z71332; CAA95929.1; -; Genomic_DNA.
DR EMBL; AY692633; AAT92652.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10488.1; -; Genomic_DNA.
DR PIR; S62984; S62984.
DR RefSeq; NP_014342.3; NM_001182895.3.
DR AlphaFoldDB; P53949; -.
DR SMR; P53949; -.
DR BioGRID; 35765; 326.
DR DIP; DIP-1989N; -.
DR IntAct; P53949; 10.
DR MINT; P53949; -.
DR STRING; 4932.YNL056W; -.
DR iPTMnet; P53949; -.
DR MaxQB; P53949; -.
DR PaxDb; P53949; -.
DR PRIDE; P53949; -.
DR EnsemblFungi; YNL056W_mRNA; YNL056W; YNL056W.
DR GeneID; 855668; -.
DR KEGG; sce:YNL056W; -.
DR SGD; S000005001; OCA2.
DR VEuPathDB; FungiDB:YNL056W; -.
DR eggNOG; KOG1572; Eukaryota.
DR GeneTree; ENSGT00940000176301; -.
DR HOGENOM; CLU_047845_3_1_1; -.
DR InParanoid; P53949; -.
DR OMA; DLEFITM; -.
DR BioCyc; YEAST:G3O-33088-MON; -.
DR PRO; PR:P53949; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53949; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..197
FT /note="Tyrosine-protein phosphatase-like protein OCA2"
FT /id="PRO_0000203451"
FT DOMAIN 10..160
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 11
FT /note="P -> S (in Ref. 5; AAT92652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 22472 MW; B5CF05FAABD9C236 CRC64;
MKYIPPLNFS PVVSTDVSLY RSGYPMPLNY SFIKHQLHLK TIIYIGDKDR PLEEYQSFLE
SEKIKYYHIF MDSSRDEGIQ ERMNQVLHLV LDVRNYPILV HSNKGKHRVG VVVGIIRKLL
QGWSTAGICQ EYGLFSGGMK DGVDLEFITM FETNLKIPRN VIPGFAKHCL YLNELEAAEG
SDDESGSESI LTAKQPI
