ID   OCA1_YARLI              Reviewed;         253 AA.
AC   Q6C4X9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
GN   Name=OCA1; OrderedLocusNames=YALI0E22880g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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).
CC   -!- FUNCTION: Putative tyrosine-protein phosphatase required for protection
CC       against superoxide stress. {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG79882.1; -; Genomic_DNA.
DR   RefSeq; XP_504283.1; XM_504283.1.
DR   AlphaFoldDB; Q6C4X9; -.
DR   SMR; Q6C4X9; -.
DR   STRING; 4952.CAG79882; -.
DR   EnsemblFungi; CAG79882; CAG79882; YALI0_E22880g.
DR   GeneID; 2912916; -.
DR   KEGG; yli:YALI0E22880g; -.
DR   VEuPathDB; FungiDB:YALI0_E22880g; -.
DR   HOGENOM; CLU_047845_2_1_1; -.
DR   InParanoid; Q6C4X9; -.
DR   OMA; NAWDPIT; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR020428; PFA-DSPs.
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   PRINTS; PR01911; PFDSPHPHTASE.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..253
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000333396"
FT   DOMAIN          93..249
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   253 AA;  28326 MW;  7E1BEB86A27B26BC CRC64;
     MHRTSIVEEL ERHQQDQKAD QEPGSVSDAS NSALQESSDP RLSTTDNTNT PEINVNDQQQ
     EQQVASGEDT DPPSPRMKTI VKPPPIKVVP PLNFGPVERN LYRSGQPEPI SFPFLEKLRL
     RTILWLAVED PSDNFLAFAD DHEIVVHHLG LVTEGTNPWD QLTESSIVAA LQIIMDRDSY
     PLLVCCGMGR HRTGTIVGCL RRLQGWNLAS VSEEYRRYAG SRGGRALIEL HIEAFDTSRI
     IVYPESAPEW CSS