ID   OCA1_CANGA              Reviewed;         217 AA.
AC   Q6FSZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
GN   Name=OCA1; OrderedLocusNames=CAGL0G06578g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
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; CR380953; CAG59573.1; -; Genomic_DNA.
DR   RefSeq; XP_446646.1; XM_446646.1.
DR   AlphaFoldDB; Q6FSZ8; -.
DR   SMR; Q6FSZ8; -.
DR   STRING; 284593.Q6FSZ8; -.
DR   EnsemblFungi; CAGL0G06578g-T; CAGL0G06578g-T-p1; CAGL0G06578g.
DR   GeneID; 2888220; -.
DR   KEGG; cgr:CAGL0G06578g; -.
DR   CGD; CAL0129231; CAGL0G06578g.
DR   VEuPathDB; FungiDB:CAGL0G06578g; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_2_2_1; -.
DR   InParanoid; Q6FSZ8; -.
DR   Proteomes; UP000002428; Chromosome G.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   CDD; cd14531; PFA-DSP_Oca1; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..217
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000333390"
FT   DOMAIN          51..209
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   217 AA;  24687 MW;  5BC2C66B82CEEDEC CRC64;
     MDSPTLEDRE NSIEDCDDDD DNIYINEETE EGHEKVLVTH APQERIVPPL NFCPVERYLY
     RSGQPSPVNF PFLLNLNLKT IVWLANEEPQ DSLLEFCDTH KINLQFAAIN PDAGEDDNPW
     DGLTEHSIIN VLQTIVTKEN YPLLVCCGMG RHRTGTVIGC LRRIMGWNLA SVSEEYRRFT
     GSRGGRILVE LLIEAFDTAL VEIDKKNAPD WLLTSLE
//