ID OCA1_CANAL Reviewed; 269 AA.
AC Q59XY9; A0A1D8PIN0; Q59XU3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
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=CAALFM_C210190CA;
GN ORFNames=CaO19.1762, CaO19.9331;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017624; AOW27996.1; -; Genomic_DNA.
DR RefSeq; XP_714407.2; XM_709314.2.
DR AlphaFoldDB; Q59XY9; -.
DR SMR; Q59XY9; -.
DR BioGRID; 1227023; 1.
DR STRING; 237561.Q59XY9; -.
DR EnsemblFungi; C2_10190C_A-T; C2_10190C_A-T-p1; C2_10190C_A.
DR GeneID; 3643929; -.
DR KEGG; cal:CAALFM_C210190CA; -.
DR CGD; CAL0000196452; OCA1.
DR VEuPathDB; FungiDB:C2_10190C_A; -.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_2_2_1; -.
DR InParanoid; Q59XY9; -.
DR OrthoDB; 131574at2759; -.
DR PRO; PR:Q59XY9; -.
DR Proteomes; UP000000559; Chromosome 2.
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; TAS:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
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; 2.
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..269
FT /note="Putative tyrosine-protein phosphatase OCA1"
FT /id="PRO_0000333389"
FT DOMAIN 45..261
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 269 AA; 30723 MW; 35F69F99C9B080FE CRC64;
MASITSNSQI LINNDSSTNK APTTNERQLR RINHPPNLRI VPPLNFCPVE NQLYRSGQPS
IINQSFLNQL NLKTIIWLSS EEPTDEFLEY CNDSSINIEY LGMINEFNSE PATATTTDKQ
SQSQSQSQSE EQKSQSQSQS QENQHHQFEQ SDNNLLQDPS HLISSTIAKI NNNNPWDSLN
ENTIKHALDL IVDKTNYPIL ICCGMGRHRT GTVIGCLRRL QHWNLNSVSE EYRRFTGSRG
GRILVELLIE SFNIDLVNIN WELAPDWLK
//
