YPI2_CANAL
ID YPI2_CANAL Reviewed; 147 AA.
AC Q59ZU1; A0A1D8PFY9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Type 1 phosphatases regulator YPI2;
GN Name=YPI2; OrderedLocusNames=CAALFM_C114350WA; ORFNames=CaO19.7250;
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: Regulator of type 1 phosphatases which maintains protein
CC phosphatase activity under strict control. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW27035.1; -; Genomic_DNA.
DR RefSeq; XP_715048.1; XM_709955.1.
DR AlphaFoldDB; Q59ZU1; -.
DR STRING; 237561.Q59ZU1; -.
DR PRIDE; Q59ZU1; -.
DR GeneID; 3643281; -.
DR KEGG; cal:CAALFM_C114350WA; -.
DR CGD; CAL0000174216; orf19.7250.
DR VEuPathDB; FungiDB:C1_14350W_A; -.
DR eggNOG; KOG4102; Eukaryota.
DR HOGENOM; CLU_098333_3_0_1; -.
DR InParanoid; Q59ZU1; -.
DR OMA; YQPHYEN; -.
DR OrthoDB; 1626526at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0072542; F:protein phosphatase activator activity; IEA:EnsemblFungi.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006873; P:cellular ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:EnsemblFungi.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:EnsemblFungi.
DR InterPro; IPR011107; PPI_Ypi1.
DR PANTHER; PTHR20835; PTHR20835; 1.
DR Pfam; PF07491; PPI_Ypi1; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..147
FT /note="Type 1 phosphatases regulator YPI2"
FT /id="PRO_0000333488"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 16840 MW; 3635D0385CCFCB93 CRC64;
MSNQPSRTIV QENNVLRLRP GSEPTPSSSN QQPPQQEQQQ ETTSTKKKKK KKAPKVRWTE
GTVDNEHMNK KKTKICCIFH PQRSFDEEVE DDKHNHSCSS SDESSDSSDN EGDKDEDESR
PSNGIPKPNA YEYQPHYENR SKLPEQG
