ID   YPI1_CANGA              Reviewed;         146 AA.
AC   Q6FUM5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Type 1 phosphatases regulator YPI1;
GN   Name=YPI1; OrderedLocusNames=CAGL0F02255g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: 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; CR380952; CAG58993.1; -; Genomic_DNA.
DR   RefSeq; XP_446069.1; XM_446069.1.
DR   AlphaFoldDB; Q6FUM5; -.
DR   STRING; 5478.XP_446069.1; -.
DR   EnsemblFungi; CAG58993; CAG58993; CAGL0F02255g.
DR   GeneID; 2887827; -.
DR   KEGG; cgr:CAGL0F02255g; -.
DR   CGD; CAL0129177; CAGL0F02255g.
DR   VEuPathDB; FungiDB:CAGL0F02255g; -.
DR   eggNOG; KOG4102; Eukaryota.
DR   HOGENOM; CLU_098333_3_0_1; -.
DR   InParanoid; Q6FUM5; -.
DR   OMA; HPQQNFD; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR   GO; GO:0072542; F:protein phosphatase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:EnsemblFungi.
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: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..146
FT                   /note="Type 1 phosphatases regulator YPI1"
FT                   /id="PRO_0000333471"
FT   REGION          23..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   146 AA;  17038 MW;  386AC0ACFF15EF17 CRC64;
     MNQVSEGSRT VSVEEMPRVL QLRAANTNIT EGESTSQSRN VRWEEDVVDN ENMNKKKTKI
     CCIFHPAQEE EDPEQLCPSD HEHSSSSSSS SSSESDDDDK YNSEQRRQRR IERRRRRQKT
     NRPASPNAYE IQPDYSEYRK RMNANV