YPI1_KLULA
ID YPI1_KLULA Reviewed; 155 AA.
AC Q6CNA0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Type 1 phosphatases regulator YPI1;
GN Name=YPI1; OrderedLocusNames=KLLA0E14212g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99676.1; -; Genomic_DNA.
DR RefSeq; XP_454589.1; XM_454589.1.
DR AlphaFoldDB; Q6CNA0; -.
DR STRING; 28985.XP_454589.1; -.
DR EnsemblFungi; CAG99676; CAG99676; KLLA0_E14169g.
DR GeneID; 2894177; -.
DR KEGG; kla:KLLA0_E14169g; -.
DR eggNOG; KOG4102; Eukaryota.
DR HOGENOM; CLU_098333_3_0_1; -.
DR InParanoid; Q6CNA0; -.
DR OMA; HIQWAED; -.
DR Proteomes; UP000000598; Chromosome E.
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..155
FT /note="Type 1 phosphatases regulator YPI1"
FT /id="PRO_0000333476"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 155 AA; 17824 MW; 6B1871A9D4BD8956 CRC64;
MSEGPSALPE GTHTVTVTEV PQLLQLRAGQ NEKNKTKKKD TKSKVRWDEK VIDNENMNKK
KTKICCIFHP NTPLESDEEE EGECEHDHNH GHDSSSSSSS SSSDEDEGKS FDERRKARLE
RRRKKLEQKR PPSPNAYEVQ PDYSAYRDKN RKDAQ