YPI1_ASHGO
ID YPI1_ASHGO Reviewed; 151 AA.
AC Q750F0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Type 1 phosphatases regulator YPI1;
GN Name=YPI1; OrderedLocusNames=AGR005C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016820; AAS54494.1; -; Genomic_DNA.
DR RefSeq; NP_986670.1; NM_211732.1.
DR AlphaFoldDB; Q750F0; -.
DR STRING; 33169.AAS54494; -.
DR EnsemblFungi; AAS54494; AAS54494; AGOS_AGR005C.
DR GeneID; 4622969; -.
DR KEGG; ago:AGOS_AGR005C; -.
DR eggNOG; KOG4102; Eukaryota.
DR HOGENOM; CLU_098333_3_0_1; -.
DR InParanoid; Q750F0; -.
DR OMA; HPQQNFD; -.
DR Proteomes; UP000000591; Chromosome VII.
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..151
FT /note="Type 1 phosphatases regulator YPI1"
FT /id="PRO_0000333465"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 17489 MW; 8BC02F79CF82407A CRC64;
MSSNNQESLA NRSHTVTVSE TSQILQLRAN QTEQVPKLAK KEQKSKVRWD ENVVDNEHMN
KKKTKICCIF HPQQNFDDED GGECEHASSS ASSSSSSESE NDTSMDFEAR RQARIARRRQ
KLERKRSSSP NAYEYQPDYS QYRQKYLHGD K