ID   YPI1_YEAS7              Reviewed;         155 AA.
AC   A7A241;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Type 1 phosphatases regulator YPI1;
GN   Name=YPI1; ORFNames=SCY_1751;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Regulator of type 1 phosphatases which maintains protein
CC       phosphatase activity under strict control. Regulates the nuclear
CC       localization of type 1 phosphatase GLC7 and SDS22, and is involved in
CC       the regulation of mRNA 3'-end processing. May also regulate the
CC       activity of type 1 phosphatase PPZ1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GLC7, PPZ1 and SDS22. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000176; EDN59152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7A241; -.
DR   PRIDE; A7A241; -.
DR   EnsemblFungi; EDN59152; EDN59152; SCY_1751.
DR   HOGENOM; CLU_098333_3_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PTHR20835; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   3: Inferred from homology;
KW   Acetylation; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P43587"
FT   CHAIN           2..155
FT                   /note="Type 1 phosphatases regulator YPI1"
FT                   /id="PRO_0000333484"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           51..53
FT                   /note="GLC7-binding"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43587"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43587"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43587"
SQ   SEQUENCE   155 AA;  18187 MW;  E191184DCD5EF8A1 CRC64;
     MSGNQMAMGS EQQQTVGSRT VSVEEVPAVL QLRATQDPPR SQEAMPTRHN VRWEENVIDN
     ENMNKKKTKI CCIFHPQNED EEECNHHSDD DGSSSSGSSS SESENEKDLD FNERRQRRLE
     RRHRKLEKKR SYSPNAYEIQ PDYSEYRRKQ QEKKD