ID   CPPED_PONAB             Reviewed;         314 AA.
AC   Q5RCR9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Serine/threonine-protein phosphatase CPPED1;
DE            EC=3.1.3.16;
DE   AltName: Full=Calcineurin-like phosphoesterase domain-containing protein 1;
GN   Name=CPPED1; Synonyms=CSTP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein phosphatase that dephosphorylates AKT family kinase
CC       specifically at 'Ser-473', blocking cell cycle progression and
CC       promoting cell apoptosis. May play an inhibitory role in glucose uptake
CC       by adipocytes (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CPPED1
CC       family. {ECO:0000305}.
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DR   EMBL; CR858200; CAH90438.1; -; mRNA.
DR   RefSeq; NP_001125220.1; NM_001131748.1.
DR   AlphaFoldDB; Q5RCR9; -.
DR   SMR; Q5RCR9; -.
DR   STRING; 9601.ENSPPYP00000008049; -.
DR   Ensembl; ENSPPYT00000059620; ENSPPYP00000033218; ENSPPYG00000036531.
DR   GeneID; 100172113; -.
DR   KEGG; pon:100172113; -.
DR   CTD; 55313; -.
DR   eggNOG; KOG1378; Eukaryota.
DR   GeneTree; ENSGT00390000008676; -.
DR   HOGENOM; CLU_077151_0_0_1; -.
DR   InParanoid; Q5RCR9; -.
DR   OMA; YENPSKC; -.
DR   OrthoDB; 908967at2759; -.
DR   TreeFam; TF329406; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07395; MPP_CSTP1; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041867; MPP_CSTP1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..314
FT                   /note="Serine/threonine-protein phosphatase CPPED1"
FT                   /id="PRO_0000320558"
FT   REGION          47..250
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRF8"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRF8"
SQ   SEQUENCE   314 AA;  35610 MW;  B5CEA4AA7869F383 CRC64;
     MSAAEAGGVF HRARGRTLDA FPAEKESEWK GPFYFILGAD PQFGLMKAWS TGDCDNGGDE
     WEQEIRLTEQ AVQAINKLNP KPKFFVLCGD LIHAMPGKPW RTEQTEDLKR VLRTVDRAIP
     LVLVSGNHDI GNAPTAETVD EFCRTWGDDY FSFWVGGVLF LVLNSQFYEN PSKCPSLKQA
     QDQWLDEQLS IARQRHCQHA IIFQHIPLFL ESIDEDDDYY FNLSKSTRKK LADKFIHAGV
     KVVFSGHYHR NAGGTYQNLD MVVSSAIGCQ LGRDPHGLRV VVVTAEKIVH RYYSLDELSE
     KGIEDDLMDL IKKK