ID   CPPED_XENTR             Reviewed;         311 AA.
AC   Q28FE0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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; ORFNames=TEgg046k19.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein phosphatase involved in the dephosphorylation of AKT
CC       kinase family. {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; CR762015; CAJ81971.1; -; mRNA.
DR   RefSeq; NP_001016142.1; NM_001016142.2.
DR   AlphaFoldDB; Q28FE0; -.
DR   SMR; Q28FE0; -.
DR   STRING; 8364.ENSXETP00000019617; -.
DR   PaxDb; Q28FE0; -.
DR   GeneID; 548896; -.
DR   KEGG; xtr:548896; -.
DR   CTD; 55313; -.
DR   Xenbase; XB-GENE-945403; cpped1.
DR   eggNOG; KOG1378; Eukaryota.
DR   HOGENOM; CLU_077151_0_0_1; -.
DR   InParanoid; Q28FE0; -.
DR   OMA; NEESWEG; -.
DR   OrthoDB; 908967at2759; -.
DR   PhylomeDB; Q28FE0; -.
DR   TreeFam; TF329406; -.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000008957; Expressed in skeletal muscle tissue and 12 other tissues.
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; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Serine/threonine-protein phosphatase CPPED1"
FT                   /id="PRO_0000320561"
FT   REGION          47..250
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  35579 MW;  1E0EF59441DBBFFB CRC64;
     MSEAREVFLR ARGRSFTSFN KDAESQWKGP FYFIQGADPQ FGLMKSWEIG DCDYGGDEWE
     QEIRLTEEAV KAINKLSPKP KFFVLCGDLV HSMPGIEWKE EQEKDLKNVL QKTHQEIPLV
     FVSGNHDIGN APTPETIQAY CDSWGDDYFS FWVGGVFFLV LNSQLFFDAS KCPELKDNHD
     RWLAAQLAIA EERKCKHAIV FQHIPLFLQK ADEDNDYFNI EKSLRQEILQ MFLKAGIKAV
     FSGHYHRNAG AKYNDLDMVV TSAIGCQLGK DAHGLRVVVV TEDKIVHKYY SLNELNTNGL
     DQELVDLLKT K