ID   CPPED_DANRE             Reviewed;         309 AA.
AC   Q5U3W0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-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; ORFNames=zgc:101576;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2004) 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; BC085372; AAH85372.1; -; mRNA.
DR   RefSeq; NP_001007414.1; NM_001007413.1.
DR   AlphaFoldDB; Q5U3W0; -.
DR   SMR; Q5U3W0; -.
DR   STRING; 7955.ENSDARP00000045608; -.
DR   PaxDb; Q5U3W0; -.
DR   GeneID; 492772; -.
DR   KEGG; dre:492772; -.
DR   CTD; 55313; -.
DR   ZFIN; ZDB-GENE-041114-118; cpped1.
DR   eggNOG; KOG1378; Eukaryota.
DR   InParanoid; Q5U3W0; -.
DR   OrthoDB; 908967at2759; -.
DR   PhylomeDB; Q5U3W0; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   PRO; PR:Q5U3W0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..309
FT                   /note="Serine/threonine-protein phosphatase CPPED1"
FT                   /id="PRO_0000320560"
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   309 AA;  35050 MW;  B289C8780ECCCCDA CRC64;
     MAADESVFLR AKDRSYKGLT EDEQKEWSGP FYFIQAADPQ LGLMKAWRIG DCDSGGDEWD
     EEVQLTKQAV QAINKLQPKP RFIVLCGDLV HAMPGSPFRE QQIKDLKDAL RGTDPHIPLV
     FVSGNHDLGN APTPDTVEQF CHEWGDDYFS FWVGGVLCLV LNSQFFFDSS GCPELMEAHE
     VWLENRLQMA VQTPSRHVLV FQHIPLFLRT PDEEDDYFNL QRGIREHLIQ RFKRAGVKAV
     FSGHYHRNAG GCHDGLDMVV SSAVGCQLGD DTHGVRVVVV TENNIIHRYH SLDQLSERGM
     DEDLKKLLL