CPPED_RAT
ID CPPED_RAT Reviewed; 312 AA.
AC Q66H71;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC081991; AAH81991.1; -; mRNA.
DR RefSeq; NP_001013985.1; NM_001013963.1.
DR AlphaFoldDB; Q66H71; -.
DR SMR; Q66H71; -.
DR STRING; 10116.ENSRNOP00000051045; -.
DR iPTMnet; Q66H71; -.
DR PhosphoSitePlus; Q66H71; -.
DR PaxDb; Q66H71; -.
DR PRIDE; Q66H71; -.
DR Ensembl; ENSRNOT00000045047; ENSRNOP00000051045; ENSRNOG00000015118.
DR GeneID; 302890; -.
DR KEGG; rno:302890; -.
DR UCSC; RGD:1306568; rat.
DR CTD; 55313; -.
DR RGD; 1306568; Cpped1.
DR eggNOG; KOG1378; Eukaryota.
DR GeneTree; ENSGT00390000008676; -.
DR HOGENOM; CLU_077151_0_0_1; -.
DR InParanoid; Q66H71; -.
DR OMA; YENPSKC; -.
DR OrthoDB; 908967at2759; -.
DR PhylomeDB; Q66H71; -.
DR TreeFam; TF329406; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q66H71; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000015118; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q66H71; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..312
FT /note="Serine/threonine-protein phosphatase CPPED1"
FT /id="PRO_0000320559"
FT REGION 47..250
FT /note="Catalytic"
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 246
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:0007744|PubMed:22673903"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRF8"
SQ SEQUENCE 312 AA; 35261 MW; 972AA5B7A7FDDEAC CRC64;
MSAAGAADVF HRARGRTLDA FSSEKEREWT GPFYFVQGAD PQFGLMKAWS TGNCDNGGDE
WGQEIRLTEQ AVEAINKLNP KPKFFVLCGD LVHAMPGTRW RKEQTRDLQR VLKVVDQDIP
LVLVSGNHDL GNAPTAETVE EFCQTWGDDY FSFWVGGALF LVLNSQFLYD ASKCPALKQA
QDHWLDQQLS IAEQQQCQHA IVFQHIPLFL KSIDEDDDYF NLTKTVRQEL ADKFTRAGIR
AVFSGHYHRN AGGTYQNLDM VVSSAIGCQL GKDTHGLRVV VVTAEKIVHR YYSLDELSKR
GLDDDLRELL KE
