CPPED_BOVIN
ID CPPED_BOVIN Reviewed; 313 AA.
AC Q58DC0; A3KMY3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58DC0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58DC0-2; Sequence=VSP_031657;
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CPPED1
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT021677; AAX46524.1; -; mRNA.
DR EMBL; BC133400; AAI33401.1; -; mRNA.
DR RefSeq; NP_001026941.2; NM_001031771.2.
DR AlphaFoldDB; Q58DC0; -.
DR SMR; Q58DC0; -.
DR STRING; 9913.ENSBTAP00000007071; -.
DR PaxDb; Q58DC0; -.
DR PRIDE; Q58DC0; -.
DR GeneID; 537938; -.
DR KEGG; bta:537938; -.
DR CTD; 55313; -.
DR eggNOG; KOG1378; Eukaryota.
DR HOGENOM; CLU_077151_0_0_1; -.
DR InParanoid; Q58DC0; -.
DR OrthoDB; 908967at2759; -.
DR TreeFam; TF329406; -.
DR Proteomes; UP000009136; 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 Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..313
FT /note="Serine/threonine-protein phosphatase CPPED1"
FT /id="PRO_0000320555"
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 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:0000250|UniProtKB:Q9BRF8"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRF8"
FT VAR_SEQ 239..312
FT /note="VKAVFSGHYHRNAGGTYRNLDMVVSSAIGCQLGTDTHGLRVVVVTAEKITHR
FT YYSLDELSEKGIEDDLMDLLKE -> TCVHAHTHKMKMPYHQRSPVPVAPCASPARTAH
FT FSSWEPLRFSFPEKWRILSSFPALSVTWQDSSCDNCYVSFWP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_031657"
FT CONFLICT 191
FT /note="I -> T (in Ref. 2; AAI33401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35410 MW; 0C3A8EF5F4FEDF54 CRC64;
MSTAEAGGVF HRARGRTLDA FSSEKEREWK GPFYFIQGAD PQFGLMKAWA TGDCDNGGDE
WEQEIRLAEQ AVQAINKLNP KPKFFVLCGD LVHAMPGRPW RKEQTEDLQR VLRTVDSDIP
LVLVSGNHDV GNVPTPETIA EFQRTWGDDY FSFWVGGVLF LVLNSQFLYD ASRCPALKQE
HDHWLDQQLR IAGQRACRHA VVFQHIPLFL QSIGEDDDYF NLTKSVRKEM ADKFVEAGVK
AVFSGHYHRN AGGTYRNLDM VVSSAIGCQL GTDTHGLRVV VVTAEKITHR YYSLDELSEK
GIEDDLMDLL KEN
