MPIP3_BOVIN
ID MPIP3_BOVIN Reviewed; 477 AA.
AC A5D7P0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=M-phase inducer phosphatase 3;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25C;
GN Name=CDC25C;
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].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. When phosphorylated, highly effective in activating G2 cells
CC into prophase. Directly dephosphorylates CDK1 and activate its kinase
CC activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated
CC on Ser-130 and/or Thr-131, interacts with PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly in G2 phase.
CC -!- PTM: Phosphorylated by CHEK1 and MAPK14 at Ser-220. This
CC phosphorylation creates a binding site for 14-3-3 protein and inhibits
CC the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1,
CC leading to activate the phosphatase activity. Phosphorylation by PLK3
CC at Ser-192 promotes nuclear translocation. Ser-199 is a minor
CC phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at
CC G2 and G2-M transition and leads to increased activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; BC140630; AAI40631.1; -; mRNA.
DR RefSeq; NP_001091465.1; NM_001097996.2.
DR AlphaFoldDB; A5D7P0; -.
DR SMR; A5D7P0; -.
DR STRING; 9913.ENSBTAP00000006968; -.
DR PaxDb; A5D7P0; -.
DR PRIDE; A5D7P0; -.
DR Ensembl; ENSBTAT00000006968; ENSBTAP00000006968; ENSBTAG00000005293.
DR GeneID; 507731; -.
DR KEGG; bta:507731; -.
DR CTD; 995; -.
DR VEuPathDB; HostDB:ENSBTAG00000005293; -.
DR VGNC; VGNC:27064; CDC25C.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000161460; -.
DR HOGENOM; CLU_014464_4_0_1; -.
DR InParanoid; A5D7P0; -.
DR OMA; MHHQDHQ; -.
DR OrthoDB; 1423329at2759; -.
DR TreeFam; TF101056; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000005293; Expressed in oocyte and 68 other tissues.
DR ExpressionAtlas; A5D7P0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Hydrolase; Mitosis; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT CHAIN 2..477
FT /note="M-phase inducer phosphatase 3"
FT /id="PRO_0000365162"
FT DOMAIN 325..432
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 48
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 68
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 123
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 169
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 192
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 199
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 218
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 220
FT /note="Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
SQ SEQUENCE 477 AA; 53794 MW; BC73134038B99915 CRC64;
MSAEFFSSKR EEGSLASGPS FRSNQRKILN LLLERDASFS ISSDLPTTPV EKKLFGDSAN
LSILSGGTPK RCLDLSNLSS GEMSATQLTA SADLDETGHL ESTGPEQVRL AGMNYRQHLI
KCSPAQLFCS TPNALEHGRR KKDAICGSSA NKENDNGNLV ENEMKHLGSP ITTVSKLHKN
PELAEDQAEE ISDELMEFSL EDQEKAKPPL NWSSLYRSSS LPDSLNSPSL KQVVKFKDST
IPDKLKKKYC SNQKELGKGL GLKKMVSLCD INMTQMLEED SNQGPLIGDF SKVCALPTVS
GKHQDLKYVN PETVAALLSG EFQGLIEKFY IIDCRYPYEY LGGHIQGALN LHSQEELYNF
FLKKPIVPWD NQKRIVIVFH CEFSSERGPR MCRSLREEDR TLNQYPALYY PELYILKGGY
RDFFPEYMEL CEPQSYCPMH HQDHKAELLR CRNQSKAWEG ERQLQEQIAL LVKDVSP
