MPIP3_MOUSE
ID MPIP3_MOUSE Reviewed; 447 AA.
AC P48967; Q99KG6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=M-phase inducer phosphatase 3;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25C;
GN Name=Cdc25c; Synonyms=Cdc25m1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7601309; DOI=10.1006/dbio.1995.1207;
RA Wu S., Wolgemuth D.J.;
RT "The distinct and developmentally regulated patterns of expression of
RT members of the mouse Cdc25 gene family suggest differential functions
RT during gametogenesis.";
RL Dev. Biol. 170:195-206(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8276463; DOI=10.1007/bf00188612;
RA Nargi J.L., Woodford-Thomas T.A.;
RT "Cloning and characterization of a cdc25 phosphatase from mouse
RT lymphocytes.";
RL Immunogenetics 39:99-108(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. Directly dephosphorylates CDK1 and activates its kinase
CC activity. When phosphorylated, highly effective in activating G2 cells
CC into prophase (By similarity). May be involved in regulating the
CC proliferation of T-lymphocytes following cytokine stimulation.
CC {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 at Ser-128 and/or Thr-129, interacts with PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Spleen and thymus.
CC -!- PTM: Phosphorylated by PLK4. Phosphorylated by PLK1, leading to
CC activate the phosphatase activity (By similarity). Phosphorylated by
CC CHEK1 and MAPKAPK2. This phosphorylation creates a binding site for 14-
CC 3-3 protein and inhibits the phosphatase activity. Phosphorylation by
CC PLK3 at Ser-213 promotes nuclear translocation. Ser-220 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; U15562; AAA74912.1; -; mRNA.
DR EMBL; L16926; AAA37409.1; -; mRNA.
DR EMBL; BC004669; AAH04669.1; -; mRNA.
DR CCDS; CCDS37759.1; -.
DR PIR; I49126; I49126.
DR RefSeq; NP_033990.2; NM_009860.3.
DR AlphaFoldDB; P48967; -.
DR SMR; P48967; -.
DR BioGRID; 198623; 2.
DR IntAct; P48967; 1.
DR STRING; 10090.ENSMUSP00000055427; -.
DR iPTMnet; P48967; -.
DR PhosphoSitePlus; P48967; -.
DR PaxDb; P48967; -.
DR PeptideAtlas; P48967; -.
DR PRIDE; P48967; -.
DR ProteomicsDB; 291395; -.
DR Antibodypedia; 3534; 1127 antibodies from 44 providers.
DR DNASU; 12532; -.
DR Ensembl; ENSMUST00000060710; ENSMUSP00000055427; ENSMUSG00000044201.
DR GeneID; 12532; -.
DR KEGG; mmu:12532; -.
DR UCSC; uc008elf.2; mouse.
DR CTD; 995; -.
DR MGI; MGI:88350; Cdc25c.
DR VEuPathDB; HostDB:ENSMUSG00000044201; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000161460; -.
DR HOGENOM; CLU_014464_4_0_1; -.
DR InParanoid; P48967; -.
DR OMA; MHHQDHQ; -.
DR OrthoDB; 1423329at2759; -.
DR PhylomeDB; P48967; -.
DR TreeFam; TF101056; -.
DR Reactome; R-MMU-156711; Polo-like kinase mediated events.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR BioGRID-ORCS; 12532; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Cdc25c; mouse.
DR PRO; PR:P48967; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P48967; protein.
DR Bgee; ENSMUSG00000044201; Expressed in floor plate of midbrain and 149 other tissues.
DR ExpressionAtlas; P48967; baseline and differential.
DR Genevisible; P48967; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
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 GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
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..447
FT /note="M-phase inducer phosphatase 3"
FT /id="PRO_0000198648"
FT DOMAIN 294..401
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
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 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 66
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 192
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 213
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 220
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT CONFLICT 153..165
FT /note="INTSLKALEWEAP -> AAFLLLSLQLNDAGPSCADKHQFKGIGMGGT (in
FT Ref. 2; AAA37409)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="V -> L (in Ref. 1; AAA74912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50046 MW; 513E51BAB3D1A39E CRC64;
MSTGPIPPAS EEGSFVSAPS FRSKQRKILH LLLERNTSFT IRSDFPESPK DKLHDSANLS
ILSGGTPKCC LDLSNLSSGE MSASPLTTSA DLEDNGSLDS SGPLDRQLTG KDFHQDLMKG
IPVQLLCSTP NAMNHGHRKK IAKRSTSAHK ENINTSLKAL EWEAPRTPRF RKMPGGPLTS
PLCELEMKHL GSPITTVPKL SQNVKLEDQE RISEDPMECS LGDQDAKGLS LRKMVPLCDM
NAIQMEEEES GSELLIGDFS KVCVLPTVPG KHPDLKYISP DTVAALLSGK FQSVIERFYI
IDCRYPYEYL GGHILGALNL HSQKELHEFF LRKPVVPLDI QKRVIIVFLC EFSSERGPRM
CRSLREKDRA LNQYPALYYP ELYILKGGYR DFFPEYMELC DPQSYCPMLH QDHQAELLSW
RSQSKAQEGE RQLQGQIALL VKGASPQ
