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   27-MAR-2024, entry version 188.
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], AND TISSUE SPECIFICITY.
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. When phosphorylated, highly effective in activating G2 cells
CC       into prophase. Directly dephosphorylates CDK1 and activates its kinase
CC       activity. {ECO:0000250|UniProtKB:P30307}.
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         Evidence={ECO:0000250|UniProtKB:P30307};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P30307};
CC   -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated
CC       on Ser-128 and/or Thr-129, interacts with PLK1. Interacts with MARK3/C-
CC       TAK1. {ECO:0000250|UniProtKB:P30307}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30307}.
CC   -!- TISSUE SPECIFICITY: Spleen and thymus. {ECO:0000269|PubMed:7601309}.
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|UniProtKB:P30307}.
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; 10090-ENSMUSP00000055427; -.
DR   PeptideAtlas; P48967; -.
DR   ProteomicsDB; 291395; -.
DR   Antibodypedia; 3534; 1249 antibodies from 44 providers.
DR   DNASU; 12532; -.
DR   Ensembl; ENSMUST00000060710.9; ENSMUSP00000055427.8; ENSMUSG00000044201.11.
DR   GeneID; 12532; -.
DR   KEGG; mmu:12532; -.
DR   UCSC; uc008elf.2; mouse.
DR   AGR; MGI:88350; -.
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; CEPRSYC; -.
DR   OrthoDB; 12481at2759; -.
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 80 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 152 other cell types or tissues.
DR   ExpressionAtlas; P48967; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA: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:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd01530; Cdc25; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000751; MPI_Phosphatase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR10828:SF64; M-PHASE INDUCER PHOSPHATASE 3; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00716; MPIPHPHTASE.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   Genevisible; P48967; MM.
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|UniProtKB:P30304"
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
//