MPIP3_MESAU
ID MPIP3_MESAU Reviewed; 420 AA.
AC P48968;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1337289; DOI=10.1091/mbc.3.12.1373;
RA Seki T., Yamashita K., Nishitani H., Takagi T., Russell P., Nishimoto T.;
RT "Chromosome condensation caused by loss of RCC1 function requires the
RT cdc25C protein that is located in the cytoplasm.";
RL Mol. Biol. Cell 3:1373-1388(1992).
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). {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-126 and/or Thr-127, interacts with PLK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by PLK4. Phosphorylated by PLK1, leading to
CC activate the phosphatase activity. Phosphorylation by PLK3 at Ser-219
CC promotes nuclear translocation. Ser-226 is a minor phosphorylation site
CC (By similarity). Phosphorylation by CDK1 occurs at G2 and G2-M
CC 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; D10878; BAA01646.1; -; mRNA.
DR RefSeq; XP_012979162.1; XM_013123708.1.
DR AlphaFoldDB; P48968; -.
DR SMR; P48968; -.
DR STRING; 10036.XP_005088641.1; -.
DR GeneID; 101828859; -.
DR CTD; 995; -.
DR eggNOG; KOG3772; Eukaryota.
DR OrthoDB; 1423329at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
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..420
FT /note="M-phase inducer phosphatase 3"
FT /id="PRO_0000198649"
FT DOMAIN 266..373
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 322
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 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 64
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 198
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 219
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 226
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:P30307"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30307"
SQ SEQUENCE 420 AA; 47327 MW; D7564B0AF2124783 CRC64;
MSTGPFPSSR REESSVSAPS FRFSQRKMLN LLLERNTSFT QDFPRSPGDK LLDSTNLSIL
SGGTPKRCLD LSNLSNGEMS ASPLITSADF DDTGSLDSSG PQDVQLTEKN HHQDPMKGIP
VQLLCSTPNA LDHSHRKKDA VRGLSANKEN INTNLKTLQW ESPRIPRFQN TPGDPLASPL
PLLGNGVSMD TEVRSLGSPI TAVPKLSKNL NLEDQEEISE EPMEFSLEDH DTKECVLPTV
SGKHQDLKYI TPDTVAALLS GKFQGLIEKF YIIDCRYPYE YLGGHILGAI NLCSQKELHE
FFLKKPIVPL DIQKRVIIVF LCEFSSERGP RMCRSLRRKD RALNQYPALY YPELYILKGG
YRDFFPEYTE LCEPQGYCPM HHQDHQAELL MWRNQSKAQE GERQLSEQIA LLMKKGVSLP
