MPIP2_RAT
ID MPIP2_RAT Reviewed; 574 AA.
AC P48966;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=M-phase inducer phosphatase 2;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase Cdc25B;
GN Name=Cdc25b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NRK49F;
RX PubMed=8156993; DOI=10.1002/j.1460-2075.1994.tb06417.x;
RA Jinno S., Suto K., Nagata A., Igarashi M., Kanaoka Y., Nojima H.,
RA Okayama H.;
RT "Cdc25A is a novel phosphatase functioning early in the cell cycle.";
RL EMBO J. 13:1549-1556(1994).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tyrosine protein phosphatase which functions as a dosage-
CC dependent inducer of mitotic progression. Required for G2/M phases of
CC the cell cycle progression and abscission during cytokinesis in a ECT2-
CC dependent manner. Directly dephosphorylates CDK1 and stimulates its
CC kinase 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 -!- ACTIVITY REGULATION: Stimulated by B-type cyclins.
CC -!- SUBUNIT: Interacts with MAPK14 and 14-3-3 proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P30305}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P30305}.
CC -!- PTM: Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which
CC inhibits the activity of this protein. Phosphorylation at Ser-349 by
CC AURKA might locally participate in the control of the onset of mitosis.
CC Phosphorylation by MELK at Ser-166 promotes localization to the
CC centrosome and the spindle poles during mitosis. Phosphorylation at
CC Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3
CC proteins (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; D16237; BAA03762.1; -; mRNA.
DR RefSeq; NP_598256.1; NM_133572.1.
DR AlphaFoldDB; P48966; -.
DR SMR; P48966; -.
DR BioGRID; 251111; 2.
DR STRING; 10116.ENSRNOP00000051129; -.
DR iPTMnet; P48966; -.
DR PhosphoSitePlus; P48966; -.
DR PaxDb; P48966; -.
DR PRIDE; P48966; -.
DR GeneID; 171103; -.
DR KEGG; rno:171103; -.
DR CTD; 994; -.
DR RGD; 621500; Cdc25b.
DR eggNOG; KOG3772; Eukaryota.
DR InParanoid; P48966; -.
DR OrthoDB; 1423329at2759; -.
DR PhylomeDB; P48966; -.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:P48966; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007144; P:female meiosis I; ISO:RGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:RGD.
DR GO; GO:0001556; P:oocyte maturation; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
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:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
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; PF06617; M-inducer_phosp; 1.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..574
FT /note="M-phase inducer phosphatase 2"
FT /id="PRO_0000198646"
FT DOMAIN 425..532
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 481
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 166
FT /note="Phosphoserine; by MELK"
FT /evidence="ECO:0000250|UniProtKB:P30305"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30305"
FT MOD_RES 319
FT /note="Phosphoserine; by MAPKAPK2 and MELK"
FT /evidence="ECO:0000250|UniProtKB:P30305"
FT MOD_RES 319
FT /note="Phosphoserine; by MELK and MAPK14"
FT /evidence="ECO:0000250"
FT MOD_RES 349
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:P30305"
FT MOD_RES 370
FT /note="Phosphoserine; by BRSK1 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:P30305"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30305"
SQ SEQUENCE 574 AA; 64287 MW; 9367CE203B15FAAD CRC64;
MEVPPQKSAP GSALSTARVL GGIQRPRHLS GFGFGSDGLL GSPERAASSS PVTTLTQTMY
NLAGLGSETP KTQVGSLSFQ NRLTDLSLSR RTSECSLSSE SSESSDAGLC MDSPSPMDPQ
TAERTFEQAI QAASRVIQKM QFTIKASVFA SEAAGHSPVL QNITNSQALD SWEKDEAGYR
AASSPGEDKE NDGYIFKMPQ KLPHSSSARA LAEWASRREA FTQRPSSAPD LMCLTTDGKM
DVEEASPVAQ SSSLTPVERA CEEDDGFVDI LESDLKDDDM VPAGMENLIS APLVKKLDKE
EEQDLIMFSK CQRLFRSPSM PCSVIRPILK RLERPHDRDV PVLSKRRKSG TPLEEQQLEE
PKARVFRSKS LCHEIESILD SDHRGLIGDY SKAFLLQTVD GKHQDLKYIS PETMVALLTG
KFSNIVEKFV IVDCRYPYEY EGGHIKNAVN LPLEPDAETF LLKHPITPCN LDKRIILIFH
CEFSSERGPR MCRFIRERDR AANDYPSLYY PEMYILKGGY KEFFPQHPNF CEPQDYRPMN
HAAFRDELRN FRLKTRSWAG ERSTTQLCSR LQDQ
