ID   MPIP2_XENLA             Reviewed;         599 AA.
AC   P30310;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=M-phase inducer phosphatase 2;
DE            EC=3.1.3.48;
GN   Name=cdc25-2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=1623517; DOI=10.1016/0092-8674(92)90540-s;
RA   Kumagai A., Dunphy W.G.;
RT   "Regulation of the cdc25 protein during the cell cycle in Xenopus
RT   extracts.";
RL   Cell 70:139-151(1992).
CC   -!- FUNCTION: This protein functions as a dosage-dependent inducer in
CC       mitotic control. It is a tyrosine protein phosphatase required for
CC       progression of the cell cycle. It may directly dephosphorylate
CC       p34(cdc2) and activate the p34(cdc2) kinase activity.
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   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; M94263; AAA49673.1; -; mRNA.
DR   PIR; B42679; I51405.
DR   RefSeq; NP_001165649.1; NM_001172178.1.
DR   AlphaFoldDB; P30310; -.
DR   SMR; P30310; -.
DR   MINT; P30310; -.
DR   MaxQB; P30310; -.
DR   GeneID; 100337563; -.
DR   KEGG; xla:100337563; -.
DR   CTD; 100337563; -.
DR   Xenbase; XB-GENE-6252614; cdc25c.S.
DR   OrthoDB; 1423329at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 100337563; Expressed in blastula and 15 other tissues.
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; 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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Hydrolase; Mitosis; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..599
FT                   /note="M-phase inducer phosphatase 2"
FT                   /id="PRO_0000198653"
FT   DOMAIN          450..557
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          125..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        506
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   599 AA;  67646 MW;  DB93EBD979367C4C CRC64;
     MYILLTLLTK STMESSCDNF EGLEHYYYTD AEPSSKCNKF QASGGSGVVM AESHIMSSEA
     PPKSNPGLNI RTNCRMILNL LREKDCSVTF SPEQPLTPVT DLAVGFSNLS TFSGETPKRC
     LDLSNLGDET APLPTESPDR MSSGKLESPK TQFVQFGGLF TPDLAWKAKK CPKRNMNSVL
     PHLLCSTPSF KKASGGQRSL SNKENEGELF KNPNCKPVAL LLPQEVVDSQ LSPTPENKVD
     ISLEEDCEMN ILGSPISADP PCLDGAHDDI KMQNLDGFAD FFSVDEEEME NPPGAVGNLS
     CSMAILLSGP LLNQDVEISN VNNISLNRSR LYRSPSMPEK LDRPMLKRPV RPLDSETPVR
     VKRRRSTSSP LQPEEENCQP QRRGTSLKKT LSLCDVDIST VLDEDCGHRQ LIGDFSKVYA
     LPTVTGRHQD LRYITGETLA ALMHGDFNSL VEKFFIIDCR YPYEYDGGHI KSAFNLHRQE
     EVTDYFLQQP LTPLMVQKRL IIIFHCEFSS ERGPKMCRFL REEDRASNDY PSLYYPELYL
     LKGGYKDFFP EYKELCEPQS YCPMHHQDFR EDLLKFRTKC KTSVGDRKRR EQVARLMKL