ID   MPI1B_XENLA             Reviewed;         550 AA.
AC   P30309;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=M-phase inducer phosphatase 1-B;
DE            EC=3.1.3.48;
GN   Name=cdc25-1-b; Synonyms=cdc25b;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1392080; DOI=10.1091/mbc.3.8.927;
RA   Izumi T., Walker D.H., Maller J.L.;
RT   "Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase
RT   regulate its activity.";
RL   Mol. Biol. Cell 3:927-939(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   -!- INTERACTION:
CC       P30309; P18654: Rps6ka3; Xeno; NbExp=3; IntAct=EBI-15888737, EBI-397744;
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; M94262; AAA49671.1; -; mRNA.
DR   EMBL; M96858; AAA49674.1; -; mRNA.
DR   PIR; A42679; A42679.
DR   RefSeq; NP_001081918.1; NM_001088449.1.
DR   RefSeq; XP_018106285.1; XM_018250796.1.
DR   AlphaFoldDB; P30309; -.
DR   SMR; P30309; -.
DR   BioGRID; 99454; 1.
DR   DIP; DIP-176N; -.
DR   IntAct; P30309; 1.
DR   iPTMnet; P30309; -.
DR   PRIDE; P30309; -.
DR   GeneID; 398119; -.
DR   KEGG; xla:398119; -.
DR   CTD; 398119; -.
DR   Xenbase; XB-GENE-944825; cdc25c.L.
DR   OMA; FRTNCRM; -.
DR   OrthoDB; 1423329at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Hydrolase; Mitosis; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..550
FT                   /note="M-phase inducer phosphatase 1-B"
FT                   /id="PRO_0000198652"
FT   DOMAIN          401..508
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          76..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  62183 MW;  FCEC83AB66FCC5B0 CRC64;
     MAESHIMSSE APPKTNTGLN FRTNCRMVLN LLREKDCSVT FSPEQPLTPV TDLAVGFSNL
     STFSGETPKR CLDLSNLGDE TAPLPTESPD RISSGKVESP KAQFVQFDGL FTPDLGWKAK
     KCPRGNMNSV LPRLLCSTPS FKKTSGGQRS VSNKENEGEL FKSPNCKPVA LLLPQEVVDS
     QFSPTPENKV DISLDEDCEM NILGSPISAD PPCLDGAHDD IKMQNLDGFA DFFSVDEEEM
     ENPPGAVGNL SSSMAILLSG PLLNQDIEVS NVNNISLNRS RLYRSPSMPE KLDRPMLKRP
     VRPLDSETPV RVKRRRSTSS SLQPQEENFQ PQRRGTSLKK TLSLCDVDIS TVLDEDCGHR
     QLIGDFTKVY ALPTVTGRHQ DLRYITGETL AALIHGDFSS LVEKIFIIDC RYPYEYDGGH
     IKGALNLHRQ EEVTDYFLKQ PLTPTMAQKR LIIIFHCEFS SERGPKMCRF LREEDRARNE
     YPSLYYPELY LLKGGYKDFF PEYKELCEPQ SYCPMHHQDF REELLKFRTK CKTSVGDRKR
     REQIARIMKL