ID   MPI1A_XENLA             Reviewed;         550 AA.
AC   P30308;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=M-phase inducer phosphatase 1-A;
DE            EC=3.1.3.48;
GN   Name=cdc25-1-a; Synonyms=cdc25a;
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].
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   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; M96857; AAA49672.1; -; mRNA.
DR   AlphaFoldDB; P30308; -.
DR   SMR; P30308; -.
DR   Proteomes; UP000186698; Genome assembly.
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..550
FT                   /note="M-phase inducer phosphatase 1-A"
FT                   /id="PRO_0000198651"
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..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  62309 MW;  407B3B7AD8EC7216 CRC64;
     MAESHIMSSE APPKSNTGLN IRTNCRMILN LLREKDCSVT FSPEQPLTPV TDLAVGFSNL
     STFSGETPKR CLDLSNLGDE TAPLPTESPD RMSSGKLESP KTQFVQFDGL FTPDLAWKAK
     KCPKRNMNSV LPHLLCSTPS FKKASGGQRS LSNKENEGEL FKNPNCKPVA LLLPQEVVDS
     QLSPTPENKV DISLEEDCEM NILGSPISAD PPCLDGAHDD IKMQNLDGFA DFFSVDEEEM
     ENPPGAVGNL SCSMAILLSG PLLNQDVEIS NVNNISLNRS RLYRSPSMPE KLDRPMLKRP
     VRPLDSETPV RVKRRRSTSS PLQPEEENCQ PQRRGTSLKK TLSLCDVDIS TVLDEDCGHR
     QLIGDFSKVY ALPTVTGRHQ DLRYITGETL AALMHGDFNS LVEKFFIIDC RYPYEYDGGH
     IKSAFNLHRQ EEVTDYFLQQ PLTPLMVQKR LIIIFHCEFS SERGPKMCRF LREEDRASND
     YPSLYYPELY LLKGGYKDFF PEYKELCEPQ SYCPMHHQDF REDLLKFRTK CKTSVGDRKR
     REQVARLMKL