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   27-MAR-2024, entry version 104.
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: Tyrosine protein phosphatase which functions as a dosage-
CC       dependent inducer of mitotic progression. Directly dephosphorylates
CC       CDK1 and stimulates its kinase activity.
CC       {ECO:0000250|UniProtKB:P30304}.
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         Evidence={ECO:0000250|UniProtKB:P30304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC         Evidence={ECO:0000250|UniProtKB:P30304};
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   AGR; Xenbase:XB-GENE-6252614; -.
DR   Xenbase; XB-GENE-6252614; cdc25c.S.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; 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:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   CDD; cd01530; Cdc25; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000751; MPI_Phosphatase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR10828:SF64; M-PHASE INDUCER PHOSPHATASE 3; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   Pfam; PF06617; M-inducer_phosp; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00716; MPIPHPHTASE.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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|UniProtKB:P30304"
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
//