ID   MPIP3_XENLA             Reviewed;         572 AA.
AC   P30311;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=M-phase inducer phosphatase 3;
DE            EC=3.1.3.48;
GN   Name=cdc25-3;
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=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; M94264; AAA49675.1; -; mRNA.
DR   PIR; C42679; C42679.
DR   RefSeq; NP_001081256.1; NM_001087787.1.
DR   PDB; 1I8G; NMR; -; A=63-72.
DR   PDBsum; 1I8G; -.
DR   AlphaFoldDB; P30311; -.
DR   SMR; P30311; -.
DR   BioGRID; 99076; 2.
DR   AGR; Xenbase:XB-GENE-6252614; -.
DR   OrthoDB; 5483572at2759; -.
DR   EvolutionaryTrace; P30311; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 397737; Expressed in muscle tissue and 19 other cell types or 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   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   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Hydrolase; Mitosis;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..572
FT                   /note="M-phase inducer phosphatase 3"
FT                   /id="PRO_0000198654"
FT   DOMAIN          420..527
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          95..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        476
FT                   /evidence="ECO:0000250"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1I8G"
SQ   SEQUENCE   572 AA;  64413 MW;  B268EA4BAA3971AC CRC64;
     MIKERVTPPF QASGGSGVVM AESHIISSEA PPKSNPGLNI RTNCRMILNL LREKDCSVTF
     SPEQPLTPVT DLAVGFSNLS TFSGETPKRC LDLSNLGDET APLPTESPDR MSSGKLESPK
     TQFVQFDGLF TPDLAWKAKK CPKRNMNSVL PHLLCSTPSF KKASGGQRSL SNKENEGELF
     KNPNCKPVAL LLPQEVVDSQ LSPTPENKVD ISLDEDCEMN ILGSPISADP PCLDGAHDDI
     KMQNLDGFAD FFSVDEEEME NPPGAVGNLS CSMAILLSGP LLNQDVEISN VNNISLNRSR
     LYRSPSMPEK LDRPMLKRPV RPLNSETPVR VKRRRSTSSP LQPEEENCQP QRRGTSLKKT
     LSLCDVDISS VLDEDCGHRQ LIGDFSKVYA LPTVTGRHQD LRYITGETLA ALMHGDFNSL
     VEKFFIIDCR YPYEYDGGHI KSAFNLHRQD EVTDYFLQQP LTPLMAQKRL IIIFHCEFSS
     ERGPKMCRSL REEDRASNDY PSLYYPELYL LKGGYKDFFP EYKELCEPQS YCPMHHQDFR
     EDLLKFRTKC KTSVGDRKRR EPEFRLTGQR LG
//