ID   MPIP1_CAEEL             Reviewed;         604 AA.
AC   O44552;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=M-phase inducer phosphatase cdc-25.1;
DE            EC=3.1.3.48;
DE   AltName: Full=Cell division cycle-related protein 25.1;
GN   Name=cdc-25.1; ORFNames=K06A5.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=9651482; DOI=10.1016/s0378-1119(98)00228-5;
RA   Ashcroft N.R., Kosinski M.E., Wickramasinghe D., Donovan P.J., Golden A.;
RT   "The four cdc25 genes from the nematode Caenorhabditis elegans.";
RL   Gene 214:59-66(1998).
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; FO080960; CCD68116.1; -; Genomic_DNA.
DR   PIR; T15091; T15091.
DR   RefSeq; NP_491862.1; NM_059461.3.
DR   AlphaFoldDB; O44552; -.
DR   SMR; O44552; -.
DR   BioGRID; 37805; 10.
DR   DIP; DIP-25238N; -.
DR   STRING; 6239.K06A5.7.2; -.
DR   iPTMnet; O44552; -.
DR   EPD; O44552; -.
DR   PaxDb; 6239-K06A5-7-1; -.
DR   PeptideAtlas; O44552; -.
DR   EnsemblMetazoa; K06A5.7.1; K06A5.7.1; WBGene00000386.
DR   GeneID; 172353; -.
DR   KEGG; cel:CELE_K06A5.7; -.
DR   UCSC; K06A5.7.1; c. elegans.
DR   AGR; WB:WBGene00000386; -.
DR   WormBase; K06A5.7; CE11778; WBGene00000386; cdc-25.1.
DR   eggNOG; KOG3772; Eukaryota.
DR   HOGENOM; CLU_452865_0_0_1; -.
DR   InParanoid; O44552; -.
DR   OMA; HVEYPEM; -.
DR   OrthoDB; 2881397at2759; -.
DR   PhylomeDB; O44552; -.
DR   Reactome; R-CEL-156711; Polo-like kinase mediated events.
DR   Reactome; R-CEL-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   Reactome; R-CEL-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-CEL-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-CEL-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-CEL-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR   PRO; PR:O44552; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00000386; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:WormBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:WormBase.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:WormBase.
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:SF43; M-PHASE INDUCER PHOSPHATASE CDC-25.1; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 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   3: Inferred from homology;
KW   Cell cycle; Cell division; Hydrolase; Mitosis; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..604
FT                   /note="M-phase inducer phosphatase cdc-25.1"
FT                   /id="PRO_0000198655"
FT   DOMAIN          305..413
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          33..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  67892 MW;  70721C95FA9F40DC CRC64;
     MATTGEKAIY EDQNNVNIIE NVVDVANGIN ESPKTLFEED GSSRDSGVSM TSCSDKSDAS
     PEEDVDFSKL ESGRVALTDC SNFVSILQRN SSVSSSRSSS FYNYDTPTGR KMKTVFDLDS
     LDHSEYEKRV MSERPTDNHR KRTSSSMSPS VTLLDRKRSR NLSLVAPQSD KSCRYNGLNN
     PRDDPFGDED DEVFEQSNVR NSQVQNTSIF AQPAPRTATS LWDLAPPMFF ERKTSDTSGN
     GSFQERPKQI LRAMSVGEID SELPPTLEVK YTLPGVDNPQ RESQAFRSIS PTTLLLEFQR
     LGDDFDKKYI IVDCRFPFEY KGGHVKGAIN LFRHDKIKPI FFPENGEASS FQNRVPIFYC
     EYSQKRGPTM AHAVRSIDRV LNELRYPHVE YPEMYLLDYG YKSLWSTAEC RQICEPCSYI
     PMTHSSFSME FKSARLERHH SMASLKPNGE TSHREEKKKR CTRSVIRRNN SSLNMLSRSS
     SALTSTGSKT SSMENILYGL DDERRPKWVS AFDIQSTESE NDLDAALIYQ RNISSNASNA
     SSIVNLAEER IVQLGLQVIT PDFPDRPSES SSTTPAGEHL PLGEGGHQIP CGILDFSSIS
     DDAE
//