MPIP_DICDI
ID MPIP_DICDI Reviewed; 1053 AA.
AC Q54QM6; Q86M49;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=M-phase inducer phosphatase;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase cdc25;
GN Name=cdc25; ORFNames=DDB_G0283617;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND
RP PHOSPHORYLATION.
RC STRAIN=AX2;
RX PubMed=15351882; DOI=10.1007/s00427-004-0429-x;
RA Mayanagi T., Maeda Y., Hirose S., Arakane T., Araki T., Amagai A.;
RT "Cloning, sequencing, and expression of the genomic DNA encoding the
RT protein phosphatase cdc25 in Dictyostelium discoideum.";
RL Dev. Genes Evol. 214:510-514(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Tyrosine protein phosphatase which may function as a dosage-
CC dependent inducer in mitotic control. {ECO:0000250}.
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 -!- DEVELOPMENTAL STAGE: Present at all developmental stages (at protein
CC level). {ECO:0000269|PubMed:15351882}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:15351882}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
CC -!- CAUTION: The protein might be post-translationally truncated or the
CC gene model could be wrong, because experimentally the protein migrates
CC like a 56 kDa protein wereas it should migrate around 117 kDa.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC66469.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB039883; BAC66469.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AAFI02000056; EAL65575.1; -; Genomic_DNA.
DR RefSeq; XP_638997.1; XM_633905.1.
DR AlphaFoldDB; Q54QM6; -.
DR SMR; Q54QM6; -.
DR STRING; 44689.DDB0191424; -.
DR PaxDb; Q54QM6; -.
DR EnsemblProtists; EAL65575; EAL65575; DDB_G0283617.
DR GeneID; 8624243; -.
DR KEGG; ddi:DDB_G0283617; -.
DR dictyBase; DDB_G0283617; cdc25.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_290614_0_0_1; -.
DR InParanoid; Q54QM6; -.
DR OMA; RTCLDFT; -.
DR Reactome; R-DDI-156711; Polo-like kinase mediated events.
DR Reactome; R-DDI-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DDI-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-DDI-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DDI-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-DDI-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR PRO; PR:Q54QM6; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:dictyBase.
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: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:0006470; P:protein dephosphorylation; ISS:dictyBase.
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; 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; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..1053
FT /note="M-phase inducer phosphatase"
FT /id="PRO_0000327912"
FT DOMAIN 901..1001
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 125..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 957
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ SEQUENCE 1053 AA; 117119 MW; F528DD893056A22B CRC64;
MGPTENQSFE IEFPNSSNTA AANSISTAIN NNTTTAATIT FTPANNNINN INNNNNNNNN
NKFNSNFDIE SNKENSINQS NINSNVNSFP LKIQTKTLNS TTTSSNNNNN NIFSIGFRPL
SPRGVSPRFH SNSSSSCSSE ISTPSSSTFL EDPNLIASNT ISSNNSINNN NNNNNNNNNN
NNNNNNDNSN NNINTNNINN NNNNTNNGEN PQKKQRNSQI LSKNFYSLSL HADSPKHSRS
TTDLSTFLGM SDPDVMTYRS KTFCISDFHQ FDIDTTTNDN KNKNNNTKST DESSTFDGKS
SNSVENNNMT IINNNNNNNN NNNNNNNNNN NNNNLNQDRP TIPTVAHSLS SNSIPHKFNS
SNSLPPQMLS SSAPSLFSLL ENSNNNNNNN NNNNNNNNNN NNNNNNNDNS NISINDESIV
LISTPVKEYS YNRSLCLSDE EGGEDDEDDT PPTPIQLVRP TPTPINPSLS LSLSSSLNAT
NSTTYLHLGR SATVLLNPPL LVSSMRQHHN SPSSSPSQSI PIVQTRERSQ SSLSFLSPYQ
QQYYPSSPEL SPMVPTPLVN RIFNNINNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNGTN
SNNLNNQSTS EDRDDSPNTS LDQISGSPYK TPSKLSFHSP NSSAIFNSIS NSQQTGKRSR
TCLDFTKFSS HLLDEDSSCF STQTNNNNTS STGLISPSSS PKQQNVLIEN TTNTTSNSSS
SSSSTTTTTT TISVTNTLAA IQQNLNSNAN LNNNNNNNNN NNNNISSYFS RSNSISSQRP
PRPLSMSSSF ISRQSPDIHI SSNSLPKPVD TSNTNNNNEN ENDTNKLDKI NNVNSNIAKI
IEQQQQRNIS NSNNNNNLTQ DQDQQDDQFK AKLLKQLSGR QGYNGVSSES VYELLKNPTL
INAIITVVDC RYKYEYDGGH IKNAINIPPT GSRQMVLDRF FKFPTPKNQQ HVIIFHCEFS
SKRAPDCYSL FRELDREHNE YPNIHYPEIY LLNGGYKKFF ESFQGDMCEG NYIRMDDKLY
QANLKEEEEK KKKEKITIRN IKAFKNRSHS FHV
