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MPIP2_CAEEL
ID   MPIP2_CAEEL             Reviewed;         480 AA.
AC   O44628;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=M-phase inducer phosphatase cdc-25.2;
DE            EC=3.1.3.48;
DE   AltName: Full=Cell division cycle-related protein 25.2;
GN   Name=cdc-25.2 {ECO:0000312|WormBase:F16B4.8a};
GN   ORFNames=F16B4.8 {ECO:0000312|WormBase:F16B4.8a};
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).
RN   [3]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=27104746; DOI=10.1080/15384101.2016.1146839;
RA   Lee Y.U., Son M., Kim J., Shim Y.H., Kawasaki I.;
RT   "CDC-25.2, a C. elegans ortholog of cdc25, is essential for the progression
RT   of intestinal divisions.";
RL   Cell Cycle 15:654-666(2016).
RN   [4]
RP   FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   SER-239.
RX   PubMed=27923661; DOI=10.1016/j.bbrc.2016.12.014;
RA   Oh S., Yoon S., Youn E., Kawasaki I., Shim Y.H.;
RT   "cdc-25.2, a Caenorhabditis elegans ortholog of cdc25, is required for male
RT   tail morphogenesis.";
RL   Biochem. Biophys. Res. Commun. 482:1213-1218(2017).
CC   -!- FUNCTION: Required for intestinal cell division following the 16E cell
CC       stage of embryogenesis (PubMed:27104746). Regulates intestinal cell
CC       divisions and binucleations probably by modulating the activity of the
CC       cell cycle regulator wee-1.3 and by activating the cdk-1/cyb-1 complex
CC       (PubMed:27104746). Plays a role in male tail development, via
CC       regulation of the cell divisions of the ray precursor cell lineages,
CC       perhaps acting together with cell cycle regulators cyl-1, cdk-1, cyb-3,
CC       and cyd-1 (PubMed:27923661). {ECO:0000269|PubMed:27104746,
CC       ECO:0000269|PubMed:27923661}.
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: Transiently expressed in the intestine during
CC       larval development (PubMed:27104746). Expressed in the intestine in L1
CC       stage larvae, not expressed in L2 to L3 stage larvae, but is then again
CC       expressed in the gonad of L4 stage larvae (PubMed:27104746). Expressed
CC       in seam cells during larval development (PubMed:27923661). Broadly
CC       expressed throughout development in multiple male somatic tissues,
CC       including pharynx, ventral nerve cord, body muscles, diagonal muscles,
CC       and hypodermis (PubMed:27923661). {ECO:0000269|PubMed:27104746,
CC       ECO:0000269|PubMed:27923661}.
CC   -!- DISRUPTION PHENOTYPE: Viable, but 85% of animals are sterile at 20
CC       degrees Celsius (PubMed:27104746). Reduced number of intestinal cells
CC       in 1.5-fold stage embryos due to defective intestinal divisions and
CC       binuleations at the 16E cell stage of embryonic development
CC       (PubMed:27104746). Knockout with wee-1.3 RNAi suppresses the defect in
CC       intestinal cell divisions in the cdc-25.2 single mutant
CC       (PubMed:27104746). RNAi-mediated knockdown causes abnormal male tail
CC       morphology; this phenotype is suppressed by simultaneous RNAi-mediated
CC       knockdown of wee-1.3 (PubMed:27923661). {ECO:0000269|PubMed:27104746,
CC       ECO:0000269|PubMed:27923661}.
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR   EMBL; FO081161; CCD69573.1; -; Genomic_DNA.
DR   PIR; B88953; B88953.
DR   PIR; T32663; T32663.
DR   PIR; T32665; T32665.
DR   RefSeq; NP_503446.1; NM_071045.3.
DR   AlphaFoldDB; O44628; -.
DR   SMR; O44628; -.
DR   BioGRID; 43712; 2.
DR   STRING; 6239.F16B4.8; -.
DR   PaxDb; O44628; -.
DR   EnsemblMetazoa; F16B4.8a.1; F16B4.8a.1; WBGene00000387.
DR   GeneID; 178645; -.
DR   KEGG; cel:CELE_F16B4.8; -.
DR   UCSC; F16B4.8; c. elegans.
DR   CTD; 178645; -.
DR   WormBase; F16B4.8a; CE19796; WBGene00000387; cdc-25.2.
DR   eggNOG; KOG3772; Eukaryota.
DR   GeneTree; ENSGT00970000196560; -.
DR   HOGENOM; CLU_548886_0_0_1; -.
DR   InParanoid; O44628; -.
DR   OMA; RYPFEYE; -.
DR   OrthoDB; 1423329at2759; -.
DR   PhylomeDB; O44628; -.
DR   PRO; PR:O44628; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000387; Expressed in embryo and 6 other tissues.
DR   ExpressionAtlas; O44628; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0010481; P:epidermal cell division; IMP:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
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; 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; 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; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..480
FT                   /note="M-phase inducer phosphatase cdc-25.2"
FT                   /id="PRO_0000198656"
FT   DOMAIN          243..349
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         239
FT                   /note="S->F: In av40; Causes abnormal male tail morphology
FT                   when cultured at 25 degrees Celsius at the larval L2
FT                   stage."
FT                   /evidence="ECO:0000269|PubMed:27923661"
SQ   SEQUENCE   480 AA;  55737 MW;  19B11B138D582FA5 CRC64;
     MNRPSQISQD VAQPLSNQHE TAMMSSDEDS MSRDSGICEL MDENTPVCFS SMSTESTTVQ
     VEECMEIDED ENLQPGPVSR RQKKVTFRRE KSSCQVRLFD ESPTSHKMFM RPQAPLSVRS
     ENQQLLQQRK RKFEKSEQSS DHFHLEPMSV EAMDDDEIVM MDQNTTKWEP GFRAPNHKKG
     RLTRSATAFP SLETFEEEEH EEQHHLNVKY HLKTVAKESS KGFRRITAET LRDIFFRLSE
     KEFDDKYILI DCRYPYEYNR GHIKNAINHF DRVTVSKIFY DENGRKRCNK IPIFYCEFSQ
     ARGPKMAYAL RQVDRELNVN HYPKCDYEEM YVLDLGYRNF FFAANEANIT NLCQPHAYCE
     MHDKEHTMEL KKYNFHNKGQ SVLRTVSMSR SFKSLPTGSA FNFVASSASF TSAPSTSTEN
     IDTNDDCQKS RTPAVPRIAS RRNLFSDPSH SPTNFAQFPL TCSRETPSPH KHPLTCPRFS
 
 
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