位置:首页 > 蛋白库 > TWINE_DROME
TWINE_DROME
ID   TWINE_DROME             Reviewed;         426 AA.
AC   Q03019; Q9V454;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Cdc25-like protein phosphatase twine;
DE            EC=3.1.3.48;
GN   Name=twe; ORFNames=CG4965;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1606618; DOI=10.1016/0092-8674(92)90616-k;
RA   Alphey L.S., Jimenez J., White-Cooper H., Dawson I., Nurse P., Glover D.M.;
RT   "Twine, a cdc25 homolog that functions in the male and female germline of
RT   Drosophila.";
RL   Cell 69:977-988(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA   Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA   Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA   Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA   Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA   Celniker S.E., Rubin G.M.;
RT   "An exploration of the sequence of a 2.9-Mb region of the genome of
RT   Drosophila melanogaster: the Adh region.";
RL   Genetics 153:179-219(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-426.
RX   PubMed=1286615; DOI=10.1242/dev.116.2.405;
RA   Courtot C., Fankhauser C., Simanis V., Lehner C.F.;
RT   "The Drosophila cdc25 homolog twine is required for meiosis.";
RL   Development 116:405-416(1992).
CC   -!- FUNCTION: Required during meiosis. Regulates the transition from the
CC       extended G2 phase to the onset of the first meiotic division.
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   -!- INTERACTION:
CC       Q03019; P23572: Cdk1; NbExp=4; IntAct=EBI-138996, EBI-108689;
CC   -!- TISSUE SPECIFICITY: Expressed in developing male and female germ cells.
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M94158; AAA28413.1; -; mRNA.
DR   EMBL; AE014134; AAF53508.1; -; Genomic_DNA.
DR   EMBL; AY061266; AAL28814.1; -; mRNA.
DR   EMBL; X69018; CAA48783.1; -; mRNA.
DR   PIR; A41910; A41910.
DR   RefSeq; NP_001260491.1; NM_001273562.2.
DR   RefSeq; NP_001260492.1; NM_001273563.1.
DR   RefSeq; NP_001260493.1; NM_001273564.2.
DR   RefSeq; NP_476633.1; NM_057285.4.
DR   AlphaFoldDB; Q03019; -.
DR   SMR; Q03019; -.
DR   BioGRID; 60966; 6.
DR   DIP; DIP-23538N; -.
DR   IntAct; Q03019; 6.
DR   STRING; 7227.FBpp0080412; -.
DR   PaxDb; Q03019; -.
DR   DNASU; 34954; -.
DR   EnsemblMetazoa; FBtr0080855; FBpp0080412; FBgn0002673.
DR   EnsemblMetazoa; FBtr0331444; FBpp0303861; FBgn0002673.
DR   EnsemblMetazoa; FBtr0331445; FBpp0303862; FBgn0002673.
DR   EnsemblMetazoa; FBtr0331446; FBpp0303863; FBgn0002673.
DR   GeneID; 34954; -.
DR   KEGG; dme:Dmel_CG4965; -.
DR   UCSC; CG4965-RA; d. melanogaster.
DR   CTD; 34954; -.
DR   FlyBase; FBgn0002673; twe.
DR   VEuPathDB; VectorBase:FBgn0002673; -.
DR   eggNOG; KOG3772; Eukaryota.
DR   GeneTree; ENSGT00940000166659; -.
DR   HOGENOM; CLU_014464_3_1_1; -.
DR   InParanoid; Q03019; -.
DR   OMA; KTKSWQC; -.
DR   OrthoDB; 1423329at2759; -.
DR   PhylomeDB; Q03019; -.
DR   Reactome; R-DME-156711; Polo-like kinase mediated events.
DR   Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-DME-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR   Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR   SignaLink; Q03019; -.
DR   BioGRID-ORCS; 34954; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; twe; fly.
DR   GenomeRNAi; 34954; -.
DR   PRO; PR:Q03019; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0002673; Expressed in cleaving embryo and 24 other tissues.
DR   ExpressionAtlas; Q03019; baseline and differential.
DR   Genevisible; Q03019; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005819; C:spindle; IDA:FlyBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:FlyBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0009880; P:embryonic pattern specification; HMP:FlyBase.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; TAS:FlyBase.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR   GO; GO:0051078; P:meiotic nuclear membrane disassembly; IMP:FlyBase.
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:FlyBase.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:FlyBase.
DR   GO; GO:0007348; P:regulation of syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
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; Meiosis; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..426
FT                   /note="Cdc25-like protein phosphatase twine"
FT                   /id="PRO_0000198659"
FT   DOMAIN          265..371
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000250"
FT   CONFLICT        48
FT                   /note="L -> M (in Ref. 6; CAA48783)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  48320 MW;  0F8626692B683D08 CRC64;
     MASKRLMLDV EEEDDESGAC GQENFDPHDA DMEYQAKRRK SAVQETPLQW MLKRHIPAST
     TVLSPITELS QNMNGARLDG TPKSTQRIPA NRTLNNFNSL SSRTLGSFSS SCSSYESGNS
     LDDEYMDMFE MESAENHNLE LPDDLEVLLS GQLKSESNLE EMSNKKGSLR RCLSMYPSEQ
     PEEAVQEPDQ ETNMPMKKMQ RKTLSMNDAE IMRALGDEPE LIGDLSKPCT LPCLATGIRH
     RDLKTISSDT LARLIQGEFD EQLGSQGGYE IIDCRYPYEF LGGHIRGAKN LYTRGQIQEA
     FPTLTSNQEN RRIYVFHCEF SSERGPKLLR YLRSNDRSQH THNYPALDYP ELYILHNGYK
     EFFGLYSQLC QPSQYVPMLA PAHNDEFRYF RAKTKSWQCG EGGDSGIGGG GSRGLRKSRS
     RLLYAE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024