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WASC3_DROME
ID   WASC3_DROME             Reviewed;         176 AA.
AC   Q9VLT8; Q8SYM1;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=WASH complex subunit 3 {ECO:0000250|UniProtKB:Q9Y3C0};
DE   AltName: Full=Coiled-coil domain-containing protein 53 homolog {ECO:0000305};
GN   Name=CCDC53 {ECO:0000312|FlyBase:FBgn0031979};
GN   ORFNames=CG7429 {ECO:0000312|FlyBase:FBgn0031979};
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 [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   [2]
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   [3]
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   [4]
RP   SUBUNIT.
RX   PubMed=20498093; DOI=10.1073/pnas.0913293107;
RA   Jia D., Gomez T.S., Metlagel Z., Umetani J., Otwinowski Z., Rosen M.K.,
RA   Billadeau D.D.;
RT   "WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein
RT   (WASP) family are controlled by analogous structurally related complexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10442-10447(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=25739458; DOI=10.1091/mbc.e14-08-1266;
RA   Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
RT   "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune
RT   cell developmental migrations.";
RL   Mol. Biol. Cell 26:1665-1674(2015).
CC   -!- FUNCTION: Acts at least in part as component of the WASH complex which
CC       may regulate wash nucleation-promoting factor (NPF) activity and is
CC       required for its membrane targeting during endosomal sorting (By
CC       similarity). During embryogenesis, not involved in the wash-dependent
CC       developmental migration of hemocytes anteriorly from the tail
CC       (PubMed:25739458). {ECO:0000250|UniProtKB:Q9Y3C0,
CC       ECO:0000269|PubMed:25739458}.
CC   -!- SUBUNIT: Component of the WASH complex. {ECO:0000269|PubMed:20498093}.
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CCDC53 family. {ECO:0000305}.
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DR   EMBL; AE014134; AAF52595.2; -; Genomic_DNA.
DR   EMBL; AY071457; AAL49079.1; -; mRNA.
DR   RefSeq; NP_609178.1; NM_135334.5.
DR   AlphaFoldDB; Q9VLT8; -.
DR   SMR; Q9VLT8; -.
DR   BioGRID; 60231; 7.
DR   IntAct; Q9VLT8; 3.
DR   STRING; 7227.FBpp0079162; -.
DR   PaxDb; Q9VLT8; -.
DR   DNASU; 34097; -.
DR   EnsemblMetazoa; FBtr0079540; FBpp0079162; FBgn0031979.
DR   GeneID; 34097; -.
DR   KEGG; dme:Dmel_CG7429; -.
DR   UCSC; CG7429-RA; d. melanogaster.
DR   CTD; 34097; -.
DR   FlyBase; FBgn0031979; CCDC53.
DR   VEuPathDB; VectorBase:FBgn0031979; -.
DR   eggNOG; KOG4496; Eukaryota.
DR   GeneTree; ENSGT00390000014084; -.
DR   HOGENOM; CLU_117940_1_0_1; -.
DR   InParanoid; Q9VLT8; -.
DR   OMA; GCETKFV; -.
DR   OrthoDB; 1425330at2759; -.
DR   PhylomeDB; Q9VLT8; -.
DR   BioGRID-ORCS; 34097; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; CCDC53; fly.
DR   GenomeRNAi; 34097; -.
DR   PRO; PR:Q9VLT8; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031979; Expressed in testis and 12 other tissues.
DR   Genevisible; Q9VLT8; DM.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR   GO; GO:0071203; C:WASH complex; IDA:UniProtKB.
DR   GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:FlyBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019309; WASHC3.
DR   PANTHER; PTHR13015; PTHR13015; 1.
DR   Pfam; PF10152; CCDC53; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Endosome; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..176
FT                   /note="WASH complex subunit 3"
FT                   /id="PRO_0000390958"
FT   REGION          84..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..74
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        86..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   176 AA;  19501 MW;  5F8EAA9E18263D63 CRC64;
     MDATAAITGN VDKTQIPPLN QKRILAFVNH FLVSTCTFLN EFALGCETKF VEMERQLQKT
     EAALIILEAK LASIPTEHHV ATEATEAPAI SNQQRNEEAS MVDTTEPPTT ENPTEPELPP
     ESVGVRACED QRYRKFFKMV QVGVPAPAVK QKMQSEGLEP RILDTPDLIL ADGQRE
 
 
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