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DGT3_DROME
ID   DGT3_DROME              Reviewed;         565 AA.
AC   Q9W2P0; C9QP53; Q7K3C0;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Augmin complex subunit dgt3 {ECO:0000305};
DE   AltName: Full=Dim gamma-tubulin 3 {ECO:0000303|PubMed:17412918};
GN   Name=dgt3 {ECO:0000303|PubMed:17412918, ECO:0000312|FlyBase:FBgn0034569};
GN   ORFNames=CG3221 {ECO:0000312|FlyBase:FBgn0034569};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:ACX36511.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:ACX36511.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:ACX36511.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAL13907.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-565.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAL13907.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAL13907.1};
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   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17412918; DOI=10.1126/science.1141314;
RA   Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D.,
RA   Stuurman N.;
RT   "Genes required for mitotic spindle assembly in Drosophila S2 cells.";
RL   Science 316:417-421(2007).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND IDENTIFICATION IN THE AUGMIN COMPLEX.
RX   PubMed=18443220; DOI=10.1083/jcb.200711053;
RA   Goshima G., Mayer M., Zhang N., Stuurman N., Vale R.D.;
RT   "Augmin: a protein complex required for centrosome-independent microtubule
RT   generation within the spindle.";
RL   J. Cell Biol. 181:421-429(2008).
RN   [7] {ECO:0000305}
RP   IDENTIFICATION IN THE AUGMIN COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19369198; DOI=10.1073/pnas.0901587106;
RA   Uehara R., Nozawa R.-S., Tomioka A., Petry S., Vale R.D., Obuse C.,
RA   Goshima G.;
RT   "The augmin complex plays a critical role in spindle microtubule generation
RT   for mitotic progression and cytokinesis in human cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:6998-7003(2009).
CC   -!- FUNCTION: As part of the augmin complex, plays a role in centrosome-
CC       independent generation of spindle microtubules (PubMed:18443220). The
CC       complex is required for mitotic spindle assembly through its
CC       involvement in localizing gamma-tubulin to spindle microtubules
CC       (PubMed:17412918). {ECO:0000269|PubMed:17412918,
CC       ECO:0000269|PubMed:18443220}.
CC   -!- SUBUNIT: Component of the augmin complex composed of dgt2, dgt3, dgt4,
CC       dgt5, dgt6, msd1, msd5 and wac (PubMed:18443220, PubMed:19369198). The
CC       complex interacts directly or indirectly with microtubules and is
CC       required for centrosome-independent generation of spindle microtubules
CC       (PubMed:18443220). {ECO:0000269|PubMed:18443220,
CC       ECO:0000269|PubMed:19369198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000305}.
CC   -!- MISCELLANEOUS: The name 'dim gamma-tubulin 3' derives from the
CC       decreased gamma-tubulin staining of the spindle pole seen following
CC       RNAi-mediated knockdown of dgt3 in S2 cells.
CC       {ECO:0000303|PubMed:17412918}.
CC   -!- SIMILARITY: Belongs to the HAUS3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL13907.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE013599; AAF46650.2; -; Genomic_DNA.
DR   EMBL; BT099935; ACX36511.1; -; mRNA.
DR   EMBL; AY058678; AAL13907.1; ALT_INIT; mRNA.
DR   RefSeq; NP_611533.2; NM_137689.5.
DR   AlphaFoldDB; Q9W2P0; -.
DR   SMR; Q9W2P0; -.
DR   DIP; DIP-48827N; -.
DR   IntAct; Q9W2P0; 4.
DR   STRING; 7227.FBpp0271922; -.
DR   PaxDb; Q9W2P0; -.
DR   PRIDE; Q9W2P0; -.
DR   EnsemblMetazoa; FBtr0273414; FBpp0271922; FBgn0034569.
DR   GeneID; 37377; -.
DR   KEGG; dme:Dmel_CG3221; -.
DR   CTD; 37377; -.
DR   FlyBase; FBgn0034569; dgt3.
DR   VEuPathDB; VectorBase:FBgn0034569; -.
DR   eggNOG; ENOG502T1P4; Eukaryota.
DR   HOGENOM; CLU_482580_0_0_1; -.
DR   InParanoid; Q9W2P0; -.
DR   OMA; SVVLWIW; -.
DR   OrthoDB; 849166at2759; -.
DR   PhylomeDB; Q9W2P0; -.
DR   BioGRID-ORCS; 37377; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 37377; -.
DR   PRO; PR:Q9W2P0; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034569; Expressed in egg cell and 13 other tissues.
DR   Genevisible; Q9W2P0; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR   InterPro; IPR032733; HAUS3_N.
DR   Pfam; PF14932; HAUS-augmin3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..565
FT                   /note="Augmin complex subunit dgt3"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438652"
FT   COILED          135..171
FT                   /evidence="ECO:0000255"
FT   COILED          212..241
FT                   /evidence="ECO:0000255"
FT   CONFLICT        132
FT                   /note="V -> A (in Ref. 3; ACX36511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="S -> Y (in Ref. 3; ACX36511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        486
FT                   /note="L -> F (in Ref. 3; ACX36511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   565 AA;  65823 MW;  13D1E05627568E53 CRC64;
     MGDLLSNSEF FKKLGVDSSN QWILYDEQME MFFKFLSGNI TDANILTERQ VLEREEMQRR
     GEWLSASDRE LKLLQIEAES PGLLNYKQQD VDALTMSIEA IEDASRDYAT LLEDMMTTKH
     SITKHLGEVE CVTAELQLRE KDLIAECQSK AKQLEELQQE NCRLSAEAKK AFTAPQLPPL
     FMHQLPLEQY FHKCDSFMQY FTLYVKENFK IQDYDEFQSA EEDLGREKAK LEDLERGIQF
     YALSYIRTKA KVKATQCLID QLDLGKIHCL SLTDMAREMH DLQLLNDYQL SNTHDTLLND
     LTIHIQQHTQ RRIELVLYEN TKLKLERAVR RHESDKKLTK IISDALSNAE LLWIAIQLDC
     DKKRNCLDTS EELRDQAQAT WQRIQTMRSI NASYQGICAQ FVQEIANLLS AHLGQNIKAT
     EAKACLFEYE KFGRLLSYSF QSMLNRKSCA AVQDQLAELK RLEQTLRPFV YDSPLEQPMF
     ENVRYLSAIY NVTQQQTRLD ESGRSLRKDF LENVVGRIER DKLYRYSVVL WIWFLTEPQR
     MMHAIDEVKK AAAAVIRPGG GLHRK
 
 
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