DGT6_DROME
ID DGT6_DROME Reviewed; 654 AA.
AC Q9VAP2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Augmin complex subunit dgt6 {ECO:0000305};
DE AltName: Full=Dim gamma-tubulin 6 {ECO:0000303|PubMed:17412918};
GN Name=dgt6 {ECO:0000303|PubMed:17412918, ECO:0000312|FlyBase:FBgn0039638};
GN ORFNames=CG11881 {ECO:0000312|FlyBase:FBgn0039638};
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:AAL39578.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39578.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39578.1};
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 [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [5] {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 [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CENP-META; GAMMA-TUBULIN; MSPS; NDC80; NUF2 AND
RP TACC, AND SUBCELLULAR LOCATION.
RX PubMed=19836241; DOI=10.1016/j.cub.2009.09.043;
RA Bucciarelli E., Pellacani C., Naim V., Palena A., Gatti M., Somma M.P.;
RT "Drosophila Dgt6 interacts with Ndc80, Msps/XMAP215, and gamma-tubulin to
RT promote kinetochore-driven MT formation.";
RL Curr. Biol. 19:1839-1845(2009).
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).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=23785300; DOI=10.1371/journal.pgen.1003562;
RA Colombie N., Gluszek A.A., Meireles A.M., Ohkura H.;
RT "Meiosis-specific stable binding of augmin to acentrosomal spindle poles
RT promotes biased microtubule assembly in oocytes.";
RL PLoS Genet. 9:E1003562-E1003562(2013).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=24829288; DOI=10.1098/rsob.140047;
RA Savoian M.S., Glover D.M.;
RT "Differing requirements for Augmin in male meiotic and mitotic spindle
RT formation in Drosophila.";
RL Open Biol. 4:140047-140047(2014).
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). dgt6 is required for kinetochore fiber formation,
CC mediating nucleation and/or initial stabilization of chromosome-induced
CC microtubules (PubMed:19836241). {ECO:0000269|PubMed:17412918,
CC ECO:0000269|PubMed:18443220, ECO:0000269|PubMed:19836241}.
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). dgt6 interacts with CENP-meta, gamma-tubulin, msps,
CC Ndc80, Nuf2 and tacc (PubMed:19836241). {ECO:0000269|PubMed:18443220,
CC ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19836241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:17412918, ECO:0000269|PubMed:19836241}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:23785300}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:24829288}. Chromosome, centromere
CC {ECO:0000269|PubMed:24829288}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:19836241}. Note=During mitosis, localizes at aster
CC centers in prophase cells (PubMed:19836241). In prometaphase and
CC metaphase, associates with the entire spindle (PubMed:19836241). During
CC early anaphase, primarily detected on the kinetochore fibers undergoing
CC anaphase shortening (PubMed:19836241). In late anaphase and telophase,
CC becomes enriched at the central spindle but is excluded from its middle
CC region (PubMed:19836241). In interphase cells, displays a uniform
CC distribution (PubMed:19836241). Enriched at spindle poles during
CC meiosis in oocytes (PubMed:23785300). During male meiosis, localizes to
CC kinetochores in a microtubule-independent manner but does not
CC concentrate on spindle microtubules (PubMed:24829288).
CC {ECO:0000269|PubMed:19836241, ECO:0000269|PubMed:23785300}.
CC -!- MISCELLANEOUS: The name 'dim gamma-tubulin 6' derives from the
CC decreased gamma-tubulin staining of the spindle pole seen following
CC RNAi-mediated knockdown of dgt6 in S2 cells.
CC {ECO:0000303|PubMed:17412918}.
CC -!- SIMILARITY: Belongs to the HAUS6 family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56860.1; -; Genomic_DNA.
DR EMBL; AY069433; AAL39578.1; -; mRNA.
DR RefSeq; NP_651671.1; NM_143414.4.
DR AlphaFoldDB; Q9VAP2; -.
DR IntAct; Q9VAP2; 9.
DR STRING; 7227.FBpp0084783; -.
DR PaxDb; Q9VAP2; -.
DR PRIDE; Q9VAP2; -.
DR DNASU; 43441; -.
DR EnsemblMetazoa; FBtr0085414; FBpp0084783; FBgn0039638.
DR GeneID; 43441; -.
DR KEGG; dme:Dmel_CG11881; -.
DR UCSC; CG11881-RA; d. melanogaster.
DR CTD; 43441; -.
DR FlyBase; FBgn0039638; dgt6.
DR VEuPathDB; VectorBase:FBgn0039638; -.
DR eggNOG; ENOG502QV4W; Eukaryota.
DR GeneTree; ENSGT00390000008250; -.
DR HOGENOM; CLU_422286_0_0_1; -.
DR InParanoid; Q9VAP2; -.
DR OMA; KINDPMQ; -.
DR OrthoDB; 453167at2759; -.
DR PhylomeDB; Q9VAP2; -.
DR BioGRID-ORCS; 43441; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43441; -.
DR PRO; PR:Q9VAP2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039638; Expressed in secondary oocyte and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0070652; C:HAUS complex; IEA:InterPro.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:1990498; C:mitotic spindle microtubule; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IEA:InterPro.
DR InterPro; IPR026797; HAUS_6.
DR InterPro; IPR028163; HAUS_6_N.
DR PANTHER; PTHR16151; PTHR16151; 1.
DR Pfam; PF14661; HAUS6_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..654
FT /note="Augmin complex subunit dgt6"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438655"
FT REGION 354..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..356
FT /evidence="ECO:0000255"
FT COMPBIAS 361..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72827 MW; 3F78AED5E3D72F7E CRC64;
MDRTIIAPWK AEEKEQSEKL HRKLQGLALV HPLPDELRKL IAWDMFLKPN QVAFVHVMHY
LFRLLDPAEF KRRFFWPITD KKSEANFRSS TVEYLKHLNE KHQLHWANIK SYLVVMPGGM
RFINFLLEFV GFVIQELIKQ REKSLGLEAG TPNVSAKVMA RQNAVMKEYA SSYVVNLEEN
TALLRDKTQK IRRLMADLSA DMGVPEEQLA DDGFLDEFEA TAALGVERVI TQPTERKFDL
EASLCGLKEA IDLFQVKQAE NNQSKEAVEK ALRGMRVLFD CDAVTEGDFY DPLGASKMDA
LLNGFNRISG TIAEQLDAND HYNESNAFVT TDLQALRVEL SQSEVQLNNL LKKLNEPSKK
DKGSANASGS ARVQTLQPAT PRFESVISSK FVSTPPIRID MGGGGGRNAP VRLALQDDFN
GKQFDALSNS LLAPAPPRSA RKLKALDQST GIDLNGTLNR SKINDPMQML RTIHKNTSKV
KAAPQANLSS LGSKWKQMQA SFGFDEAPVP GAAVISPQTS PTDPSDPFTP LSGSECTRIE
RIPRTSENNT SLIAKSAAVI KVLEVSRNVL NLSTSPSGRL DALVPHTESH QQDVAPRLQL
NDRTINDSLQ LDPDFNIEND KNAFNVSHKF DFDQIGGEDD LQNISDSVLK DIIF
