WAGC_DROME
ID WAGC_DROME Reviewed; 163 AA.
AC Q9W0S8; E1JHV2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Augmin complex subunit wac {ECO:0000305};
DE AltName: Full=wee Augmin component {ECO:0000303|PubMed:19289792};
GN Name=wac {ECO:0000303|PubMed:19289792, ECO:0000312|FlyBase:FBgn0035120};
GN Synonyms=dgt8 {ECO:0000303|PubMed:19369198};
GN ORFNames=CG13879 {ECO:0000312|FlyBase:FBgn0035120};
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:ANY27392.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE AUGMIN COMPLEX, INTERACTION WITH DGT2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19289792; DOI=10.1083/jcb.200811102;
RA Meireles A.M., Fisher K.H., Colombie N., Wakefield J.G., Ohkura H.;
RT "Wac: a new Augmin subunit required for chromosome alignment but not for
RT acentrosomal microtubule assembly in female meiosis.";
RL J. Cell Biol. 184:777-784(2009).
RN [5] {ECO:0000305}
RP IDENTIFICATION IN THE AUGMIN COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS 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 [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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:19289792). The
CC complex is required for mitotic spindle assembly through its
CC involvement in localizing gamma-tubulin to spindle microtubules
CC (PubMed:19289792). wac is dispensable for somatic mitosis and for
CC assembly of spindle microtubules in oocytes during female meiosis but
CC is required during female meiosis for chromosome alignment and
CC segregation (PubMed:19289792). It is required for microtubule assembly
CC near spindle poles in oocytes (PubMed:23785300). It is also required
CC for acentrosomal microtubule nucleation and meiotic spindle formation
CC during male meiosis (PubMed:24829288). wac binds to microtubules in
CC vitro (PubMed:19289792). {ECO:0000269|PubMed:19289792,
CC ECO:0000269|PubMed:23785300, ECO:0000269|PubMed:24829288}.
CC -!- SUBUNIT: Component of the augmin complex composed of dgt2, dgt3, dgt4,
CC dgt5, dgt6, msd1, msd5 and wac (PubMed:19289792, PubMed:19369198). The
CC complex interacts directly or indirectly with microtubules and is
CC required for centrosome-independent generation of spindle microtubules
CC (PubMed:19289792). wac interacts directly (via coiled coil) with dgt2
CC (PubMed:19289792). {ECO:0000269|PubMed:19289792,
CC ECO:0000269|PubMed:19369198}.
CC -!- INTERACTION:
CC Q9W0S8; Q9VKD6: dgt2; NbExp=3; IntAct=EBI-180262, EBI-84322;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19289792, ECO:0000269|PubMed:19369198}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:23785300}. Note=Enriched
CC at spindle poles during meiosis in oocytes.
CC {ECO:0000269|PubMed:23785300}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0035120}; Synonyms=D
CC {ECO:0000312|FlyBase:FBgn0035120};
CC IsoId=Q9W0S8-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0035120};
CC IsoId=Q9W0S8-2; Sequence=VSP_058701;
CC -!- TISSUE SPECIFICITY: In adult females, detected only in the abdomen with
CC no expression in the head or thorax (at protein level).
CC {ECO:0000269|PubMed:19289792}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in early embryos but at
CC low levels in larva, pupa and adult (at protein level).
CC {ECO:0000269|PubMed:19289792}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable but have greatly reduced
CC levels of augmin complex subunit Dgt2 (PubMed:19289792). Mitotic
CC progression is delayed but is not blocked before anaphase onset and
CC chromosomes are properly segregated (PubMed:19289792). 7% of meiotic
CC chromosomes in spermatids are missegregated (PubMed:19289792). Mutant
CC males are fertile but mutant females are sterile, developing fully
CC mature ovaries but laying eggs that fail to hatch (PubMed:19289792).
CC Chromosome positioning and segregation are disrupted in oocytes
CC (PubMed:19289792). Chromosome spreading in oocytes following nuclear
CC envelope breakdown is not limited as in wild-type and instead is spread
CC along the spindle axis (PubMed:23785300). Significant increase in the
CC frequency of oocyte spindles with a missing or weak spindle pole
CC (PubMed:23785300). Delayed spindle formation in spermatocytes during
CC male meiosis (PubMed:24829288). {ECO:0000269|PubMed:19289792,
CC ECO:0000269|PubMed:23785300, ECO:0000269|PubMed:24829288}.
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DR EMBL; AE014296; AAF47365.2; -; Genomic_DNA.
DR EMBL; AE014296; AGB93889.1; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94578.1; -; Genomic_DNA.
DR EMBL; KX531582; ANY27392.1; -; mRNA.
DR EMBL; KX531622; ANY27432.1; -; mRNA.
DR RefSeq; NP_001163306.1; NM_001169835.1. [Q9W0S8-2]
DR RefSeq; NP_001261194.1; NM_001274265.1. [Q9W0S8-1]
DR RefSeq; NP_612020.2; NM_138176.3. [Q9W0S8-1]
DR AlphaFoldDB; Q9W0S8; -.
DR SMR; Q9W0S8; -.
DR IntAct; Q9W0S8; 9.
DR STRING; 7227.FBpp0304416; -.
DR PaxDb; Q9W0S8; -.
DR DNASU; 38044; -.
DR EnsemblMetazoa; FBtr0289972; FBpp0288410; FBgn0035120. [Q9W0S8-1]
DR EnsemblMetazoa; FBtr0300711; FBpp0289935; FBgn0035120. [Q9W0S8-2]
DR EnsemblMetazoa; FBtr0332106; FBpp0304416; FBgn0035120. [Q9W0S8-1]
DR GeneID; 38044; -.
DR KEGG; dme:Dmel_CG13879; -.
DR UCSC; CG13879-RB; d. melanogaster. [Q9W0S8-1]
DR CTD; 51322; -.
DR FlyBase; FBgn0035120; wac.
DR VEuPathDB; VectorBase:FBgn0035120; -.
DR eggNOG; ENOG502T8ST; Eukaryota.
DR HOGENOM; CLU_1760722_0_0_1; -.
DR InParanoid; Q9W0S8; -.
DR OMA; IPKDFNI; -.
DR PhylomeDB; Q9W0S8; -.
DR BioGRID-ORCS; 38044; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38044; -.
DR PRO; PR:Q9W0S8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035120; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q9W0S8; baseline and differential.
DR Genevisible; E1JHV2; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072687; C:meiotic spindle; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0051301; P:cell division; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IMP:FlyBase.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Meiosis; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..163
FT /note="Augmin complex subunit wac"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438658"
FT COILED 86..115
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_058701"
SQ SEQUENCE 163 AA; 19053 MW; B0C2372BD98E8A9F CRC64;
MQNLKIQEEV NSLMRLGQHF DDQLKLASVE LGDFSDDDLA LLDKCAQYYS LLHIHDINLN
YLRDFYCAKK RECIENRQTT VQQRVELQRI LSSIEEATRD VVMLERFNAA AEERLIPDIV
VMQRNAQQLA TKQALLDRQK TLKIPKDFSI ESVIEKVDSL EQR
