TBG2_DROME
ID TBG2_DROME Reviewed; 457 AA.
AC P42271; O77160; Q9V476;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Tubulin gamma-2 chain;
DE AltName: Full=Gamma-2-tubulin;
GN Name=gammaTub37C; Synonyms=Tub37CD, TubG2, TubG37C; ORFNames=CG17566;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9155007; DOI=10.1093/emboj/16.8.1809;
RA Tavosanis G., Llamazares S., Goulielmos G., Gonzalez C.;
RT "Essential role for gamma-tubulin in the acentriolar female meiotic spindle
RT of Drosophila.";
RL EMBO J. 16:1809-1819(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Ovary;
RX PubMed=9133431; DOI=10.1006/dbio.1997.8545;
RA Wilson P.G., Zheng Y., Oakley C.E., Oakley B.R., Borisy G.G., Fuller M.T.;
RT "Differential expression of two gamma-tubulin isoforms during gametogenesis
RT and development in Drosophila.";
RL Dev. Biol. 184:207-221(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9698447; DOI=10.1006/dbio.1998.8900;
RA Wilson P.G., Borisy G.G.;
RT "Maternally expressed gamma Tub37CD in Drosophila is differentially
RT required for female meiosis and embryonic mitosis.";
RL Dev. Biol. 199:273-290(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH OTE.
RX PubMed=22751930; DOI=10.1128/mcb.00814-12;
RA Habermann K., Mirgorodskaya E., Gobom J., Lehmann V., Mueller H.,
RA Bluemlein K., Deery M.J., Czogiel I., Erdmann C., Ralser M.,
RA von Kries J.P., Lange B.M.;
RT "Functional analysis of centrosomal kinase substrates in Drosophila
RT melanogaster reveals a new function of the nuclear envelope component
RT otefin in cell cycle progression.";
RL Mol. Cell. Biol. 32:3554-3569(2012).
RN [8]
RP FUNCTION, 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).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles or the centrosome, suggesting that it is involved in the
CC minus-end nucleation of microtubule assembly. Required for oocyte
CC activation and consequently for organization of the female meiotic
CC spindle (PubMed:9155007, PubMed:9698447). Essential for centrosome
CC organization and assembly of biastral mitotic spindles in embryos.
CC Plays a role in stabilizing the augmin complex on the meiotic spindle
CC (PubMed:23785300). {ECO:0000269|PubMed:23785300,
CC ECO:0000269|PubMed:9155007, ECO:0000269|PubMed:9698447}.
CC -!- SUBUNIT: Interacts with Ote. {ECO:0000269|PubMed:22751930}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:9155007}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:9155007}. Note=Embryonic
CC mitotic spindle, female meiotic spindle.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cells and oocytes of developing
CC egg chambers. {ECO:0000269|PubMed:9133431, ECO:0000269|PubMed:9698447}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression is restricted to adult females. {ECO:0000269|PubMed:9133431,
CC ECO:0000269|PubMed:9155007}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in oocytes results in
CC spindle defects. {ECO:0000269|PubMed:23785300}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF081252; AAC35843.1; -; Genomic_DNA.
DR EMBL; AJ010552; CAA09233.1; -; Genomic_DNA.
DR EMBL; M76765; AAB52553.1; -; mRNA.
DR EMBL; AF091265; AAC64117.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53774.1; -; Genomic_DNA.
DR EMBL; AY070558; AAL48029.1; -; mRNA.
DR PIR; T08419; T08419.
DR RefSeq; NP_001260565.1; NM_001273636.1.
DR RefSeq; NP_476922.1; NM_057574.5.
DR AlphaFoldDB; P42271; -.
DR SMR; P42271; -.
DR BioGRID; 61183; 31.
DR DIP; DIP-60707N; -.
DR IntAct; P42271; 4.
DR MINT; P42271; -.
DR STRING; 7227.FBpp0304827; -.
DR PaxDb; P42271; -.
DR DNASU; 35199; -.
DR EnsemblMetazoa; FBtr0081228; FBpp0080769; FBgn0010097.
DR EnsemblMetazoa; FBtr0332572; FBpp0304827; FBgn0010097.
DR GeneID; 35199; -.
DR KEGG; dme:Dmel_CG17566; -.
DR CTD; 35199; -.
DR FlyBase; FBgn0010097; gammaTub37C.
DR VEuPathDB; VectorBase:FBgn0010097; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000174463; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P42271; -.
DR OMA; RRESMFK; -.
DR OrthoDB; 687389at2759; -.
DR PhylomeDB; P42271; -.
DR BioGRID-ORCS; 35199; 0 hits in 3 CRISPR screens.
DR ChiTaRS; gammaTub37C; fly.
DR GenomeRNAi; 35199; -.
DR PRO; PR:P42271; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010097; Expressed in secondary oocyte and 5 other tissues.
DR ExpressionAtlas; P42271; differential.
DR Genevisible; P42271; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0072687; C:meiotic spindle; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IMP:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:FlyBase.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding; Meiosis;
KW Microtubule; Mitosis; Nucleotide-binding; Reference proteome.
FT CHAIN 1..457
FT /note="Tubulin gamma-2 chain"
FT /id="PRO_0000048455"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 282
FT /note="T -> A (in Ref. 2; AAB52553)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="E -> K (in Ref. 1; AAC35843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 51296 MW; 00C326DC5744618A CRC64;
MPSEIITLQL GQCGNQIGFE FWKRLCLEHG ISPDGVLEDF ATDGQDRKDV FFYQADDNHY
IPRAVLIDLE PRVINNIMTS PYSKLYNQEN VFLSKHGGGA GNNWASGFSQ GEKVQEEVFD
ILDREADGSD SLEGFVLCHS IAGGTGSGMG SYVLERLSER FPKKLIQTYS VFPNQDEISD
VVVQPYNSIL TLKRLTKCAD SVVVLDNTAL NRIATERLHI QTPTFTQINN LVSTIMSLST
TTLRYPSYMN NNLIGLTASL IPTPQLHFLM TGYTPLMSDC ETKTSVRKTT VLDVMRRLLQ
PKNMMVSALT DKQSRQCFVS ILNIIQGEVD PSQVHKSLQR IRERKLANFI PWGPASIQVA
LPRSSPYVQS AHKVSGLMMA NHTGISSLFK RALAQYDKLR KRNAFLDNFR RESMFQDDLT
ELDIARDTVD CLVQEYEAAT QIDYPQWSPA VEASKAG
