TBB3_DROME
ID TBB3_DROME Reviewed; 454 AA.
AC P08841; Q6I8M0; Q6I8M1; Q9W184;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Tubulin beta-3 chain;
DE AltName: Full=Beta-3-tubulin;
GN Name=betaTub60D; Synonyms=TubB60C; ORFNames=CG3401;
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].
RX PubMed=3037352; DOI=10.1128/mcb.7.6.2231-2242.1987;
RA Rudolph J.E., Kimble M., Hoyle H.D., Subler M.A., Raff E.C.;
RT "Three Drosophila beta-tubulin sequences: a developmentally regulated
RT isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-
RT defective mutation of the testis-specific isoform (B2t8) reveal both an
RT ancient divergence in metazoan isotypes and structural constraints for
RT beta-tubulin function.";
RL Mol. Cell. Biol. 7:2231-2242(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=8375576; DOI=10.1016/0303-7207(93)90052-l;
RA Bruhat A., Dreau D., Drake M.E., Tourmente S., Chapel S., Couderc J.-L.,
RA Dastugue B.;
RT "Intronic and 5' flanking sequences of the Drosophila betasub3 tubulin gene
RT are essential to confer ecdysone responsiveness.";
RL Mol. Cell. Endocrinol. 94:61-71(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-21.
RC STRAIN=Oregon-R;
RX PubMed=1363225; DOI=10.1242/dev.116.3.543;
RA Hinz U., Wolk A., Renkawitz-Pohl R.;
RT "Ultrabithorax is a regulator of beta 3 tubulin expression in the
RT Drosophila visceral mesoderm.";
RL Development 116:543-554(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-44.
RX PubMed=8485515; DOI=10.1016/0965-1748(93)90092-7;
RA Tourmente S., Chapel S., Dreau D., Drake M.E., Bruhat A., Couderc J.L.,
RA Dastugue B.;
RT "Enhancer and silencer elements within the first intron mediate the
RT transcriptional regulation of the beta 3 tubulin gene by 20-hydroxyecdysone
RT in Drosophila Kc cells.";
RL Insect Biochem. Mol. Biol. 23:137-143(1993).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- MISCELLANEOUS: Beta-3 is a developmentally regulated isoform.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M22335; AAA28993.1; -; Genomic_DNA.
DR EMBL; M22341; AAA28993.1; JOINED; Genomic_DNA.
DR EMBL; X16825; CAA34725.1; -; Genomic_DNA.
DR EMBL; X16826; CAA34726.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47193.2; -; Genomic_DNA.
DR EMBL; BT015991; AAV36876.1; -; mRNA.
DR EMBL; X68393; CAA48459.1; -; Genomic_DNA.
DR EMBL; S60740; AAD13917.1; -; Genomic_DNA.
DR PIR; B27810; B27810.
DR PIR; S33567; S33567.
DR PIR; S60269; S60269.
DR RefSeq; NP_523842.2; NM_079118.3.
DR AlphaFoldDB; P08841; -.
DR SMR; P08841; -.
DR BioGRID; 63462; 24.
DR IntAct; P08841; 3.
DR STRING; 7227.FBpp0072177; -.
DR PaxDb; P08841; -.
DR PRIDE; P08841; -.
DR DNASU; 37888; -.
DR EnsemblMetazoa; FBtr0072270; FBpp0072177; FBgn0003888.
DR GeneID; 37888; -.
DR KEGG; dme:Dmel_CG3401; -.
DR CTD; 37888; -.
DR FlyBase; FBgn0003888; betaTub60D.
DR VEuPathDB; VectorBase:FBgn0003888; -.
DR eggNOG; KOG1375; Eukaryota.
DR InParanoid; P08841; -.
DR OMA; EMEGECV; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P08841; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-5620924; Intraflagellar transport.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; P08841; -.
DR BioGRID-ORCS; 37888; 0 hits in 3 CRISPR screens.
DR ChiTaRS; betaTub60D; fly.
DR GenomeRNAi; 37888; -.
DR PRO; PR:P08841; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003888; Expressed in embryonic/larval hemocyte (Drosophila) and 53 other tissues.
DR ExpressionAtlas; P08841; baseline and differential.
DR Genevisible; P08841; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0030537; P:larval behavior; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; 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:0009416; P:response to light stimulus; IMP:FlyBase.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..454
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000048280"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 6
FT /note="N -> H (in Ref. 1; AAA28993 and 2; CAA34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="R -> G (in Ref. 2; CAA34726)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> I (in Ref. 2; CAA34726)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..339
FT /note="AV -> NI (in Ref. 2; CAA34726)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="K -> R (in Ref. 1; AAA28993 and 2; CAA34726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50849 MW; 573DD088E5664D57 CRC64;
MREIVNLQAG QCGNQIGAKF WEIISEEHGI DSNGIYVGDS DLQLERVSVY YNEASAVTRS
SGGKYVPRAI LLDLEPGTME SVRSGPYGQL FRPDNFVYGQ SGAGNNWAKG HYTEGAELVD
NVLDVVRKEC ENCDCLQGFQ LTHSLGGGTG SGMGTLLISK IREEYPDRIM NTYSVVPSPK
VSDTVVEPYN ATLSIHQLVE NTDETYCIDN EALYDICFRT LKVSNPSYGD LNHLVSLTMS
GVTTCLRFPG QLNADLRKLA VNMVPFPRLH FFMPGFAPLT SRGSQQYRAL TVPELTQQMF
DAKNMMAACD PRHGRYLTVA AVFRGRMSMK EVDEQMLAVQ NKNSSYFVEW IPNNVKTAVC
DIPPKGLKMS STFIGNTTAI QELFKRISEQ FSAMFRRKAF LHWYTGEGMD EMEFTEAESN
MNDLVSEYQQ YQEATADDEF DPEVNQEEVE GDCI
