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   25-OCT-2017, entry version 169.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3037352; DOI=10.1128/MCB.7.6.2231;
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
RT   assembly-defective mutation of the testis-specific isoform (B2t8)
RT   reveal both an ancient divergence in metazoan isotypes and structural
RT   constraints for 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.,
RA   Couderc J.-L., Dastugue B.;
RT   "Intronic and 5' flanking sequences of the Drosophila betasub3 tubulin
RT   gene 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   Pacleb J.M., 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;
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.,
RA   Couderc J.L., Dastugue B.;
RT   "Enhancer and silencer elements within the first intron mediate the
RT   transcriptional regulation of the beta 3 tubulin gene by 20-
RT   hydroxyecdysone in Drosophila Kc cells.";
RL   Insect Biochem. Mol. Biol. 23:137-143(1993).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
CC       a hollow water-filled tube with an outer diameter of 25 nm and an
CC       inner diameter of 15 nM. Alpha-beta heterodimers associate head-
CC       to-tail to form protofilaments running lengthwise along the
CC       microtubule wall with the beta-tubulin subunit facing the
CC       microtubule plus end conferring a structural polarity.
CC       Microtubules usually have 13 protofilaments but different
CC       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   UniGene; Dm.21376; -.
DR   ProteinModelPortal; P08841; -.
DR   SMR; P08841; -.
DR   BioGrid; 63462; 24.
DR   IntAct; P08841; 3.
DR   MINT; MINT-1021949; -.
DR   STRING; 7227.FBpp0072177; -.
DR   PaxDb; P08841; -.
DR   PRIDE; P08841; -.
DR   EnsemblMetazoa; FBtr0072270; FBpp0072177; FBgn0003888.
DR   GeneID; 37888; -.
DR   KEGG; dme:Dmel_CG3401; -.
DR   CTD; 37888; -.
DR   FlyBase; FBgn0003888; betaTub60D.
DR   eggNOG; KOG1375; Eukaryota.
DR   eggNOG; COG5023; LUCA.
DR   GeneTree; ENSGT00760000119061; -.
DR   InParanoid; P08841; -.
DR   KO; K07375; -.
DR   OMA; DEMEGEC; -.
DR   OrthoDB; EOG091G06U2; -.
DR   PhylomeDB; P08841; -.
DR   ChiTaRS; betaTub60D; fly.
DR   GenomeRNAi; 37888; -.
DR   PRO; PR:P08841; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0003888; -.
DR   ExpressionAtlas; P08841; differential.
DR   Genevisible; P08841; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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:0007507; P:heart development; NAS:FlyBase.
DR   GO; GO:0030537; P:larval behavior; IMP:FlyBase.
DR   GO; GO:0007017; P:microtubule-based process; ISS:FlyBase.
DR   GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR037103; Tubulin/FtsZ_C_sf.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
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   Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    454       Tubulin beta-3 chain.
FT                                /FTId=PRO_0000048280.
FT   NP_BIND     146    152       GTP. {ECO:0000255}.
FT   CONFLICT      6      6       N -> H (in Ref. 1; AAA28993 and 2;
FT                                CAA34725). {ECO:0000305}.
FT   CONFLICT    288    288       R -> G (in Ref. 2; CAA34726).
FT                                {ECO:0000305}.
FT   CONFLICT    322    322       V -> I (in Ref. 2; CAA34726).
FT                                {ECO:0000305}.
FT   CONFLICT    338    339       AV -> NI (in Ref. 2; CAA34726).
FT                                {ECO:0000305}.
FT   CONFLICT    365    365       K -> R (in Ref. 1; AAA28993 and 2;
FT                                CAA34726). {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
//