TBA1_DROME
ID TBA1_DROME Reviewed; 450 AA.
AC P06603; Q9VI59;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Tubulin alpha-1 chain;
GN Name=alphaTub84B; Synonyms=tubA84B; ORFNames=CG1913;
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=3095837; DOI=10.1073/pnas.83.22.8477;
RA Theurkauf W.E., Baum H., Bo J., Wensink P.C.;
RT "Tissue-specific and constitutive alpha-tubulin genes of Drosophila
RT melanogaster code for structurally distinct proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8477-8481(1986).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
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 (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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. Interacts with Ote (PubMed:22751930).
CC {ECO:0000269|PubMed:22751930}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL),
CC respectively. {ECO:0000250}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and
CC affects affinity and processivity of microtubule motors. This
CC modification has a role in multiple cellular functions, ranging from
CC cell motility, cell cycle progression or cell differentiation to
CC intracellular trafficking and signaling (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M14643; AAA28985.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54067.1; -; Genomic_DNA.
DR EMBL; BT012506; AAS93777.1; -; mRNA.
DR PIR; A26488; A26488.
DR RefSeq; NP_476772.1; NM_057424.4.
DR PDB; 6TIS; X-ray; 2.30 A; A/C=1-450.
DR PDB; 6TIU; X-ray; 3.57 A; A/C=1-450.
DR PDB; 6TIY; X-ray; 2.29 A; A/C=1-450.
DR PDB; 6TIZ; X-ray; 2.20 A; A/C=1-450.
DR PDBsum; 6TIS; -.
DR PDBsum; 6TIU; -.
DR PDBsum; 6TIY; -.
DR PDBsum; 6TIZ; -.
DR AlphaFoldDB; P06603; -.
DR SMR; P06603; -.
DR BioGRID; 66045; 46.
DR DIP; DIP-17129N; -.
DR IntAct; P06603; 4.
DR MINT; P06603; -.
DR STRING; 7227.FBpp0081153; -.
DR PaxDb; P06603; -.
DR PRIDE; P06603; -.
DR DNASU; 40848; -.
DR EnsemblMetazoa; FBtr0081639; FBpp0081153; FBgn0003884.
DR GeneID; 40848; -.
DR KEGG; dme:Dmel_CG1913; -.
DR CTD; 40848; -.
DR FlyBase; FBgn0003884; alphaTub84B.
DR VEuPathDB; VectorBase:FBgn0003884; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_1_1; -.
DR InParanoid; P06603; -.
DR OMA; KVGICYQ; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; P06603; -.
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-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; P06603; -.
DR BioGRID-ORCS; 40848; 1 hit in 3 CRISPR screens.
DR ChiTaRS; alphaTub84B; fly.
DR GenomeRNAi; 40848; -.
DR PRO; PR:P06603; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003884; Expressed in cleaving embryo and 20 other tissues.
DR ExpressionAtlas; P06603; baseline and differential.
DR Genevisible; P06603; DM.
DR GO; GO:0000235; C:astral microtubule; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; 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 Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_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; PR01162; ALPHATUBULIN.
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 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin alpha-1 chain"
FT /id="PRO_0000048158"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 450
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6TIY"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6TIY"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 415..435
FT /evidence="ECO:0007829|PDB:6TIZ"
SQ SEQUENCE 450 AA; 49908 MW; E4521F429F5045D2 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TVGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD
RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGMDSG DGEGEGAEEY
