ID TBA1D_BOVIN Reviewed; 452 AA.
AC Q2HJ86;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Tubulin alpha-1D chain;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1D chain;
GN Name=TUBA1D;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=6504138; DOI=10.1038/312237a0;
RA Mitchison T., Kirschner M.;
RT "Dynamic instability of microtubule growth.";
RL Nature 312:237-242(1984).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2207090; DOI=10.1021/bi00479a022;
RA Stewart R.J., Farrell K.W., Wilson L.;
RT "Role of GTP hydrolysis in microtubule polymerization: evidence for a
RT coupled hydrolysis mechanism.";
RL Biochemistry 29:6489-6498(1990).
RN [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=7704569; DOI=10.1016/s0960-9822(00)00243-8;
RA Drechsel D.N., Kirschner M.W.;
RT "The minimum GTP cap required to stabilize microtubules.";
RL Curr. Biol. 4:1053-1061(1994).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers (PubMed:6504138, PubMed:2207090,
CC PubMed:7704569). Microtubules grow by the addition of GTP-tubulin
CC dimers to the microtubule end, where a stabilizing cap forms. Below the
CC cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of
CC alpha-tubulin (PubMed:6504138, PubMed:2207090, PubMed:7704569).
CC {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138,
CC ECO:0000269|PubMed:7704569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC -!- SUBUNIT: Dimer of alpha and beta chains (PubMed:6504138,
CC PubMed:2207090, PubMed:7704569). A typical microtubule is a hollow
CC water-filled tube with an outer diameter of 25 nm and an inner diameter
CC of 15 nM. Alpha-beta heterodimers associate head-to-tail to form
CC protofilaments running lengthwise along the microtubule wall with the
CC 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. {ECO:0000269|PubMed:2207090,
CC ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138,
CC ECO:0000269|PubMed:7704569}.
CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm
CC motility. {ECO:0000250|UniProtKB:P68369}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group (By
CC similarity). Polyglutamylation plays a key role in microtubule severing
CC by spastin (SPAST). SPAST preferentially recognizes and acts on
CC microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC microtubule lumen. This modification has been correlated with increased
CC microtubule stability, intracellular transport and ciliary assembly.
CC {ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC microtubules and is required for normal mitosis and cytokinesis
CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Nitration of Tyr-452 is irreversible and interferes with normal
CC dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.
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 (MATCAP, VASH1 or VASH2) and tubulin tyrosine
CC ligase (TTL), respectively. {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Tubulin alpha-1D chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation
CC of dynein-dynactin motility via interaction with DCTN1, which brings
CC the dynein-dynactin complex into contact with microtubules. In neurons,
CC tyrosinated tubulins mediate the initiation of retrograde vesicle
CC transport (By similarity). {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Detyrosinated tubulin alpha-1D chain]: Detyrosination is involved
CC in metaphase plate congression by guiding chromosomes during mitosis:
CC detyrosination promotes interaction with CENPE, promoting pole-proximal
CC transport of chromosomes toward the equator (By similarity).
CC Detyrosination increases microtubules-dependent mechanotransduction in
CC dystrophic cardiac and skeletal muscle. In cardiomyocytes,
CC detyrosinated microtubules are required to resist to contractile
CC compression during contraction: detyrosination promotes association
CC with desmin (DES) at force-generating sarcomeres, leading to buckled
CC microtubules and mechanical resistance to contraction (By similarity).
CC {ECO:0000250|UniProtKB:P68373, ECO:0000250|UniProtKB:Q9BQE3}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BC113253; AAI13254.1; -; mRNA.
DR RefSeq; NP_001039875.1; NM_001046410.1.
DR PDB; 1JFF; EM; 3.50 A; A=1-452.
DR PDB; 1SA0; X-ray; 3.58 A; A/C=1-452.
DR PDB; 1SA1; X-ray; 4.20 A; A/C=1-452.
DR PDB; 1TVK; EM; 2.89 A; A=1-440.
DR PDB; 1Z2B; X-ray; 4.10 A; A/C=1-451.
DR PDB; 2WBE; EM; 9.40 A; A=1-452.
DR PDB; 2XRP; EM; 8.20 A; B/D/F/H=1-449.
DR PDB; 3EDL; EM; 28.00 A; F=1-452.
DR PDB; 3IZ0; EM; 8.60 A; A=1-452.
DR PDB; 4AQV; EM; 9.70 A; A=1-452.
DR PDB; 4AQW; EM; 9.50 A; A=1-452.
DR PDB; 4ATU; EM; 8.30 A; B/D/F/H=1-452.
DR PDB; 4ATX; EM; 8.20 A; B=1-452.
DR PDB; 4CK5; EM; 10.00 A; A=1-452.
DR PDB; 4CK6; EM; 9.20 A; A=1-452.
DR PDB; 4CK7; EM; 9.20 A; A=1-452.
DR PDB; 5M5I; EM; 9.30 A; A=1-447.
DR PDB; 5M5L; EM; 9.30 A; A=1-452.
DR PDB; 5M5M; EM; 9.30 A; A=1-452.
DR PDB; 5M5N; EM; 9.30 A; A=1-452.
DR PDB; 5M5O; EM; 9.30 A; A=1-452.
DR PDB; 7RRO; EM; 3.40 A; AA/AC/AE/AG/AI/AK/AM/BA/BC/BE/BG/BI/BK/BM/CA/CC/CE/CG/CI/CK/CM/DA/DC/DE/DG/DI/DK/DM/EC/EE=1-452.
DR PDBsum; 1JFF; -.
DR PDBsum; 1SA0; -.
DR PDBsum; 1SA1; -.
DR PDBsum; 1TVK; -.
DR PDBsum; 1Z2B; -.
DR PDBsum; 2WBE; -.
DR PDBsum; 2XRP; -.
DR PDBsum; 3EDL; -.
DR PDBsum; 3IZ0; -.
DR PDBsum; 4AQV; -.
DR PDBsum; 4AQW; -.
DR PDBsum; 4ATU; -.
DR PDBsum; 4ATX; -.
DR PDBsum; 4CK5; -.
DR PDBsum; 4CK6; -.
DR PDBsum; 4CK7; -.
DR PDBsum; 5M5I; -.
DR PDBsum; 5M5L; -.
DR PDBsum; 5M5M; -.
DR PDBsum; 5M5N; -.
DR PDBsum; 5M5O; -.
DR PDBsum; 7RRO; -.
DR AlphaFoldDB; Q2HJ86; -.
DR EMDB; EMD-16435; -.
DR EMDB; EMD-16436; -.
DR EMDB; EMD-1788; -.
DR EMDB; EMD-2078; -.
DR EMDB; EMD-2095; -.
DR EMDB; EMD-2098; -.
DR EMDB; EMD-21919; -.
DR EMDB; EMD-24664; -.
DR EMDB; EMD-2533; -.
DR EMDB; EMD-2534; -.
DR EMDB; EMD-2535; -.
DR EMDB; EMD-2536; -.
DR EMDB; EMD-2537; -.
DR EMDB; EMD-2538; -.
DR EMDB; EMD-2539; -.
DR EMDB; EMD-2540; -.
DR EMDB; EMD-2541; -.
DR EMDB; EMD-2542; -.
DR EMDB; EMD-25649; -.
DR EMDB; EMD-25658; -.
DR EMDB; EMD-25664; -.
DR EMDB; EMD-25674; -.
DR EMDB; EMD-25897; -.
DR EMDB; EMD-25908; -.
DR EMDB; EMD-3445; -.
DR EMDB; EMD-8546; -.
DR EMDB; EMD-8547; -.
DR SMR; Q2HJ86; -.
DR STRING; 9913.ENSBTAP00000057311; -.
DR PaxDb; 9913-ENSBTAP00000038183; -.
DR PeptideAtlas; Q2HJ86; -.
DR Ensembl; ENSBTAT00000076713.1; ENSBTAP00000057311.1; ENSBTAG00000030973.2.
DR GeneID; 535605; -.
DR KEGG; bta:535605; -.
DR CTD; 535605; -.
DR VEuPathDB; HostDB:ENSBTAG00000030973; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q2HJ86; -.
DR OMA; MAISREC; -.
DR OrthoDB; 899149at2759; -.
DR TreeFam; TF300314; -.
DR EvolutionaryTrace; Q2HJ86; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000030973; Expressed in oviduct epithelium and 89 other cell types or tissues.
DR ExpressionAtlas; Q2HJ86; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd02186; alpha_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF292; TUBULIN ALPHA-1D CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Methylation; Microtubule;
KW Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..452
FT /note="Tubulin alpha-1D chain"
FT /id="PRO_0000288849"
FT CHAIN 1..448
FT /note="Detyrosinated tubulin alpha-1D chain"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT /id="PRO_0000437391"
FT REGION 432..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT COMPBIAS 438..452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 11
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT SITE 452
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 446
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
FT MOD_RES 452
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 211..215
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1TVK"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:1TVK"
FT HELIX 415..432
FT /evidence="ECO:0007829|PDB:1TVK"
FT TURN 433..437
FT /evidence="ECO:0007829|PDB:1TVK"
SQ SEQUENCE 452 AA; 50283 MW; BF41F4296CAC7A56 CRC64;
MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKELIDLVLD
RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGMDSV EGEGEEEEGD EY
//
