ID TBA4A_BOVIN Reviewed; 448 AA.
AC P81948; Q17QT1; Q5E986;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Tubulin alpha-4A chain;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE AltName: Full=Alpha-tubulin 1;
DE AltName: Full=Tubulin alpha-1 chain;
GN Name=TUBA4A; Synonyms=TUBA1;
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 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 430-448.
RC TISSUE=Brain cortex;
RX PubMed=9571153; DOI=10.1006/bbrc.1998.8426;
RA Banerjee A., Kasmala L.T.;
RT "Differential assembly kinetics of alpha-tubulin isoforms in the presence
RT of paclitaxel.";
RL Biochem. Biophys. Res. Commun. 245:349-351(1998).
RN [4]
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 [5]
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 [6]
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 -!- INTERACTION:
CC P81948; P46065: GUCA1A; NbExp=2; IntAct=EBI-6943159, EBI-6943108;
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:P68368}.
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:P68368,
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: Although this tubulin does not encode a C-terminal tyrosine, a C-
CC terminal tyrosine can be added post-translationally by the tubulin
CC tyrosine ligase (TTL). It can then undergo a detyrosination cycle by
CC the tubulin tyrosine carboxypeptidase (KIAA0895L/MATCAP).
CC {ECO:0000250|UniProtKB:P68366}.
CC -!- MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BT021034; AAX09051.1; -; mRNA.
DR EMBL; BC118199; AAI18200.1; -; mRNA.
DR RefSeq; NP_001071626.1; NM_001078158.1.
DR AlphaFoldDB; P81948; -.
DR SMR; P81948; -.
DR CORUM; P81948; -.
DR IntAct; P81948; 8.
DR MINT; P81948; -.
DR STRING; 9913.ENSBTAP00000065307; -.
DR PaxDb; 9913-ENSBTAP00000003192; -.
DR PeptideAtlas; P81948; -.
DR Ensembl; ENSBTAT00000085322.1; ENSBTAP00000065307.1; ENSBTAG00000030974.2.
DR GeneID; 777775; -.
DR KEGG; bta:777775; -.
DR CTD; 7277; -.
DR VEuPathDB; HostDB:ENSBTAG00000030974; -.
DR VGNC; VGNC:49986; TUBA4A.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000183165; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P81948; -.
DR OMA; RRVTDNC; -.
DR OrthoDB; 899149at2759; -.
DR TreeFam; TF300314; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR Reactome; R-BTA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-BTA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-BTA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-BTA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-BTA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-BTA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-BTA-5610787; Hedgehog 'off' state.
DR Reactome; R-BTA-5617833; Cilium Assembly.
DR Reactome; R-BTA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-BTA-5620924; Intraflagellar transport.
DR Reactome; R-BTA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-BTA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-BTA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-BTA-68877; Mitotic Prometaphase.
DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-BTA-8854518; AURKA Activation by TPX2.
DR Reactome; R-BTA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-BTA-9646399; Aggrephagy.
DR Reactome; R-BTA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-BTA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-BTA-983189; Kinesins.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000030974; Expressed in choroid plexus and 104 other cell types or tissues.
DR ExpressionAtlas; P81948; 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:SF53; TUBULIN ALPHA-4A 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 Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Hydrolase; Magnesium; Metal-binding; Methylation; Microtubule;
KW Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..448
FT /note="Tubulin alpha-4A chain"
FT /id="PRO_0000048115"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
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 MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68366"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68366"
FT MOD_RES 83
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68368"
FT MOD_RES 432
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIF6"
SQ SEQUENCE 448 AA; 49924 MW; C00ED90A183FE8F2 CRC64;
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFCETGAGK
HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD
RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGIDSY EDEDEGEE
//
