ID   TBA_XENLA               Reviewed;         449 AA.
AC   P08537; Q4V850;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Tubulin alpha chain;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE   Contains:
DE     RecName: Full=Detyrosinated tubulin alpha chain;
GN   Name=tuba; Synonyms=tuba1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=3342025; DOI=10.1042/bj2490465;
RA   Smith D.J.;
RT   "The complete sequence of a frog alpha-tubulin gene and its regulated
RT   expression in mouse L-cells.";
RL   Biochem. J. 249:465-472(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin.
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. 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   -!- 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. The precise function of polyglycylation is still unclear.
CC       {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). {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: 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 chain]: Tyrosination promotes microtubule
CC       interaction with CAP-Gly microtubule plus-end tracking proteins.
CC       Tyrosinated tubulins regulate the initiation of dynein-driven motility.
CC       {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: [Detyrosinated tubulin alpha chain]: Detyrosination is involved in
CC       metaphase plate congression by guiding chromosomes during mitosis (By
CC       similarity). Detyrosination increases microtubules-dependent
CC       mechanotransduction in dystrophic cardiac and skeletal muscle. In
CC       cardiomyocytes, detyrosinated microtubules are required to resist to
CC       contractile compression during contraction (By similarity).
CC       {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X07046; CAA30094.1; -; mRNA.
DR   EMBL; X07045; CAA30093.1; -; Genomic_DNA.
DR   EMBL; BC097546; AAH97546.1; -; mRNA.
DR   EMBL; BC106207; AAI06208.1; -; mRNA.
DR   PIR; S00253; S00253.
DR   RefSeq; NP_001095253.1; NM_001101783.1.
DR   RefSeq; NP_001165669.1; NM_001172198.1.
DR   AlphaFoldDB; P08537; -.
DR   SMR; P08537; -.
DR   BioGRID; 100638; 1.
DR   IntAct; P08537; 2.
DR   DNASU; 100337592; -.
DR   GeneID; 100337592; -.
DR   GeneID; 399313; -.
DR   KEGG; xla:100337592; -.
DR   AGR; Xenbase:XB-GENE-6464328; -.
DR   CTD; 100337592; -.
DR   CTD; 399313; -.
DR   Xenbase; XB-GENE-866172; XB22063824.L.
DR   OMA; TTPECIS; -.
DR   OrthoDB; 899149at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 100337592; Expressed in brain and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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:SF298; TUBULIN ALPHA-1C 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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Microtubule; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..449
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048238"
FT   CHAIN           1..448
FT                   /note="Detyrosinated tubulin alpha chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT                   /id="PRO_0000437410"
FT   REGION          430..449
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   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            449
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P41351,
FT                   ECO:0000250|UniProtKB:Q71U36"
FT   CONFLICT        154
FT                   /note="M -> L (in Ref. 1; CAA30094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   449 AA;  49879 MW;  9A5B8497FA27FF8C CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAD ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGADSA DAEDEGEEY
//