ID   TBA_TORMA               Reviewed;         451 AA.
AC   P36220;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tubulin alpha chain;
DE   AltName: Full=Alpha T6;
DE   Contains:
DE     RecName: Full=Detyrosinated tubulin alpha chain;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric organ;
RX   PubMed=7607545; DOI=10.1016/0378-1119(95)00109-j;
RA   Canals J.M., Ruiz-Avila L., Aguado F., Majo G., Marsal J.;
RT   "Cloning characterization and expression of the cDNA encoding a neuron-
RT   specific alpha-tubulin isoform highly represented in the electric lobe of
RT   Torpedo marmorata.";
RL   Gene 158:219-223(1995).
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.
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 (vash1 or vash2) and tubulin tyrosine ligase
CC       (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; X71980; CAA50802.1; -; mRNA.
DR   PIR; JC4133; JC4133.
DR   PIR; S33517; S33517.
DR   AlphaFoldDB; P36220; -.
DR   SMR; P36220; -.
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:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond;
KW   Microtubule; Nucleotide-binding.
FT   CHAIN           1..451
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048232"
FT   CHAIN           1..450
FT                   /note="Detyrosinated tubulin alpha chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT                   /id="PRO_0000437409"
FT   REGION          432..451
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   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            451
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   MOD_RES         445
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P68369"
SQ   SEQUENCE   451 AA;  50168 MW;  83838E659EF5FA49 CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVSE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y