TBA1_CHICK
ID TBA1_CHICK Reviewed; 412 AA.
AC P02552;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tubulin alpha-1 chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1 chain;
DE Flags: Fragment;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7464932; DOI=10.1038/289650a0;
RA Valenzuela P., Quiroga M., Zaldivar J., Rutter W.J., Kirschner M.W.,
RA Cleveland D.W.;
RT "Nucleotide and corresponding amino acid sequences encoded by alpha and
RT beta tubulin mRNAs.";
RL Nature 289:650-655(1981).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=7328649; DOI=10.1016/0022-2836(81)90223-0;
RA Lemischka I.R., Farmer S., Racaniello V.R., Sharp P.A.;
RT "Nucleotide sequence and evolution of a mammalian alpha-tubulin messenger
RT RNA.";
RL J. Mol. Biol. 151:101-120(1981).
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 -!- 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: 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-1 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-1 chain]: Detyrosination is involved
CC in metaphase plate congression by guiding chromosomes during mitosis
CC (By 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 -!- MISCELLANEOUS: There are at least seven alpha tubulin genes (alpha-1 to
CC alpha-6, and alpha-8), and a pseudogene (alpha-7) in chicken.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; V00388; CAA23686.1; -; mRNA.
DR PIR; A02968; UBCHA.
DR AlphaFoldDB; P02552; -.
DR SMR; P02552; -.
DR PaxDb; P02552; -.
DR PRIDE; P02552; -.
DR VEuPathDB; HostDB:LOC100857858; -.
DR PhylomeDB; P02552; -.
DR Proteomes; UP000000539; Unplaced.
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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
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 Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW Isopeptide bond; Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN <1..412
FT /note="Tubulin alpha-1 chain"
FT /id="PRO_0000048147"
FT CHAIN <1..411
FT /note="Detyrosinated tubulin alpha-1 chain"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT /id="PRO_0000437404"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 412
FT /note="Involved in polymerization"
FT MOD_RES 406
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
FT NON_TER 1
SQ SEQUENCE 412 AA; 45901 MW; FF55DAEF6AF78682 CRC64;
ETIGGGDDSF NTFFSETGAG KHVPRAVFVD LEPTVIDEVR TGTYRQLFHP EQLITGKEDA
ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFSVFH SFGGGTGSGF TSLLMERLSV
DYGKKSKLEF SIYPARQVST AVVEPYNSIL TTHTTLEHSD CAFMVDNEAI YDICRRNLDI
ERPTYTNLNR LIGQIVSSIT ASLRFDGALN VDLTEFQTNL VPYPRIHFPL ATYAPVISAE
KAYHEQLSVA EITNACFEPA NQMVKCDPRH GKYMACCLLY RGDVVPKDVN AAIATIKTKR
TIQFVDWCPT GFKVGINYQP PTVVPGGDLA KVQRAVCMLS NTTAIAEAWA RLDHKFDLMY
AKRAFVHWYV GEGMEEGEFS EAREDMAALE KDYEEVGVDS VEGEGEEEGE EY
