ID   TBA1_HORVU              Reviewed;         450 AA.
AC   Q43473;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tubulin alpha-1 chain;
GN   Name=TUBA1; Synonyms=ATUB1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Igri; TISSUE=Leaf;
RX   PubMed=11430434; DOI=10.1023/a:1010648519206;
RA   Schroeder J., Stenger H., Wernicke W.;
RT   "Alpha-tubulin genes are differentially expressed during leaf cell
RT   development in barley (Hordeum vulgare L.).";
RL   Plant Mol. Biol. 45:723-730(2001).
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: 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 (TTCP) and tubulin tyrosine ligase (TTL),
CC       respectively. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X99623; CAA67942.1; -; mRNA.
DR   AlphaFoldDB; Q43473; -.
DR   SMR; Q43473; -.
DR   EnsemblPlants; HORVU.MOREX.r2.2HG0109010.1; HORVU.MOREX.r2.2HG0109010.1; HORVU.MOREX.r2.2HG0109010.
DR   EnsemblPlants; HORVU.MOREX.r2.2HG0109010.1.mrna1; HORVU.MOREX.r2.2HG0109010.1.mrna1; HORVU.MOREX.r2.2HG0109010.1.
DR   Gramene; HORVU.MOREX.r2.2HG0109010.1; HORVU.MOREX.r2.2HG0109010.1; HORVU.MOREX.r2.2HG0109010.
DR   Gramene; HORVU.MOREX.r2.2HG0109010.1.mrna1; HORVU.MOREX.r2.2HG0109010.1.mrna1; HORVU.MOREX.r2.2HG0109010.1.
DR   OMA; EGTHIND; -.
DR   ExpressionAtlas; Q43473; baseline and differential.
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; IPR013838; Beta-tubulin_BS.
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   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha-1 chain"
FT                   /id="PRO_0000048182"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            450
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  49597 MW;  58DBEC9328ECFCED CRC64;
     MREIISIHIG QAGIQVGNAC WELYCLEHGI NQDGTMPSDT TVGVAHDAFN TFFSETGAGK
     HVPRAIFVDL EPTVIDEVRT GAYRQLFHPE QLISGKEDAA NNFARGHYTV GKEIVDLCLD
     RVRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA
     VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL ISQIISSLTT
     SLRFDGAINV DVTEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVPE ITNAVFEPSS
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT VQFVDWCPTG FKCGINYQPP
     SVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGAEGA DDEGDEGDDY