ID   TBA4_MAIZE              Reviewed;          61 AA.
AC   P33626;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tubulin alpha-4 chain;
DE   AltName: Full=Alpha-4-tubulin;
DE   Flags: Fragments;
GN   Name=TUBA4; Synonyms=TUA4;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73; TISSUE=Shoot;
RX   PubMed=1522603; DOI=10.1016/0022-2836(92)90683-b;
RA   Villemur R., Joyce C.M., Haas N.A., Goddard R.H., Kopczak S.D.,
RA   Hussey P.J., Snustad D.P., Silflow C.D.;
RT   "Alpha-tubulin gene family of maize (Zea mays L.). Evidence for two ancient
RT   alpha-tubulin genes in plants.";
RL   J. Mol. Biol. 227:81-96(1992).
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   -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and
CC       affects affinity and processivity of microtubule motors. This
CC       modification has a role in multiple cellular functions, ranging from
CC       cell motility, cell cycle progression or cell differentiation to
CC       intracellular trafficking and signaling (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X63179; CAA44864.1; -; mRNA.
DR   EMBL; X63180; CAA44865.1; -; mRNA.
DR   AlphaFoldDB; P33626; -.
DR   SMR; P33626; -.
DR   MaizeGDB; 17141; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   HOGENOM; CLU_207403_1_0_1; -.
DR   Proteomes; UP000007305; Unplaced.
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:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..61
FT                   /note="Tubulin alpha-4 chain"
FT                   /id="PRO_0000048191"
FT   REGION          35..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            61
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   61 AA;  6532 MW;  C607503FE066E128 CRC64;
     MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDAEFD EGEDGDEGDE
     Y