TBA3_MAIZE
ID TBA3_MAIZE Reviewed; 450 AA.
AC P22275;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tubulin alpha-3 chain;
DE AltName: Full=Alpha-3-tubulin;
GN Name=TUBA3; Synonyms=TUA3;
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.
RX PubMed=1701749; DOI=10.1016/0378-1119(90)90388-8;
RA Montoliu L., Puigdomenech P., Rigau J.;
RT "The Tub alpha 3 gene from Zea mays: structure and expression in dividing
RT plant tissues.";
RL Gene 94:201-207(1990).
RN [2]
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; M60171; AAA33518.1; -; Genomic_DNA.
DR EMBL; X63176; CAA44861.1; -; mRNA.
DR PIR; JN0105; JN0105.
DR RefSeq; NP_001105440.1; NM_001111970.1.
DR AlphaFoldDB; P22275; -.
DR SMR; P22275; -.
DR STRING; 4577.AC195340.3_FGP001; -.
DR PaxDb; P22275; -.
DR PRIDE; P22275; -.
DR EnsemblPlants; Zm00001eb213760_T001; Zm00001eb213760_P001; Zm00001eb213760.
DR GeneID; 542395; -.
DR Gramene; Zm00001eb213760_T001; Zm00001eb213760_P001; Zm00001eb213760.
DR KEGG; zma:542395; -.
DR MaizeGDB; 17141; -.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR OMA; ADSAENC; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; P22275; baseline and differential.
DR Genevisible; P22275; ZM.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin alpha-3 chain"
FT /id="PRO_0000048190"
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 MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 49561 MW; 1BAB7E7C16615224 CRC64;
MRECISVHIG QAGIQVGNAC WELYCLEHGI QPDGQVPGDK TAGHHDDAFS TFFSQTGAGK
HVPRAIFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVE YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV SILLDNEAIY DICRRSLDIE RPNYSNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISSAK AFHEQLSVAE ITSSAFEPAS
MMVKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQAP
TVVPGADLAK VQRAVCMISN STSVVEVFSR INSKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVAAEGG SDDGDEEEEY
