TBA1_MAIZE
ID TBA1_MAIZE Reviewed; 451 AA.
AC P14640;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tubulin alpha-1 chain;
DE AltName: Full=Alpha-1-tubulin;
GN Name=TUBA1; Synonyms=TUA1;
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 [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 64A; TISSUE=Root;
RX PubMed=1713800; DOI=10.1007/bf00015650;
RA Montoliu L., Rigau J., Puigdomenech P.;
RT "A tandem of alpha-tubulin genes preferentially expressed in radicular
RT tissues from Zea mays.";
RL Plant Mol. Biol. 14:1-15(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-451.
RX PubMed=2269365; DOI=10.1016/0014-5793(90)80802-p;
RA Montoliu L., Rigau J., Puigdomenech P.;
RT "Multiple polyadenylation sites are active in the alpha 1-tubulin gene from
RT Zea mays.";
RL FEBS Lett. 277:29-32(1990).
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; X15704; CAA33734.1; -; Genomic_DNA.
DR PIR; S15773; S15773.
DR PIR; S28980; S28980.
DR RefSeq; NP_001295436.1; NM_001308507.1.
DR AlphaFoldDB; P14640; -.
DR SMR; P14640; -.
DR STRING; 4577.GRMZM2G152466_P01; -.
DR PaxDb; P14640; -.
DR PRIDE; P14640; -.
DR EnsemblPlants; Zm00001eb055850_T001; Zm00001eb055850_P001; Zm00001eb055850.
DR GeneID; 100037751; -.
DR Gramene; Zm00001eb055850_T001; Zm00001eb055850_P001; Zm00001eb055850.
DR KEGG; zma:100037751; -.
DR MaizeGDB; 17141; -.
DR eggNOG; KOG1376; Eukaryota.
DR OMA; KVGICYQ; -.
DR OrthoDB; 514396at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; P14640; baseline and differential.
DR Genevisible; P14640; 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 3: Inferred from homology;
KW Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin alpha-1 chain"
FT /id="PRO_0000048188"
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"
SQ SEQUENCE 451 AA; 49731 MW; 32815A2055702414 CRC64;
MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDDAFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV AILLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
SVVPGGDLAK VQRAVCMISN STSVVEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGAEFD EGEDGDEGDE Y
