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Entry: TBA2_ORYSJ
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ID   TBA2_ORYSJ              Reviewed;         451 AA.
AC   Q53M52; Q43606;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Tubulin alpha-2 chain;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
GN   Name=TUBA; OrderedLocusNames=Os11g0247300, LOC_Os11g14220;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Arborio; TISSUE=Coleoptile;
RA   Maestroni A., Giani S., Breviario D.;
RT   "Rice alpha-tubulin cDNAs.";
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
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 {ECO:0000250}.
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; X91807; CAA62917.1; -; mRNA.
DR   EMBL; AC137924; AAX96762.1; -; Genomic_DNA.
DR   EMBL; DP000010; ABA92352.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT13424.1; -; Genomic_DNA.
DR   RefSeq; XP_015616885.1; XM_015761399.1.
DR   AlphaFoldDB; Q53M52; -.
DR   SMR; Q53M52; -.
DR   STRING; 39947.Q53M52; -.
DR   PaxDb; 39947-Q53M52; -.
DR   EnsemblPlants; Os11t0247300-01; Os11t0247300-01; Os11g0247300.
DR   GeneID; 4350197; -.
DR   Gramene; Os11t0247300-01; Os11t0247300-01; Os11g0247300.
DR   KEGG; osa:4350197; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; Q53M52; -.
DR   OMA; ESCYDIC; -.
DR   OrthoDB; 1206011at2759; -.
DR   PlantReactome; R-OSA-9035605; Regulation of seed size.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   ExpressionAtlas; Q53M52; baseline and differential.
DR   Genevisible; Q53M52; OS.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd02186; alpha_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF489; TUBULIN ALPHA-2 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Microtubule; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Tubulin alpha-2 chain"
FT                   /id="PRO_0000247465"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   SITE            451
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        74
FT                   /note="V -> M (in Ref. 1; CAA62917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="L -> V (in Ref. 1; CAA62917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="L -> R (in Ref. 1; CAA62917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="V -> A (in Ref. 1; CAA62917)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   451 AA;  49737 MW;  4EB46E096C684F0B CRC64;
     MRECISIHIG QAGIQVGNAC WELYCLEHGI QPDGQMPGDK TVGGGDDAFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GDYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
     RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
     VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA
     SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
     SVVPGGDLAK VQRAVCMISN STSVVEVFSR IDIKFDLMYS KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGSEFD DGDEGDEGDE Y
//
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