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TBA1_ORYSJ
ID   TBA1_ORYSJ              Reviewed;         450 AA.
AC   P28752; Q6ZL40;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Tubulin alpha-1 chain;
GN   Name=TUBA1; OrderedLocusNames=Os07g0574800, LOC_Os07g38730;
GN   ORFNames=OJ1562_B11.119, OJ1699_E05.40;
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. Nakdong; TISSUE=Anther;
RA   An G., Finkel D., Chen W., Kim S., Kim Y.;
RT   "Nucleotide sequence of alpha 1 tubulin gene from rice.";
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Arborio; TISSUE=Coleoptile;
RX   PubMed=9375785; DOI=10.1016/s0167-4781(97)00110-3;
RA   Qin X., Giani S., Breviario D.;
RT   "Molecular cloning of three rice alpha-tubulin isotypes: differential
RT   expression in tissues and during flower development.";
RL   Biochim. Biophys. Acta 1354:19-23(1997).
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).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-6.
RC   STRAIN=cv. Nipponbare; TISSUE=Sheath;
RX   PubMed=14681440; DOI=10.1093/nar/gkh020;
RA   Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT   "Rice proteome database based on two-dimensional polyacrylamide gel
RT   electrophoresis: its status in 2003.";
RL   Nucleic Acids Res. 32:D388-D392(2004).
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; Z11931; CAA77988.1; -; mRNA.
DR   EMBL; X91808; CAA62918.1; -; mRNA.
DR   EMBL; AP003758; BAD30236.1; -; Genomic_DNA.
DR   EMBL; AP003845; BAC83168.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT02277.1; -; Genomic_DNA.
DR   PIR; S20758; S20758.
DR   RefSeq; XP_015647082.1; XM_015791596.1.
DR   AlphaFoldDB; P28752; -.
DR   SMR; P28752; -.
DR   BioGRID; 812731; 1.
DR   STRING; 4530.OS07T0574800-02; -.
DR   PaxDb; P28752; -.
DR   PRIDE; P28752; -.
DR   EnsemblPlants; Os07t0574800-01; Os07t0574800-01; Os07g0574800.
DR   EnsemblPlants; Os07t0574800-02; Os07t0574800-02; Os07g0574800.
DR   GeneID; 4343694; -.
DR   Gramene; Os07t0574800-01; Os07t0574800-01; Os07g0574800.
DR   Gramene; Os07t0574800-02; Os07t0574800-02; Os07g0574800.
DR   KEGG; osa:4343694; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; P28752; -.
DR   OMA; VDNEACY; -.
DR   OrthoDB; 514396at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   ExpressionAtlas; P28752; baseline and differential.
DR   Genevisible; P28752; 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: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; 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   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha-1 chain"
FT                   /id="PRO_0000048206"
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;  49654 MW;  6CBD2FCFAD47EC8F CRC64;
     MREIISIHIG QAGIQVGNAC WELYCLEHGI EPDGTMPSDT TVGVAHDAFN TFFSETGAGK
     HVPRAIFVDL EPTVIDEVRT GSYRQLFHPE 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 DDENDDGEDY
 
 
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