TBB3_ORYSJ
ID TBB3_ORYSJ Reviewed; 446 AA.
AC Q40665; A3BEJ5; Q652I6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Tubulin beta-3 chain;
DE AltName: Full=Beta-3-tubulin;
GN Name=TUBB3; Synonyms=RTUB-2, TUB3;
GN OrderedLocusNames=Os06g0671900, LOC_Os06g46000;
GN ORFNames=OsJ_22330 {ECO:0000312|EMBL:EAZ37984.1}, OSJNBa0032M14.15,
GN P0485A07.25;
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] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC TISSUE=Leaf;
RX PubMed=7858231; DOI=10.1007/bf00019507;
RA Kang M.S., Choi Y.J., Kim M.C., Lim C.O., Hwang I., Cho M.J.;
RT "Isolation and characterization of two beta-tubulin cDNA clones from
RT rice.";
RL Plant Mol. Biol. 26:1975-1979(1994).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX PubMed=14634157; DOI=10.1093/pcp/pcg150;
RA Yoshikawa M., Yang G., Kawaguchi K., Komatsu S.;
RT "Expression analyses of beta-tubulin isotype genes in rice.";
RL Plant Cell Physiol. 44:1202-1207(2003).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q40665-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q40665-2; Sequence=VSP_015369;
CC -!- TISSUE SPECIFICITY: Expressed in roots, second node, leaf sheaths, and
CC suspension cultured cells. {ECO:0000269|PubMed:14634157}.
CC -!- DEVELOPMENTAL STAGE: Expressed in shoots of 4 day old dark-grown
CC seedlings. {ECO:0000269|PubMed:7858231}.
CC -!- INDUCTION: Down-regulated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:14634157}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; L33263; AAA67322.1; -; mRNA.
DR EMBL; AP005192; BAD46004.1; -; Genomic_DNA.
DR EMBL; AP005610; BAD46281.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99085.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ37984.1; -; Genomic_DNA.
DR EMBL; AK069237; BAG91329.1; -; mRNA.
DR PIR; S52008; S52008.
DR RefSeq; XP_015643315.1; XM_015787829.1. [Q40665-1]
DR AlphaFoldDB; Q40665; -.
DR SMR; Q40665; -.
DR STRING; 4530.OS06T0671900-01; -.
DR PaxDb; Q40665; -.
DR PRIDE; Q40665; -.
DR EnsemblPlants; Os06t0671900-01; Os06t0671900-01; Os06g0671900. [Q40665-1]
DR GeneID; 4341810; -.
DR Gramene; Os06t0671900-01; Os06t0671900-01; Os06g0671900. [Q40665-1]
DR KEGG; osa:4341810; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q40665; -.
DR OMA; MQLERIN; -.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q40665; 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; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..446
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000048365"
FT REGION 421..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 378..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7858231"
FT /id="VSP_015369"
FT CONFLICT 15
FT /note="Q -> K (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> V (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="N -> NN (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="M -> S (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> Y (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="SV -> C (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> R (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="I -> M (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="R -> W (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="D -> DPG (in Ref. 1; AAA67322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 50121 MW; B66C7C6E160AF129 CRC64;
MREILHIQGG QCGNQIGAKF WEVICDEHGI DHTGKYSGDS DLQLERINVY YNEASGGRYV
PRAVLMDLEP GTMDSVRSGP YGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLATP TFGDLNHLIS ATMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDAKNMM
CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPIG
LKMASTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
EYQQYQDATA EEEDYEEEEE DEEVAA
