TBB1_ARATH
ID TBB1_ARATH Reviewed; 447 AA.
AC P12411; Q8GZ16; Q9SYQ7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=TUBB1; Synonyms=TUB1; OrderedLocusNames=At1g75780;
GN ORFNames=F10A5.3, T4O12.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3384336; DOI=10.1016/0378-1119(88)90548-3;
RA Oppenheimer D.G., Haas N.A., Silflow C.D., Snustad D.P.;
RT "The beta-tubulin gene family of Arabidopsis thaliana: preferential
RT accumulation of the beta 1 transcript in roots.";
RL Gene 63:87-102(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10080719; DOI=10.1023/a:1006127302671;
RA Williams R.W., Clark S.E., Meyerowitz E.M.;
RT "Genetic and physical characterization of a region of Arabidopsis
RT chromosome 1 containing the CLAVATA1 gene.";
RL Plant Mol. Biol. 39:171-176(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(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 -!- TISSUE SPECIFICITY: Accumulates predominantly in roots.
CC -!- MISCELLANEOUS: There are nine genes coding for beta-tubulin.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD02498.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M20405; AAA32893.1; -; Genomic_DNA.
DR EMBL; AF049870; AAD02498.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006434; AAF87106.1; -; Genomic_DNA.
DR EMBL; AC007396; AAF26774.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE35758.1; -; Genomic_DNA.
DR EMBL; AK117262; BAC41937.1; -; mRNA.
DR EMBL; BT005372; AAO63436.1; -; mRNA.
DR PIR; JT0275; UBMUBM.
DR RefSeq; NP_177706.1; NM_106228.3.
DR AlphaFoldDB; P12411; -.
DR SMR; P12411; -.
DR BioGRID; 29130; 6.
DR STRING; 3702.AT1G75780.1; -.
DR PaxDb; P12411; -.
DR PRIDE; P12411; -.
DR ProteomicsDB; 226581; -.
DR EnsemblPlants; AT1G75780.1; AT1G75780.1; AT1G75780.
DR GeneID; 843911; -.
DR Gramene; AT1G75780.1; AT1G75780.1; AT1G75780.
DR KEGG; ath:AT1G75780; -.
DR Araport; AT1G75780; -.
DR TAIR; locus:2005724; AT1G75780.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P12411; -.
DR OMA; YEEEAPD; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P12411; -.
DR PRO; PR:P12411; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P12411; baseline and differential.
DR Genevisible; P12411; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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 GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IEP:TAIR.
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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048321"
FT REGION 420..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 210
FT /note="D -> G (in Ref. 5; BAC41937 and 6; AAO63436)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="F -> S (in Ref. 5; BAC41937 and 6; AAO63436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50217 MW; E36D5A915F75C852 CRC64;
MREILHVQGG QCGNQIGSKF WEVICDEHGV DPTGRYNGDS ADLQLERINV YYNEASGGRY
VPRAVLMDLE PGTMDSIRSG PYGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELIDAVLDV
VRKEAENCDC LQGFQVCHSL GGGTGSGMGT LLISKIREEY PDRMMLTFSV FPSPKVSDTV
VEPYNATLSV HQLVENADEC MVLDNEALYD ICFRTLKLST PSFGDLNHLI SATMSGVTCS
LRFPGQLNSD LRKLAVNLIP FPRLHFFMVG FAPLTSRGSQ QYISLTVPEL TQQMWDAKNM
MCAADPRHGR YLTASAMFRG KMSTKEVDEQ ILNVQNKNSS YFVEWIPNNV KSSVCDIPPT
GIKMASTFVG NSTSIQEMFR RVSEQFTAMF RRKAFLHWYT GEGMDEMEFT EAESNMNDLV
SEYQQYQDAT ADEEDEYDEE EEQVYES
