TBB4_ARATH
ID TBB4_ARATH Reviewed; 444 AA.
AC P24636; Q9FKV4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Tubulin beta-4 chain;
DE AltName: Full=Beta-4-tubulin;
GN Name=TUBB4; Synonyms=TUB4; OrderedLocusNames=At5g44340; ORFNames=K9L2.12;
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.
RX AGRICOLA=IND92001182; DOI=10.1007/BF00016147;
RA Marks M.D., West J., Weeks D.P.;
RT "The relatively large beta-tubulin gene family of Arabidopsis contains a
RT member with an unusual transcribed 5' noncoding sequence.";
RL Plant Mol. Biol. 10:91-104(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
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 -!- MISCELLANEOUS: There are nine genes coding for beta-tubulin.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M21415; AAA32757.1; -; Genomic_DNA.
DR EMBL; AB011475; BAB10119.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95098.1; -; Genomic_DNA.
DR EMBL; AY059075; AAL15181.1; -; mRNA.
DR EMBL; AY035141; AAK59645.1; -; mRNA.
DR PIR; S68122; S68122.
DR RefSeq; NP_199247.1; NM_123801.2.
DR AlphaFoldDB; P24636; -.
DR SMR; P24636; -.
DR BioGRID; 19709; 5.
DR IntAct; P24636; 3.
DR MINT; P24636; -.
DR STRING; 3702.AT5G44340.1; -.
DR iPTMnet; P24636; -.
DR MetOSite; P24636; -.
DR PaxDb; P24636; -.
DR PRIDE; P24636; -.
DR ProteomicsDB; 234156; -.
DR EnsemblPlants; AT5G44340.1; AT5G44340.1; AT5G44340.
DR GeneID; 834459; -.
DR Gramene; AT5G44340.1; AT5G44340.1; AT5G44340.
DR KEGG; ath:AT5G44340; -.
DR Araport; AT5G44340; -.
DR TAIR; locus:2158755; AT5G44340.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P24636; -.
DR OMA; YLIDNEA; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P24636; -.
DR PRO; PR:P24636; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P24636; baseline and differential.
DR Genevisible; P24636; AT.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0045298; C:tubulin complex; ISS: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; ISS:TAIR.
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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..444
FT /note="Tubulin beta-4 chain"
FT /id="PRO_0000048323"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 313
FT /note="A -> R (in Ref. 1; AAA32757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 49823 MW; EEDC37FE26D1E80D CRC64;
MREILHIQGG QCGNQIGAKF WEVICDEHGI DHTGQYVGDS PLQLERIDVY FNEASGGKYV
PRAVLMDLEP GTMDSLRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAENSDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMMTFSVF PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLANP TFGDLNHLIS ATMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YSALSVPELT QQMWDAKNMM
CAADPRHGRY LTASAVFRGK LSTKEVDEQM MNIQNKNSSY FVEWIPNNVK SSVCDIAPKG
LKMASTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
EYQQYQDATA GEEEYEEEEE EYET
