TBB3_WHEAT
ID TBB3_WHEAT Reviewed; 445 AA.
AC Q9ZRB0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tubulin beta-3 chain;
DE AltName: Full=Beta-3-tubulin;
GN Name=TUBB3;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chinese Spring; TISSUE=Root tip;
RA Segal G., Feldman M.;
RT "Tubb3, a beta-tubulin cDNA from common wheat.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; U76746; AAD10489.1; -; mRNA.
DR AlphaFoldDB; Q9ZRB0; -.
DR SMR; Q9ZRB0; -.
DR STRING; 4565.Traes_6AS_FAFAAFD12.2; -.
DR PRIDE; Q9ZRB0; -.
DR EnsemblPlants; TraesCAD_scaffold_004383_01G000500.1; TraesCAD_scaffold_004383_01G000500.1; TraesCAD_scaffold_004383_01G000500.
DR EnsemblPlants; TraesCLE_scaffold_002142_01G000300.1; TraesCLE_scaffold_002142_01G000300.1; TraesCLE_scaffold_002142_01G000300.
DR EnsemblPlants; TraesCS6D02G130500.2; TraesCS6D02G130500.2; TraesCS6D02G130500.
DR EnsemblPlants; TraesPAR_scaffold_001819_01G000300.1; TraesPAR_scaffold_001819_01G000300.1; TraesPAR_scaffold_001819_01G000300.
DR EnsemblPlants; TraesROB_scaffold_002825_01G000200.1; TraesROB_scaffold_002825_01G000200.1; TraesROB_scaffold_002825_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_028387_01G000200.1; TraesWEE_scaffold_028387_01G000200.1; TraesWEE_scaffold_028387_01G000200.
DR Gramene; TraesCAD_scaffold_004383_01G000500.1; TraesCAD_scaffold_004383_01G000500.1; TraesCAD_scaffold_004383_01G000500.
DR Gramene; TraesCLE_scaffold_002142_01G000300.1; TraesCLE_scaffold_002142_01G000300.1; TraesCLE_scaffold_002142_01G000300.
DR Gramene; TraesCS6D02G130500.2; TraesCS6D02G130500.2; TraesCS6D02G130500.
DR Gramene; TraesPAR_scaffold_001819_01G000300.1; TraesPAR_scaffold_001819_01G000300.1; TraesPAR_scaffold_001819_01G000300.
DR Gramene; TraesROB_scaffold_002825_01G000200.1; TraesROB_scaffold_002825_01G000200.1; TraesROB_scaffold_002825_01G000200.
DR Gramene; TraesWEE_scaffold_028387_01G000200.1; TraesWEE_scaffold_028387_01G000200.1; TraesWEE_scaffold_028387_01G000200.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR OMA; MQLERIN; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q9ZRB0; baseline and differential.
DR Genevisible; Q9ZRB0; TA.
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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000048387"
FT REGION 421..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
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"
SQ SEQUENCE 445 AA; 49960 MW; B2FC10F342F7D913 CRC64;
MREILHIQGG QCGNQIGAKF WEVICDEHGI DQTGKYAGDS DLQLERINVY YNEASGGRFV
PRAVLMDLEP GTMDSLRSGP YGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLATP TFGDLNHLIS ATMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDSKNMM
CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPTG
LSMSSTFVGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
EYQQYQDATA DEEEEYDEEE EEEAA
