ID   TBB3_GOSHI              Reviewed;         430 AA.
AC   Q6VAF8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Beta-3-tubulin;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Feng J.-X., Wei G., Wang L., Ji S.-J., Zhang T.-Z., Zhu Y.-X.;
RT   "Cloning and expression of nine tubulin genes from elongating cotton fiber
RT   cells.";
RL   Submitted (JUL-2003) 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; AY345606; AAQ92664.1; -; mRNA.
DR   AlphaFoldDB; Q6VAF8; -.
DR   SMR; Q6VAF8; -.
DR   Proteomes; UP000189702; Genome assembly.
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   GO; GO:0009741; P:response to brassinosteroid; IEP:AgBase.
DR   GO; GO:0090378; P:seed trichome elongation; IMP:AgBase.
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..430
FT                   /note="Tubulin beta-3 chain"
FT                   /id="PRO_0000048347"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   430 AA;  48197 MW;  7800A2D48381CC18 CRC64;
     MREILHVQGG QCGNQIGSKF WEVVCDEHGI DPTGRYIGSS DLQLERVNVY YNEASCGRFV
     PRAVLMDLEP GTMDSVRTGP YGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDAVLDVV
     RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTTP SFGDLNHLIS ATMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDAKNMM
     CAADPRHGRY LTASAMFRGK MSTKEADEQM INVQNKNSSY FVEWIPNNVK SSVCDIPPRG
     LSMASTFVGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     GYQQIPGRYR