ID   TBB6_GOSHI              Reviewed;         450 AA.
AC   Q6VAF6;
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-6 chain;
DE   AltName: Full=Beta-6-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; AY345608; AAQ92666.1; -; mRNA.
DR   AlphaFoldDB; Q6VAF6; -.
DR   SMR; Q6VAF6; -.
DR   STRING; 3635.Q6VAF6; -.
DR   PRIDE; Q6VAF6; -.
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   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..450
FT                   /note="Tubulin beta-6 chain"
FT                   /id="PRO_0000048349"
FT   REGION          429..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   450 AA;  50493 MW;  E1AAB13B4DDF8A49 CRC64;
     MREILHVQGG QCGNQIGSKF WEVICDEHGV DPTGKYNGDG SSDIQLERID VYYNEASGGR
     YVPRAVLMDL EPGTMDSIRS GPIGQIFRPD NFVFGQSGAG NNWAKGHYTE GAELIDAVLD
     VVRKEAENCD CLQGFQVCHS LGGGTGSGMG TLLISKIREE YPDRMMMTFS VFPSPKVSDT
     VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLT TPSFGDLNHL ISATMSGVTC
     CLRFPGQLNS DLRKLAVNLI PFPRLHFFMV GFAPLTSRGS QQYVSLTVPE LTQQMWDAKN
     MMCAADPRHG RYLTASAMFR GKMSTKEVDE QMMNVQNKNS SYFVEWIPNN VKSSVCDIPP
     RGLKTSSTFI GNSTSIQEMF RRVSEQFTAM FRRKAFLHWY TGEGMDEMEF TEAESNMNDL
     VAEYQQYQDA TVEDEEEYEG EEGLDENYET