ID   TBB_CICAR               Reviewed;         449 AA.
AC   Q39445;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
GN   Name=TUBB;
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Castellana; TISSUE=Etiolated epicotyl;
RX   PubMed=9678576; DOI=10.1023/a:1006013718429;
RA   Munoz F.J., Labrador E., Dopico B.;
RT   "Brassinolides promote the expression of a new Cicer arietinum beta-tubulin
RT   gene involved in the epicotyl elongation.";
RL   Plant Mol. Biol. 37:807-817(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X98406; CAA67056.1; -; mRNA.
DR   RefSeq; NP_001265938.1; NM_001279009.1.
DR   AlphaFoldDB; Q39445; -.
DR   SMR; Q39445; -.
DR   STRING; 3827.XP_004500938.1; -.
DR   PRIDE; Q39445; -.
DR   GeneID; 101506098; -.
DR   KEGG; cam:101506098; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   OrthoDB; 962471at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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..449
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048336"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   449 AA;  50577 MW;  FC3E349166105CBA CRC64;
     MREILHVQGG QCGNQIGSKF WEVICDEHGI DQTGKYISEG GSDTQLERIN VYYNEASGGR
     YVPRAVLMDL EPGTMESIRS GPFGKIFRPD NFVFGQSGAG NNWAKGHYTE GAELIDSVLD
     VVRKEAENCD CLQGFQVCHS LGGGTGSGMG TLLISKIREE YPDRMMLTFS VFPSPKVSDT
     VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLS TPSFGDLNHL ISATMSGVTC
     CLRFPGQLNS DLRKLAVNLI PFPRLHFFMV GFAPLTSRGS QQYVSLTVPE LTQQMWDAKN
     MMCAADPRHG RYLTASAMFR GKMSTKEVDE QIINVQNKNS SYFVEWIPNN VKSSVCDIPP
     KNLKMSSTFI GNSTSIQEMF RRVSEQFTAM FRRKAFLHWY TGEGMDEMEF TEAESNMNDL
     VAEYQQYQDA IAEEEDEYEE EGEEQYDEQ