ID A0A1S2X7K7_CICAR Unreviewed; 449 AA.
AC A0A1S2X7K7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN Name=TUBB {ECO:0000313|RefSeq:NP_001265938.1};
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 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:NP_001265938.1};
RN [1] {ECO:0000313|RefSeq:NP_001265938.1}
RP NUCLEOTIDE SEQUENCE.
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).
RN [2] {ECO:0000313|RefSeq:NP_001265938.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. {ECO:0000256|ARBA:ARBA00034296,
CC ECO:0000256|RuleBase:RU000352}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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. {ECO:0000256|ARBA:ARBA00011747,
CC ECO:0000256|RuleBase:RU000352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR RefSeq; NP_001265938.1; NM_001279009.1.
DR AlphaFoldDB; A0A1S2X7K7; -.
DR SMR; A0A1S2X7K7; -.
DR GeneID; 101506098; -.
DR KEGG; cam:101506098; -.
DR OrthoDB; 3124041at2759; -.
DR Proteomes; UP000087171; Chromosome Ca5.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF116; TUBULIN BETA-1 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171}.
FT DOMAIN 49..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..385
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT COILED 410..444
FT /evidence="ECO:0000256|SAM:Coils"
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
//
