ID A9PL21_GOSHI Unreviewed; 450 AA.
AC A9PL21;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN Name=TUA12 {ECO:0000313|EMBL:ABO47742.1};
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 {ECO:0000313|EMBL:ABO47742.1};
RN [1] {ECO:0000313|EMBL:ABO47742.1}
RP NUCLEOTIDE SEQUENCE.
RA Li X.-B.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABO47742.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17761728; DOI=10.1093/jxb/erm167;
RA Li L., Wang X.L., Huang G.Q., Li X.B.;
RT "Molecular characterization of cotton GhTUA9 gene specifically expressed in
RT fibre and involved in cell elongation.";
RL J. Exp. Bot. 58:3227-3238(2007).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; EF151308; ABO47742.1; -; mRNA.
DR RefSeq; NP_001314569.1; NM_001327640.1.
DR RefSeq; XP_016749939.1; XM_016894450.1.
DR AlphaFoldDB; A9PL21; -.
DR SMR; A9PL21; -.
DR GeneID; 107955533; -.
DR GeneID; 107958627; -.
DR KEGG; ghi:107955533; -.
DR KEGG; ghi:107958627; -.
DR OMA; NDFSREC; -.
DR OrthoDB; 1206011at2759; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; 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 GO; GO:0090378; P:seed trichome elongation; IEP:AgBase.
DR CDD; cd02186; alpha_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; IPR002452; Alpha_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:SF425; TUBULIN ALPHA CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
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.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 49..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..393
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 450 AA; 49502 MW; EE7ECC376B894F13 CRC64;
MRECISVHIG QAGIQVGNAC WELYCLEHGI QPDGQMPGDK TVGGGDDAFN TFFSETGAGK
HVPRAVFLDL EPTVIDEVRT GAYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFHA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPAYTNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITSSAFEPAS
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
TVVPGGDLAK VQRAVCMISN STSVAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGLESG EGDEDEGDEY
//
