TBA1_ELEIN
ID TBA1_ELEIN Reviewed; 451 AA.
AC O22347; O65805;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tubulin alpha-1 chain;
DE AltName: Full=Alpha-1-tubulin;
GN Name=TUBA1; Synonyms=TUA1;
OS Eleusine indica (Goosegrass) (Cynosurus indicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Chloridoideae; Cynodonteae; Eleusininae; Eleusine.
OX NCBI_TaxID=29674;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-239 AND THR-268.
RC TISSUE=Leaf;
RX PubMed=9490751; DOI=10.2307/3870706;
RA Yamamoto E., Zeng L., Baird W.V.;
RT "Alpha-tubulin missense mutations correlate with antimicrotubule drug
RT resistance in Eleusine indica.";
RL Plant Cell 10:297-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-239.
RX PubMed=9607761; DOI=10.1038/30484;
RA Anthony R.G., Waldin T.R., Ray J.A., Bright S.W.J., Hussey P.J.;
RT "Herbicide resistance caused by spontaneous mutation of the cytoskeletal
RT protein tubulin.";
RL Nature 393:260-263(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 -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL),
CC respectively. {ECO:0000250}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and
CC affects affinity and processivity of microtubule motors. This
CC modification has a role in multiple cellular functions, ranging from
CC cell motility, cell cycle progression or cell differentiation to
CC intracellular trafficking and signaling (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Dinitroaniline herbicides (such as trifluralin and
CC oryzalin) are antimicrotubule drugs that bind to tubulins and inhibit
CC polymerization. Prolonged use of these chemicals has resulted in the
CC selection of resistant (R) and intermediately resistant (I) biotypes.
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; AF008120; AAC05717.1; -; mRNA.
DR EMBL; AJ005598; CAA06618.1; -; mRNA.
DR EMBL; AJ005599; CAA06619.1; -; mRNA.
DR AlphaFoldDB; O22347; -.
DR SMR; O22347; -.
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; 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; PTHR11588; 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; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding.
FT CHAIN 1..451
FT /note="Tubulin alpha-1 chain"
FT /id="PRO_0000048162"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 451
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT VARIANT 239
FT /note="T -> I (in R biotype)"
FT /evidence="ECO:0000269|PubMed:9490751,
FT ECO:0000269|PubMed:9607761"
FT VARIANT 268
FT /note="M -> T (in I biotype)"
FT /evidence="ECO:0000269|PubMed:9490751"
SQ SEQUENCE 451 AA; 49731 MW; C786F920557DB415 CRC64;
MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDDAFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS
VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA
SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
SVVPGGDLAK VQRAVCMISN STSVVEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGAEFD EGEEGDEGDE Y
