ID   TBA2_ELEIN              Reviewed;         447 AA.
AC   O22348;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tubulin alpha-2 chain;
DE   AltName: Full=Alpha-2-tubulin;
GN   Name=TUBA2; Synonyms=TUA2;
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].
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).
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   -!- 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; AF008121; AAC05718.1; -; mRNA.
DR   AlphaFoldDB; O22348; -.
DR   SMR; O22348; -.
DR   PRIDE; O22348; -.
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; IPR013838; Beta-tubulin_BS.
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   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..447
FT                   /note="Tubulin alpha-2 chain"
FT                   /id="PRO_0000048163"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            447
FT                   /note="Involved in polymerization"
SQ   SEQUENCE   447 AA;  49823 MW;  0AEA21D6E756025C CRC64;
     MREIISIHIG QAGIQVGNSC WELYCLEHGI QPDGLMPSDT SLGVARDAFN TFFSETGAGK
     HVPRALFVDL EPTVIDEVKT GPYRQLFHPE QLISYKEDAA NNFARGHYTV GREIVDPCLD
     RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGRKSKLGFT IYPSPQISTA
     VVEPYNSVLS THSLIEHTDV VVLLDNEAIY DICKRSLDIE RPTYTNLNRL ISQVISSLTT
     SLRFDGAINV DITEFQTNLV PYPRIHFMLS SYAPIISVEK AYHEQHSVPE ITNSVFESSS
     VMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVHSIKTKRT VQFVDWCPTG FKCGINYQPP
     TVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDRKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGAEVE EDDEEEY