ID   TBA_EUPOC               Reviewed;         450 AA.
AC   Q08114;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin alpha chain;
OS   Euplotoides octocarinatus (Freshwater ciliate) (Euplotes octocarinatus).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX   NCBI_TaxID=2716877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3(58)-IX;
RX   PubMed=8167618; DOI=10.1111/j.1550-7408.1994.tb01490.x;
RA   Liang A., Schmidt H.J., Heckmann K.;
RT   "The alpha- and beta-tubulin genes of Euplotes octocarinatus.";
RL   J. Eukaryot. Microbiol. 41:163-169(1994).
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: 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   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X69466; CAA49226.1; -; Genomic_DNA.
DR   PIR; S31399; S31399.
DR   AlphaFoldDB; Q08114; -.
DR   SMR; Q08114; -.
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   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048171"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  49606 MW;  1CEB3715D2C6A393 CRC64;
     MREVISIHIG QGGIQVGNAC WDLFCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK
     HVPRAVFLDL EPTVCDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
     RIRKLADNCT GLQGFIGFHS VGGGTGSGLG SLLLERLSVD YGKKSKLTFT IYPSPQVSTA
     VVEPYNSVLS THSLLEHTDV AVMLDNEAVY DICRRNLDIE RPTYTNLNRL IAQVISSLTA
     SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSSFEPAS
     MMAKCDPRHG KYMACCMMYR GDVVPKDVNA AVATIKTKRT IQFVDWSPTG FKCGINYQPP
     TVVPGGDLAK VMRAVCMISN STAIAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGIETA EGEGEEEGME