ID   TBA_TETPY               Reviewed;         449 AA.
AC   P10872;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Tubulin alpha chain;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CGL;
RX   PubMed=3139885; DOI=10.1016/0022-2836(88)90271-9;
RA   Barahona I., Soares H., Cyrne L., Penque D., Denoulet P.,
RA   Rodrigues-Pousada C.;
RT   "Sequence of one alpha- and two beta-tubulin genes of Tetrahymena
RT   pyriformis. Structural and functional relationships with other eukaryotic
RT   tubulin genes.";
RL   J. Mol. Biol. 202:365-382(1988).
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   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X12767; CAA31256.1; -; Genomic_DNA.
DR   PIR; S01767; S01767.
DR   AlphaFoldDB; P10872; -.
DR   SMR; P10872; -.
DR   PRIDE; P10872; -.
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..449
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048230"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            449
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  49577 MW;  CE22F20495EEA38A CRC64;
     MREVISIHVG QGGIQVGNAC WELFCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK
     HVPRAVFLDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
     RIRKLADNCT GLQGFLVFNS VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA
     VVEPYNSILS THSLLEHTDV AVMLDNEAIY DICRRNLDIE RPTYTNLNRL IAQVISSLTA
     SLRFDGALNV DITEFQTNLV PYPRIHFMLS SYAPIISAEK AYHEQLSVAE ITNSAFEPAN
     MMAKCDPRHG KYMACSMMYR GDVVPKDVNA SIATIKTKRT IQFVDWCPTG FKVGINYQPS
     TVVPGGDLAK VMRAVCMISN STAIAEVFSR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGIETA EGEGEEEGY