ID   TBA_TOXGO               Reviewed;         453 AA.
AC   P10873;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Tubulin alpha chain;
DE   AltName: Full=Alpha-tubulin;
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3412377; DOI=10.1016/0166-6851(88)90081-3;
RA   Nagel S.D., Boothroyd J.C.;
RT   "The alpha- and beta-tubulins of Toxoplasma gondii are encoded by single
RT   copy genes containing multiple introns.";
RL   Mol. Biochem. Parasitol. 29:261-273(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; M20024; AAA30145.1; -; Genomic_DNA.
DR   PIR; S16339; S16339.
DR   PDB; 7MIZ; EM; 3.40 A; A0/A2/A4/A6/A8/B0/B2/B4/B6/B8/C0/C2/C4/C6/C8/D0/D2/D4/D6/D8/E0/E2/E4/E6/E8/F0=1-453.
DR   PDBsum; 7MIZ; -.
DR   AlphaFoldDB; P10873; -.
DR   SMR; P10873; -.
DR   EnsemblProtists; TGME49_316400-t26_1; TGME49_316400-t26_1; TGME49_316400.
DR   VEuPathDB; ToxoDB:TGARI_316400; -.
DR   VEuPathDB; ToxoDB:TGCAST_316400; -.
DR   VEuPathDB; ToxoDB:TGCOUG_316400; -.
DR   VEuPathDB; ToxoDB:TGDOM2_316400; -.
DR   VEuPathDB; ToxoDB:TGFOU_316400; -.
DR   VEuPathDB; ToxoDB:TGGT1_316400B; -.
DR   VEuPathDB; ToxoDB:TGMAS_316400; -.
DR   VEuPathDB; ToxoDB:TGME49_316400; -.
DR   VEuPathDB; ToxoDB:TGP89_316400; -.
DR   VEuPathDB; ToxoDB:TGPRC2_316400; -.
DR   VEuPathDB; ToxoDB:TGRH88_055140; -.
DR   VEuPathDB; ToxoDB:TGRUB_316400; -.
DR   VEuPathDB; ToxoDB:TGVAND_316400; -.
DR   VEuPathDB; ToxoDB:TGVEG_316400; -.
DR   OMA; KVGICYQ; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding;
KW   Microtubule; Nucleotide-binding.
FT   CHAIN           1..453
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048233"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            453
FT                   /note="Involved in polymerization"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  50114 MW;  1D86EBB220E01546 CRC64;
     MREVISIHVG QAGIQIGNAC WELFCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK
     HVPRCVFLDL EPTVVDEVRT GTYRHLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLSLD
     RIRKLADNCT GLQGFLMFNA VGGGTGSGLG CLLLERLSVD YGKKSKLNFC SWPSPQVSTA
     VVEPYNSVLS THSLLEHTDV AVMLDNEAIY DICRRNLDIE RPTYTNLNRL IAQVISSLTA
     SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SYAPIISAEK AYHEQLSVAE ITNSAFEPAS
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
     TVVPGGDLAK VMRAVCMISN STAIAEVFSR MDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGIETA EGEGEEEGYG DEY