ID   TBA_HAECO               Reviewed;         450 AA.
AC   P50719;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Tubulin alpha chain;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1484557; DOI=10.1016/0166-6851(92)90185-m;
RA   Klein R.D., Nulf S.C., Alexander-Bowman S.J., Mainone C.B., Geary T.G.;
RT   "Cloning of a cDNA encoding alpha-tubulin from Haemonchus contortus.";
RL   Mol. Biochem. Parasitol. 56:345-348(1992).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
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; L02108; AAA29167.1; -; mRNA.
DR   PIR; A48466; A48466.
DR   AlphaFoldDB; P50719; -.
DR   SMR; P50719; -.
DR   DrugCentral; P50719; -.
DR   WBParaSite; HCON_00067020-00002; HCON_00067020-00002; HCON_00067020.
DR   OrthoDB; 1844at2759; -.
DR   Proteomes; UP000025227; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02186; alpha_tubulin; 1.
DR   FunFam; 1.10.287.600:FF:000005; Tubulin alpha chain; 1.
DR   FunFam; 3.30.1330.20:FF:000001; Tubulin alpha chain; 1.
DR   FunFam; 3.40.50.1440:FF:000019; Tubulin alpha chain; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Microtubule; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048178"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   SITE            450
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50111 MW;  41A3283301951D08 CRC64;
     MREVISIHIG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK SLGGCDDSFS TFFSETGSGR
     HVPRAVMIDL EPTVIDEIRT GTYRSLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLTLD
     RIRRLADNCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKAKLEFS VYPAPQVSTA
     VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLDIE RPSYTNLNRL IGQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TFSPVISAEK AYHEQLSVAE ITNMCFEPHN
     QMVKCDPRHG KYMAVCLLFR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VPRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGVDSL EDNGEEGDEY
//