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   03-AUG-2022, entry version 95.
DE   RecName: Full=Tubulin alpha chain;
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; 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. 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; L02108; AAA29167.1; -; mRNA.
DR   PIR; A48466; A48466.
DR   AlphaFoldDB; P50719; -.
DR   SMR; P50719; -.
DR   DrugCentral; P50719; -.
DR   PRIDE; P50719; -.
DR   WBParaSite; HCON_00067020-00002; HCON_00067020-00002; HCON_00067020.
DR   Proteomes; UP000025227; Unplaced.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048178"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
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