P50719 (TBA_HAECO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Tubulin alpha chain
Organism	Haemonchus contortus (Barber pole worm)
Taxonomic identifier	6289 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Strongylida › Trichostrongyloidea › Haemonchidae › Haemonchinae › Haemonchus

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
Subunit structure	Dimer of alpha and beta chains.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively By similarity. Acetylation of alpha-tubulins at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Tubulin alpha chain		PRO_0000048178
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	450	1	Involved in polymerization By similarity
Amino acid modifications
	Modified residue	40	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50719 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 41A3283301951D08	FASTA	450	50,111
	10 20 30 40 50 60 MREVISIHIG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK SLGGCDDSFS TFFSETGSGR 70 80 90 100 110 120 HVPRAVMIDL EPTVIDEIRT GTYRSLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLTLD 130 140 150 160 170 180 RIRRLADNCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKAKLEFS VYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLDIE RPSYTNLNRL IGQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TFSPVISAEK AYHEQLSVAE ITNMCFEPHN 310 320 330 340 350 360 QMVKCDPRHG KYMAVCLLFR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 420 TVVPGGDLAK VPRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 450 AREDLAALEK DYEEVGVDSL EDNGEEGDEY

References

[1]	"Cloning of a cDNA encoding alpha-tubulin from Haemonchus contortus." Klein R.D., Nulf S.C., Alexander-Bowman S.J., Mainone C.B., Geary T.G. Mol. Biochem. Parasitol. 56:345-348(1992) [PubMed: 1484557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L02108 mRNA. Translation: AAA29167.1.
PIR	A48466.
3D structure databases
ProteinModelPortal	P50719.
SMR	P50719. Positions 1-440.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002452. Alpha_tubulin. IPR008280. Tub_FtsZ_C. IPR000217. Tubulin. IPR018316. Tubulin/FtsZ_2-layer-sand-dom. IPR023123. Tubulin_C. IPR017975. Tubulin_CS. IPR003008. Tubulin_FtsZ_GTPase. [Graphical view]
Gene3D	G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit. G3DSA:1.10.287.600. Tubulin_C. 1 hit. G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.
Pfam	PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view]
PRINTS	PR01162. ALPHATUBULIN. PR01161. TUBULIN.
SMART	SM00864. Tubulin. 1 hit. SM00865. Tubulin_C. 1 hit. [Graphical view]
SUPFAM	SSF55307. Tub_FtsZ_C. 1 hit. SSF52490. Tubulin_FtsZ. 1 hit.
PROSITE	PS00227. TUBULIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00518. Albendazole. DB00643. Mebendazole.

Entry information

Entry name

TBA_HAECO

Accession

Primary (citable) accession number: P50719

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	March 8, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)