Q8WQ47 (TBA_LEPDS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Tubulin alpha chain Alternative name(s): Allergen=Lep d ?
Organism	Lepidoglyphus destructor (Fodder mite)
Taxonomic identifier	36936 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Arachnida › Acari › Acariformes › Sarcoptiformes › Astigmata › Glycyphagoidea › Glycyphagidae › Lepidoglyphus

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 chains 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.
Allergenic properties	Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. Ref.1
Sequence similarities	Belongs to the tubulin family.
Caution	This protein lacks the required Tyr in position 450; it is replaced by a Phe.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Disease	Allergen
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation
Gene Ontology (GO)
Biological_process	microtubule-based process 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 constituent of cytoskeleton 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_0000048185
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Amino acid modifications
	Modified residue	40	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8WQ47 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: 1B2910B19021220D	FASTA	450	50,038
	10 20 30 40 50 60 MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGTGDDSFN TFFSETGSGK 70 80 90 100 110 120 HVPRAVYVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD 130 140 150 160 170 180 RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA VYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPVISSEK AYHEQLTVSE ITNTCFEPAN 310 320 330 340 350 360 QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 420 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 450 AREDLAALEK DYEEVGLDST EADDTAGEEF

References

[1]

"Cloning and characterisation of two IgE-binding proteins, homologous to tropomyosin and alpha-tubulin, from the mite Lepidoglyphus destructor." Saarne T., Kaiser L., Rasool O., Huecas S., van Hage-Hamsten M., Gafvelin G. Int. Arch. Allergy Immunol. 130:258-265(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ428050 mRNA. Translation: CAD20979.2.
3D structure databases
ProteinModelPortal	Q8WQ47.
SMR	Q8WQ47. Positions 1-439.
ModBase	Search...
Protein family/group databases
Allergome	1075. Lep d alpha Tubulin.
Proteomic databases
PRIDE	Q8WQ47.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit.
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]
PANTHER	PTHR11588. PTHR11588. 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...

Entry information

Entry name

TBA_LEPDS

Accession

Primary (citable) accession number: Q8WQ47

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)