Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8WQ47 (TBA_LEPDS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin alpha chain
Alternative name(s):
Allergen=Lep d ?
OrganismLepidoglyphus destructor (Fodder mite)
Taxonomic identifier36936 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataGlycyphagoideaGlycyphagidaeLepidoglyphus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence 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. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Subcellular location

Cytoplasmcytoskeleton.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Tubulin alpha chain
PRO_0000048185

Regions

Nucleotide binding142 – 1487GTP Potential

Amino acid modifications

Modified residue401N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WQ47 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: 1B2910B19021220D

FASTA45050,038
        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 

« Hide

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

ProteinModelPortalQ8WQ47.
SMRQ8WQ47. Positions 1-439.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1075. Lep d alpha Tubulin.

Proteomic databases

PRIDEQ8WQ47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTBA_LEPDS
AccessionPrimary (citable) accession number: Q8WQ47
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: January 22, 2014
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Allergens

Nomenclature of allergens and list of entries