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Protein

Tubulin alpha chain

Gene
N/A
Organism
Lepidoglyphus destructor (Fodder mite)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. microtubule-based process Source: InterPro
  2. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha chain
Alternative name(s):
Allergen: Lep d ?
OrganismiLepidoglyphus destructor (Fodder mite)
Taxonomic identifieri36936 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataGlycyphagoideaGlycyphagidaeLepidoglyphus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei1075. Lep d 33.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Tubulin alpha chainPRO_0000048185Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ8WQ47.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ8WQ47.
SMRiQ8WQ47. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WQ47-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGTGDDSFN
60 70 80 90 100
TFFSETGSGK HVPRAVYVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIVDLVLD RIRKLADQCT GLQGFLIFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFA VYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLV TYAPVISSEK AYHEQLTVSE ITNTCFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGLDST EADDTAGEEF
Length:450
Mass (Da):50,038
Last modified:June 1, 2002 - v2
Checksum:i1B2910B19021220D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ428050 mRNA. Translation: CAD20979.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ428050 mRNA. Translation: CAD20979.2.

3D structure databases

ProteinModelPortaliQ8WQ47.
SMRiQ8WQ47. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1075. Lep d 33.

Proteomic databases

PRIDEiQ8WQ47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiTBA_LEPDS
AccessioniPrimary (citable) accession number: Q8WQ47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: February 4, 2015
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

This protein lacks the required Tyr in position 450; it is replaced by a Phe.Curated

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.