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O97192 (TPM_HELAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:
Tropomyosin
Alternative name(s):
Allergen=Hel as 1
OrganismHelix aspersa (Brown garden snail) (Cornu aspersum)
Taxonomic identifier6535 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraPanpulmonataEupulmonataStylommatophoraSigmurethraHelicoideaHelicidaeHelix

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.

Subunit structure

Homodimer By similarity.

Domain

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the tropomyosin family.

Ontologies

Keywords
   DiseaseAllergen
   DomainCoiled coil
Repeat
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin
PRO_0000205667

Regions

Coiled coil1 – 284284 By similarity

Sequences

Sequence LengthMass (Da)Tools
O97192 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 01B87021E0F32D4D

FASTA28432,637
        10         20         30         40         50         60 
MDAIKKKMLA MKMEKENALD RAEQVEQKLR DCECNKNKVE EDLNNLQKKF AILENDFDSI 

        70         80         90        100        110        120 
NEQLLDANTK LEASEKKNAE IESETAGLQR RIQLLEEDLE RSEERLQSAT EKLEEASKAA 

       130        140        150        160        170        180 
DESERGRKVL ESRSLADDER LDGLEAQLKE AKYIAEDAER KFDEAARKLA ITEVDLERAE 

       190        200        210        220        230        240 
ARLEAAEAKI LELEEELKVV GNNMKSLEIS EQEASQREDS YEETIRDLTQ RLKDAENRAS 

       250        260        270        280 
EAERTVSKLQ KEVDRLEDEL LAEKERYKAT SDELDSTFAE LAGY 

« Hide

References

[1]"Cloning, isolation, and IgE-binding properties of Helix aspersa (brown garden snail) tropomyosin."
Asturias J.A., Eraso E., Arilla M.C., Gomez-Bayon N., Inacio F., Martinez A.
Int. Arch. Allergy Immunol. 128:90-96(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14855 mRNA. Translation: CAB38044.1.

3D structure databases

ProteinModelPortalO97192.
SMRO97192. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3309. Hel as 1.0101.
378. Hel as 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
ProtoNetSearch...

Entry information

Entry nameTPM_HELAS
AccessionPrimary (citable) accession number: O97192
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 33 of the entry and version 1 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