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O97162 (TPM_RHIMP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRhipicephalus microplus (Cattle tick) (Boophilus microplus)
Taxonomic identifier6941 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariParasitiformesIxodidaIxodoideaIxodidaeRhipicephalinaeRhipicephalusBoophilus

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the tropomyosin family.

Ontologies

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin
PRO_0000205677

Regions

Coiled coil1 – 284284 By similarity

Sequences

Sequence LengthMass (Da)Tools
O97162 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DFFEA6828BCD73E2

FASTA28433,002
        10         20         30         40         50         60 
MEAIKKKMQA MKLEKDNAVD RAETAEQQSR EAALRAEKAE EEVRSLQKKI QQIENELDQV 

        70         80         90        100        110        120 
QEQLSQANSK LEEKDKALQA AEAEVAAHNR RIQLLEEDLE RSEERLKIAT QKLEEASQAA 

       130        140        150        160        170        180 
DESERMRKML EHRSITDEER MDGLEGQLKE ARTMAEDADR KYDEVARKLA MVEADLERAE 

       190        200        210        220        230        240 
ERAETGETKI VELEEELRVV GNNLKSLEVS EEKALQKEET YEMQIRQMTN RLQEAEARAE 

       250        260        270        280 
FAERSVQKLQ KEVDRLEDEL VQEKEKYKAI SDELDQTFSE LTGY 

« Hide

References

[1]Johnson C.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF124514 mRNA. Translation: AAD17324.1.

3D structure databases

ProteinModelPortalO97162.
SMRO97162. Positions 1-283.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome7728. Boo m 7.
7729. Boo m 7.0101.

Proteomic databases

PRIDEO97162.

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_RHIMP
AccessionPrimary (citable) accession number: O97162
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 34 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