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O16127 (TPM_ECHGR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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 A

Short name=EgTrpA
OrganismEchinococcus granulosus (Hydatid tapeworm)
Taxonomic identifier6210 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

Protein attributes

Sequence length278 AA.
Sequence statusFragment.
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

Chain‹1 – 278›278Tropomyosin A
PRO_0000205652

Regions

Coiled coil‹1 – 270›270 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O16127 [UniParc].

Last modified April 8, 2008. Version 3.
Checksum: 5227AEEB1B358885

FASTA27832,269
        10         20         30         40         50         60 
IMMAMKLEKE NALEKAINLE NQLKEKAKDF EKKEEEMNDW LSKVKNIQTE VDTVQESLQE 

        70         80         90        100        110        120 
AISKLEETEK RATNAEAEVA AMTRRIRLLE EDFEQSSGRL TETSTKLDDA SKAAEESERN 

       130        140        150        160        170        180 
RKTLETRSIS DDERMAQLEE QVKEAKYIAE DAERKYDEAA RRLAVTEVDL ERAESRLETS 

       190        200        210        220        230        240 
ESKIVELEEE LRIVGNNMKS LEVSEQESLQ REESYEETIR DLTERLKTAE QRAAEAERQV 

       250        260        270 
SKLQNEVDRL EDELLSEKER YRAISGELDT TFAELTSF 

« Hide

References

[1]Esteves A., Senorale M., Fernandez C., Bruzzone H., Ehrlich R.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF011923 mRNA. Translation: AAB65799.4.

3D structure databases

ModBaseSearch...
MobiDBSearch...

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_ECHGR
AccessionPrimary (citable) accession number: O16127
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 35 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families