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P09495 (TPM4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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 alpha-4 chain
Alternative name(s):
Tropomyosin-4
Short name=TM-4
Gene names
Name:Tpm4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium.

Subunit structure

Heterodimer of an alpha and a beta chain.

Subcellular location

Cytoplasmcytoskeleton.

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
   Cellular componentCytoplasm
Cytoskeleton
   DomainCoiled coil
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionMuscle protein
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmuscle contraction

Traceable author statement Ref.2. Source: RGD

   Cellular_componentcortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

filamentous actin

Inferred from electronic annotation. Source: Ensembl

podosome

Inferred from electronic annotation. Source: Ensembl

stress fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 248247Tropomyosin alpha-4 chain
PRO_0000205638

Regions

Coiled coil2 – 248247 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue1771N6-acetyllysine By similarity
Modified residue2151N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P09495 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 53C9327CA60CF954

FASTA24828,510
        10         20         30         40         50         60 
MAGLNSLEAV KRKIQALQQQ ADDAEDRAQG LQRELDGERE RREKAEGDAA ALNRRIQLVE 

        70         80         90        100        110        120 
EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE 

       130        140        150        160        170        180 
EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKSSDLEEE LKNVTNNLKS LEAASEKYSE 

       190        200        210        220        230        240 
KEDKYEEEIK LLSDKLKEAE TRAEFAERTV SKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ 


TLNELNCI 

« Hide

References

[1]"Isolation and characterization of cDNA clones encoding a low molecular weight nonmuscle tropomyosin isoform."
Yamawaki-Kataoka Y., Helfman D.M.
J. Biol. Chem. 262:10791-10800(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and complete nucleotide sequence of the gene encoding rat fibroblast tropomyosin 4."
Lees-Miller J.P., Yan A., Helfman D.M.
J. Mol. Biol. 213:399-405(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain and Liver.
[3]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02780 mRNA. Translation: AAA42291.1.
Y00169 Genomic DNA. Translation: CAA68360.1.
PIRS10623.
RefSeqNP_036810.1. NM_012678.2.
UniGeneRn.108199.

3D structure databases

ProteinModelPortalP09495.
SMRP09495. Positions 5-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021073.

Proteomic databases

PaxDbP09495.
PRIDEP09495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021073; ENSRNOP00000021073; ENSRNOG00000015496.
GeneID24852.
KEGGrno:24852.
UCSCRGD:3899. rat.

Organism-specific databases

CTD7171.
RGD3899. Tpm4.

Phylogenomic databases

eggNOGNOG249432.
GeneTreeENSGT00550000074494.
HOGENOMHOG000231522.
HOVERGENHBG107404.
InParanoidP09495.
KOK10375.
OMAEKCKQVE.
OrthoDBEOG7673C8.
PhylomeDBP09495.
TreeFamTF351519.

Gene expression databases

GenevestigatorP09495.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604640.
PROP09495.

Entry information

Entry nameTPM4_RAT
AccessionPrimary (citable) accession number: P09495
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families