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Protein

Tropomyosin alpha-4 chain

Gene

Tpm4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. muscle contraction Source: RGD
  2. osteoblast differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_224772. Smooth Muscle Contraction.
REACT_234304. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-4 chain
Alternative name(s):
Tropomyosin-4
Short name:
TM-4
Gene namesi
Name:Tpm4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3899. Tpm4.

Subcellular locationi

GO - Cellular componenti

  1. cortical cytoskeleton Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. filamentous actin Source: Ensembl
  4. focal adhesion Source: Ensembl
  5. membrane Source: Ensembl
  6. podosome Source: Ensembl
  7. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 248247Tropomyosin alpha-4 chainPRO_0000205638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei177 – 1771N6-acetyllysineBy similarity
Modified residuei215 – 2151N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09495.
PRIDEiP09495.

Expressioni

Gene expression databases

GenevestigatoriP09495.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

BioGridi246969. 1 interaction.
STRINGi10116.ENSRNOP00000021073.

Structurei

3D structure databases

ProteinModelPortaliP09495.
SMRiP09495. Positions 5-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 248247By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the tropomyosin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG249432.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.
HOVERGENiHBG107404.
InParanoidiP09495.
KOiK10375.
OMAiAELKCSD.
OrthoDBiEOG7673C8.
PhylomeDBiP09495.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLNSLEAV KRKIQALQQQ ADDAEDRAQG LQRELDGERE RREKAEGDAA
60 70 80 90 100
ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK
110 120 130 140 150
DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS
160 170 180 190 200
ELKSSDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE
210 220 230 240
TRAEFAERTV SKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI
Length:248
Mass (Da):28,510
Last modified:January 23, 2007 - v3
Checksum:i53C9327CA60CF954
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02780 mRNA. Translation: AAA42291.1.
Y00169 Genomic DNA. Translation: CAA68360.1.
PIRiS10623.
RefSeqiNP_036810.1. NM_012678.2.
UniGeneiRn.108199.

Genome annotation databases

EnsembliENSRNOT00000021073; ENSRNOP00000021073; ENSRNOG00000015496.
GeneIDi24852.
KEGGirno:24852.
UCSCiRGD:3899. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02780 mRNA. Translation: AAA42291.1.
Y00169 Genomic DNA. Translation: CAA68360.1.
PIRiS10623.
RefSeqiNP_036810.1. NM_012678.2.
UniGeneiRn.108199.

3D structure databases

ProteinModelPortaliP09495.
SMRiP09495. Positions 5-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246969. 1 interaction.
STRINGi10116.ENSRNOP00000021073.

Proteomic databases

PaxDbiP09495.
PRIDEiP09495.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021073; ENSRNOP00000021073; ENSRNOG00000015496.
GeneIDi24852.
KEGGirno:24852.
UCSCiRGD:3899. rat.

Organism-specific databases

CTDi7171.
RGDi3899. Tpm4.

Phylogenomic databases

eggNOGiNOG249432.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.
HOVERGENiHBG107404.
InParanoidiP09495.
KOiK10375.
OMAiAELKCSD.
OrthoDBiEOG7673C8.
PhylomeDBiP09495.
TreeFamiTF351519.

Enzyme and pathway databases

ReactomeiREACT_224772. Smooth Muscle Contraction.
REACT_234304. Striated Muscle Contraction.

Miscellaneous databases

NextBioi604640.
PROiP09495.

Gene expression databases

GenevestigatoriP09495.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiTPM4_RAT
AccessioniPrimary (citable) accession number: P09495
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.