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Protein

Tropomyosin alpha-4 chain

Gene

Tpm4

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

Functioni

Binds to actin filaments in muscle and non-muscle cells (PubMed:7568216). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (By similarity). Smooth muscle contraction is regulated by interaction with caldesmon (By similarity). In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments (By similarity). Binds calcium (By similarity).By similarity1 Publication

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • structural constituent of muscle Source: GO_Central

GO - Biological processi

  • actin filament organization Source: GO_Central
  • muscle contraction Source: RGD
  • osteoblast differentiation Source: RGD

Keywordsi

Molecular functionActin-binding, Muscle protein
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-390522 Striated Muscle Contraction
R-RNO-445355 Smooth 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi3899 Tpm4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002056382 – 248Tropomyosin alpha-4 chainAdd BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei6PhosphoserineCombined sources1
Modified residuei177N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei216PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP09495
PRIDEiP09495

PTM databases

iPTMnetiP09495
PhosphoSitePlusiP09495

Expressioni

Gene expression databases

BgeeiENSRNOG00000015496
ExpressionAtlasiP09495 baseline and differential
GenevisibleiP09495 RN

Interactioni

Subunit structurei

Homodimer (PubMed:7568216). Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain (PubMed:7568216).1 Publication

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi246969, 1 interactor
IntActiP09495, 1 interactor
STRINGi10116.ENSRNOP00000021073

Structurei

3D structure databases

ProteinModelPortaliP09495
SMRiP09495
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2 – 248By similarityAdd BLAST247

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

eggNOGiKOG1003 Eukaryota
ENOG410XR5K LUCA
GeneTreeiENSGT00550000074494
HOGENOMiHOG000231522
HOVERGENiHBG107404
InParanoidiP09495
KOiK10375
OMAiEDKCKQM
OrthoDBiEOG091G0UO7
PhylomeDBiP09495
TreeFamiTF351519

Family and domain databases

InterProiView protein in InterPro
IPR000533 Tropomyosin
PfamiView protein in Pfam
PF00261 Tropomyosin, 1 hit
PRINTSiPR00194 TROPOMYOSIN
PROSITEiView protein in PROSITE
PS00326 TROPOMYOSIN, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiTPM4_RAT
AccessioniPrimary (citable) accession number: P09495
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 128 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health