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P09495

- TPM4_RAT

UniProt

P09495 - TPM4_RAT

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Protein
Tropomyosin alpha-4 chain
Gene
Tpm4
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_224772. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi3899. Tpm4.

Subcellular locationi

GO - Cellular componenti

  1. cortical cytoskeleton Source: Ensembl
  2. filamentous actin Source: Ensembl
  3. podosome Source: Ensembl
  4. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 248247Tropomyosin alpha-4 chain
PRO_0000205638Add
BLAST

Amino acid modifications

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

STRINGi10116.ENSRNOP00000021073.

Structurei

3D structure databases

ProteinModelPortaliP09495.
SMRiP09495. Positions 5-248.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 248247 By similarity
Add
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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG249432.
GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.
HOVERGENiHBG107404.
InParanoidiP09495.
KOiK10375.
OMAiEKCKQVE.
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

MAGLNSLEAV KRKIQALQQQ ADDAEDRAQG LQRELDGERE RREKAEGDAA    50
ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK 100
DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS 150
ELKSSDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE 200
TRAEFAERTV SKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI 248
Length:248
Mass (Da):28,510
Last modified:January 23, 2007 - v3
Checksum:i53C9327CA60CF954
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
J02780 mRNA. Translation: AAA42291.1 .
Y00169 Genomic DNA. Translation: CAA68360.1 .
PIRi S10623.
RefSeqi NP_036810.1. NM_012678.2.
UniGenei Rn.108199.

3D structure databases

ProteinModelPortali P09495.
SMRi P09495. Positions 5-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021073.

Proteomic databases

PaxDbi P09495.
PRIDEi P09495.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021073 ; ENSRNOP00000021073 ; ENSRNOG00000015496 .
GeneIDi 24852.
KEGGi rno:24852.
UCSCi RGD:3899. rat.

Organism-specific databases

CTDi 7171.
RGDi 3899. Tpm4.

Phylogenomic databases

eggNOGi NOG249432.
GeneTreei ENSGT00550000074494.
HOGENOMi HOG000231522.
HOVERGENi HBG107404.
InParanoidi P09495.
KOi K10375.
OMAi EKCKQVE.
OrthoDBi EOG7673C8.
PhylomeDBi P09495.
TreeFami TF351519.

Enzyme and pathway databases

Reactomei REACT_224772. Smooth Muscle Contraction.

Miscellaneous databases

NextBioi 604640.
PROi P09495.

Gene expression databases

Genevestigatori P09495.

Family and domain databases

InterProi IPR000533. Tropomyosin.
[Graphical view ]
Pfami PF00261. Tropomyosin. 1 hit.
[Graphical view ]
PRINTSi PR00194. TROPOMYOSIN.
PROSITEi PS00326. TROPOMYOSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 100 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

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