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P09495

- TPM4_RAT

UniProt

P09495 - TPM4_RAT

Protein

Tropomyosin alpha-4 chain

Gene

Tpm4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    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.
    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: October 1, 2014
    This is version 101 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