Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02561

- TPM4_HORSE

UniProt

P02561 - TPM4_HORSE

Protein

Tropomyosin alpha-4 chain

Gene

TPM4

Organism
Equus caballus (Horse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin alpha-4 chain
    Alternative name(s):
    Platelet beta tropomyosin
    Tropomyosin-4
    Gene namesi
    Name:TPM4
    OrganismiEquus caballus (Horse)
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 248247Tropomyosin alpha-4 chainPRO_0000205634Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP02561.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain.

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000019820.

    Structurei

    3D structure databases

    ProteinModelPortaliP02561.
    SMRiP02561. 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

    eggNOGiNOG304012.
    HOGENOMiHOG000231522.
    HOVERGENiHBG107404.
    InParanoidiP02561.

    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.

    P02561-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA    50
    ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK 100
    DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS 150
    ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE 200
    TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLDELNCI 248
    Length:248
    Mass (Da):28,523
    Last modified:January 23, 2007 - v2
    Checksum:i5D5CDF6BF76BB2A8
    GO

    Sequence databases

    PIRiA02984. TMHOBP.

    Cross-referencesi

    Sequence databases

    PIRi A02984. TMHOBP.

    3D structure databases

    ProteinModelPortali P02561.
    SMRi P02561. Positions 5-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000019820.

    Proteomic databases

    PRIDEi P02561.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG304012.
    HOGENOMi HOG000231522.
    HOVERGENi HBG107404.
    InParanoidi P02561.

    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. "Amino acid sequence of equine platelet tropomyosin. Correlation with interaction properties."
      Lewis W.G., Cote G.P., Mak A.S., Smillie L.B.
      FEBS Lett. 156:269-273(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-248.

    Entry informationi

    Entry nameiTPM4_HORSE
    AccessioniPrimary (citable) accession number: P02561
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein can span only six actin monomers.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3