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P58773

- TPM1_COTJA

UniProt

P58773 - TPM1_COTJA

Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Coturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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.

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin alpha-1 chain
    Alternative name(s):
    Alpha-tropomyosin
    Tropomyosin-1
    Gene namesi
    Name:TPM1
    OrganismiCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
    Taxonomic identifieri93934 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePerdicinaeCoturnix

    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
    Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205626Add
    BLAST

    Proteomic databases

    PRIDEiP58773.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP58773.
    SMRiP58773. Positions 1-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1 – 284284By 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

    HOVERGENiHBG107404.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P58773-1) [UniParc]FASTAAdd to Basket

    Also known as: Skeletal muscle, cC402, SK74

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEERSKQLE DELVALQKKL    50
    KGTEDELDKY SESLKDAQEK LELADKKATD AESEVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAQKDEEK MEIQEIQLKE 150
    AKHIAEEADR KYEEVARKLV IIEGDLERAE ERAELSESKC AELEEELKTV 200
    TNNLKSLEAQ AEKYSQKEDK YEEEIKVLTD KLKEAETRAE FAERSVTKLE 250
    KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
    Length:284
    Mass (Da):32,766
    Last modified:August 13, 1987 - v1
    Checksum:iDBBBD3DB7F36DACB
    GO
    Isoform 2 (identifier: P58773-2) [UniParc]FASTAAdd to Basket

    Also known as: Smooth muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         42-80: ELVALQKKLK...LELADKKATD → DIVQLEKQLR...LLSAEEIAAK
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,865
    Checksum:i180403F2D27453D7
    GO
    Isoform 3 (identifier: P58773-3) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast, cC401

    The sequence of this isoform differs from the canonical sequence as follows:
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,821
    Checksum:iCEA880914631B0DC
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLSAEEIAAK in isoform 2. CuratedVSP_006592Add
    BLAST
    Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2 and isoform 3. 1 PublicationVSP_006593Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16230
    , X16236, X16237, X16238, X16239, X16240 Genomic DNA. Translation: CAA34344.1.
    X16230
    , X16236, X16237, X16238, X16241 Genomic DNA. Translation: CAA34343.1.
    X04690 mRNA. Translation: CAA28393.1.
    M15043 mRNA. Translation: AAA49511.1.
    M17914 mRNA. Translation: AAA49510.1.
    M15044 mRNA. Translation: AAA49508.1.
    PIRiA28499.
    B28499. A26113.
    S05445.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16230
    , X16236 , X16237 , X16238 , X16239 , X16240 Genomic DNA. Translation: CAA34344.1 .
    X16230
    , X16236 , X16237 , X16238 , X16241 Genomic DNA. Translation: CAA34343.1 .
    X04690 mRNA. Translation: CAA28393.1 .
    M15043 mRNA. Translation: AAA49511.1 .
    M17914 mRNA. Translation: AAA49510.1 .
    M15044 mRNA. Translation: AAA49508.1 .
    PIRi A28499.
    B28499. A26113.
    S05445.

    3D structure databases

    ProteinModelPortali P58773.
    SMRi P58773. Positions 1-284.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P58773.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG107404.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    2. "A novel hybrid alpha-tropomyosin in fibroblasts is produced by alternative splicing of transcripts from the skeletal muscle alpha-tropomyosin gene."
      Pearson-White S.H., Emerson C.P. Jr.
      J. Biol. Chem. 262:15998-16010(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    3. "Analysis of tropomyosin cDNAs isolated from skeletal and smooth muscle mRNA."
      Flach J.E., Lindquester G.J., Berish S., Hickman K.H., Devlin R.
      Nucleic Acids Res. 14:9193-9211(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Closely related alpha-tropomyosin mRNAs in quail fibroblasts and skeletal muscle cells."
      Hallauer P.L., Hastings K.E.M., Baldwin A.S. Jr., Pearson-White S.H., Merrifield P.A., Emerson C.P. Jr.
      J. Biol. Chem. 262:3590-3596(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).

    Entry informationi

    Entry nameiTPM1_COTJA
    AccessioniPrimary (citable) accession number: P58773
    Secondary accession number(s): P02559
    , P08942, P18442, P49437
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3