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)

P58772

- TPM1_RABIT

UniProt

P58772 - TPM1_RABIT

Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.

    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
    Synonyms:TPMA
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: 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
    Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205623Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei283 – 2831Phosphoserine; by DAPK11 Publication

    Post-translational modificationi

    Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP58772.

    Miscellaneous databases

    PMAP-CutDBP58772.

    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

    Protein-protein interaction databases

    BioGridi1172720. 1 interaction.
    DIPiDIP-46098N.
    IntActiP58772. 2 interactions.
    MINTiMINT-1500045.

    Structurei

    Secondary structure

    1
    284
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 2423
    Helixi176 – 27398

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D3EX-ray2.60A/B/C/D176-284[»]
    2EFRX-ray1.80A/B/C/D176-273[»]
    2EFSX-ray2.00A/B/C/D176-273[»]
    2TMAX-ray15.00A/B1-284[»]
    2W49electron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
    2W4Uelectron microscopy35.00A/B/C/T/U/V/W/X8-284[»]
    2Z5HX-ray2.89A/B/C/D/E/F/G/H254-284[»]
    I1-24[»]
    2Z5IX-ray2.10A/B/C/D/E/F/G/H254-284[»]
    I/J1-24[»]
    4A7Felectron microscopy7.70B/H98-233[»]
    4A7Helectron microscopy7.80B/H98-233[»]
    4A7Lelectron microscopy8.10B/H98-233[»]
    ProteinModelPortaliP58772.
    SMRiP58772. Positions 8-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP58772.

    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

    eggNOGiNOG304012.
    HOGENOMiHOG000231521.
    HOVERGENiHBG107404.
    OrthoDBiEOG7673C8.

    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.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms may be produced.

    Isoform 1 (identifier: P58772-1) [UniParc]FASTAAdd to Basket

    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 AAEDRSKQLE DELVSLQKKL    50
    KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
    AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
    TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
    KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
    Length:284
    Mass (Da):32,681
    Last modified:July 21, 1986 - v1
    Checksum:iE25609F597A72F4D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78854 mRNA. Translation: AAB34957.1.
    V00892 mRNA. Translation: CAA24257.1.
    PIRiI47056. TMRBA.
    RefSeqiNP_001099158.1. NM_001105688.1. [P58772-1]
    UniGeneiOcu.3324.

    Genome annotation databases

    GeneIDi100125989.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78854 mRNA. Translation: AAB34957.1 .
    V00892 mRNA. Translation: CAA24257.1 .
    PIRi I47056. TMRBA.
    RefSeqi NP_001099158.1. NM_001105688.1. [P58772-1 ]
    UniGenei Ocu.3324.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D3E X-ray 2.60 A/B/C/D 176-284 [» ]
    2EFR X-ray 1.80 A/B/C/D 176-273 [» ]
    2EFS X-ray 2.00 A/B/C/D 176-273 [» ]
    2TMA X-ray 15.00 A/B 1-284 [» ]
    2W49 electron microscopy 35.00 A/B/C/T/U/V/W/X 8-284 [» ]
    2W4U electron microscopy 35.00 A/B/C/T/U/V/W/X 8-284 [» ]
    2Z5H X-ray 2.89 A/B/C/D/E/F/G/H 254-284 [» ]
    I 1-24 [» ]
    2Z5I X-ray 2.10 A/B/C/D/E/F/G/H 254-284 [» ]
    I/J 1-24 [» ]
    4A7F electron microscopy 7.70 B/H 98-233 [» ]
    4A7H electron microscopy 7.80 B/H 98-233 [» ]
    4A7L electron microscopy 8.10 B/H 98-233 [» ]
    ProteinModelPortali P58772.
    SMRi P58772. Positions 8-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1172720. 1 interaction.
    DIPi DIP-46098N.
    IntActi P58772. 2 interactions.
    MINTi MINT-1500045.

    Proteomic databases

    PRIDEi P58772.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100125989.

    Organism-specific databases

    CTDi 7168.

    Phylogenomic databases

    eggNOGi NOG304012.
    HOGENOMi HOG000231521.
    HOVERGENi HBG107404.
    OrthoDBi EOG7673C8.

    Miscellaneous databases

    EvolutionaryTracei P58772.
    PMAP-CutDB P58772.

    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. "The amino acid sequence of rabbit skeletal alpha-tropomyosin. The NH2-terminal half and complete sequence."
      Stone D., Smillie L.B.
      J. Biol. Chem. 253:1137-1148(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Skeletal muscle.
    2. "The amino acid sequence of rabbit cardiac tropomyosin."
      Lewis W.G., Smillie L.B.
      J. Biol. Chem. 255:6854-6859(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Heart muscle.
    3. "Rabbit skeletal muscle alpha alpha-tropomyosin expressed in baculovirus-infected insect cells possesses the authentic N-terminus structure and functions."
      Kluwe L., Maeda K., Miegel A., Fujita-Becker S., Maeda Y., Talbo G., Houthaeve T., Kellner R.
      J. Muscle Res. Cell Motil. 16:103-110(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Skeletal muscle.
    4. "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
      Putney S.D., Herlihy W.C., Schimmel P.R.
      Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-146.
    5. "Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle."
      Mak A.S., Smillie L.B., Barany M.
      Proc. Natl. Acad. Sci. U.S.A. 75:3588-3592(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-283.
      Tissue: Skeletal muscle.
    6. "Construction of an atomic model for tropomyosin and implications for interactions with actin."
      Phillips G.N. Jr.
      J. Mol. Biol. 192:128-131(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (15 ANGSTROMS).

    Entry informationi

    Entry nameiTPM1_RABIT
    AccessioniPrimary (citable) accession number: P58772
    Secondary accession number(s): P02558, P46902, P99034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3