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P04268

- TPM1_CHICK

UniProt

P04268 - TPM1_CHICK

Protein

Tropomyosin alpha-1 chain

Gene

TPM1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (13 Aug 1987)
      Previous versions | rss
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    • 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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 10

    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_0000205625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP04268.
    PRIDEiP04268.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain By similarity. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Smtnl1Q99LM33EBI-8073544,EBI-8073484From a different organism.

    Protein-protein interaction databases

    IntActiP04268. 1 interaction.

    Structurei

    Secondary structure

    284
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 9696
    Helixi257 – 28327

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IC2X-ray2.00A/B/C/D1-80[»]
    3MTUX-ray2.10A/B/C/D1-29[»]
    E/F257-284[»]
    3MUDX-ray2.20A/B246-257[»]
    C/D1-29[»]
    3U1AX-ray2.00A/B/C/D1-81[»]
    3U1CX-ray1.80A/B1-98[»]
    ProteinModelPortaliP04268.
    SMRiP04268. Positions 1-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04268.

    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.
    GeneTreeiENSGT00550000074494.
    HOVERGENiHBG107404.
    KOiK10373.
    OMAiEASAEKY.
    OrthoDBiEOG7673C8.
    PhylomeDBiP04268.
    TreeFamiTF351519.

    Family and domain databases

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

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P04268-1) [UniParc]FASTAAdd to Basket

    Also known as: Fast-twitch skeletal muscle, CTm7

    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 - v2
    Checksum:iDBBBD3DB7F36DACB
    GO
    Isoform 2 (identifier: P04268-2) [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...LLFAEENAAK
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,926
    Checksum:iC29E05F9DEA8F27F
    GO
    Isoform 4 (identifier: P04268-4) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast F1

    The sequence of this isoform differs from the canonical sequence as follows:
         189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLNMHQMLDQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,960
    Checksum:iE94405DA8D65597F
    GO
    Isoform 5 (identifier: P04268-5) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast F2

    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
    Isoform 6 (identifier: P04268-6) [UniParc]FASTAAdd to Basket

    Also known as: Brain major

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELADKKATD → MAALSSLEAV...VDQERALREE
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYQQLEQNSRLTNELKLALNED

    Show »
    Length:245
    Mass (Da):28,361
    Checksum:i0F45465ECA0AD748
    GO
    Isoform 7 (identifier: P04268-7) [UniParc]FASTAAdd to Basket

    Also known as: Brain minor

    The sequence of this isoform differs from the canonical sequence as follows:
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYQQLEQNSRLTNELKLALNED

    Show »
    Length:281
    Mass (Da):32,502
    Checksum:i862297483A4C684C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341E → D AA sequence (PubMed:3997866)Curated
    Sequence conflicti45 – 451A → S AA sequence (PubMed:3997866)Curated
    Sequence conflicti63 – 631S → A AA sequence (PubMed:3997866)Curated
    Sequence conflicti75 – 751D → E AA sequence (PubMed:3997866)Curated
    Sequence conflicti83 – 842SE → AD AA sequence (PubMed:3997866)Curated
    Sequence conflicti132 – 1321N → S AA sequence (PubMed:3997866)Curated
    Sequence conflicti157 – 1571E → D AA sequence (PubMed:3997866)Curated
    Sequence conflicti165 – 1651V → A in AAA48610. (PubMed:3671073)Curated
    Sequence conflicti172 – 1721I → L AA sequence (PubMed:3997866)Curated
    Sequence conflicti174 – 1741G → S AA sequence (PubMed:3997866)Curated
    Sequence conflicti188 – 1881S → G AA sequence (PubMed:3997866)Curated
    Sequence conflicti229 – 2291T → S AA sequence (PubMed:3997866)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711I → V.
    Natural varianti175 – 1751D → E.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080MDAIK…KKATD → MAALSSLEAVRKKIRSLQEQ ADAAEERAGKLQREVDQERA LREE in isoform 6. CuratedVSP_006587Add
    BLAST
    Alternative sequencei42 – 8039ELVAL…KKATD → DIVQLEKQLRVTEDSRDQVL EELHKSEDSLLFAEENAAK in isoform 2. CuratedVSP_006588Add
    BLAST
    Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 4. 1 PublicationVSP_006589Add
    BLAST
    Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLNMHQMLDQT LLELNNM in isoform 2, isoform 4 and isoform 5. 1 PublicationVSP_006590Add
    BLAST
    Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYQQLEQNSRLTNELKLAL NED in isoform 6 and isoform 7. CuratedVSP_006591Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32441 mRNA. Translation: AAA48610.1.
    X57991
    , X57993, X57994, X57995 Genomic DNA. Translation: CAA41056.1.
    M69144
    , M69140, M69142, M69143 Genomic DNA. Translation: AAA48577.1.
    X16090 Genomic DNA. Translation: CAA34217.1. Sequence problems.
    X57991
    , X57993, X57994, X57996 Genomic DNA. Translation: CAA41059.1.
    X57991
    , X57993, X57994, X57996 Genomic DNA. Translation: CAA41058.1.
    X57991
    , X57993, X57994, X57996 Genomic DNA. Translation: CAA41057.1.
    M36336 mRNA. Translation: AAA65120.1.
    M36337 mRNA. Translation: AAA65121.1.
    AY150210 mRNA. Translation: AAN75276.1.
    AADN02040437 Genomic DNA. No translation available.
    AADN02040438 Genomic DNA. No translation available.
    J00910 mRNA. Translation: AAA49113.1.
    PIRiS24399. TMCHA.
    S24400. TMCHS2.
    S24401.
    S24402.
    RefSeqiNP_990732.1. NM_205401.1. [P04268-4]
    UniGeneiGga.4108.

    Genome annotation databases

    EnsembliENSGALT00000039589; ENSGALP00000038799; ENSGALG00000003521. [P04268-4]
    GeneIDi396366.
    KEGGigga:396366.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32441 mRNA. Translation: AAA48610.1 .
    X57991
    , X57993 , X57994 , X57995 Genomic DNA. Translation: CAA41056.1 .
    M69144
    , M69140 , M69142 , M69143 Genomic DNA. Translation: AAA48577.1 .
    X16090 Genomic DNA. Translation: CAA34217.1 . Sequence problems.
    X57991
    , X57993 , X57994 , X57996 Genomic DNA. Translation: CAA41059.1 .
    X57991
    , X57993 , X57994 , X57996 Genomic DNA. Translation: CAA41058.1 .
    X57991
    , X57993 , X57994 , X57996 Genomic DNA. Translation: CAA41057.1 .
    M36336 mRNA. Translation: AAA65120.1 .
    M36337 mRNA. Translation: AAA65121.1 .
    AY150210 mRNA. Translation: AAN75276.1 .
    AADN02040437 Genomic DNA. No translation available.
    AADN02040438 Genomic DNA. No translation available.
    J00910 mRNA. Translation: AAA49113.1 .
    PIRi S24399. TMCHA.
    S24400. TMCHS2.
    S24401.
    S24402.
    RefSeqi NP_990732.1. NM_205401.1. [P04268-4 ]
    UniGenei Gga.4108.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IC2 X-ray 2.00 A/B/C/D 1-80 [» ]
    3MTU X-ray 2.10 A/B/C/D 1-29 [» ]
    E/F 257-284 [» ]
    3MUD X-ray 2.20 A/B 246-257 [» ]
    C/D 1-29 [» ]
    3U1A X-ray 2.00 A/B/C/D 1-81 [» ]
    3U1C X-ray 1.80 A/B 1-98 [» ]
    ProteinModelPortali P04268.
    SMRi P04268. Positions 1-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04268. 1 interaction.

    Proteomic databases

    PaxDbi P04268.
    PRIDEi P04268.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000039589 ; ENSGALP00000038799 ; ENSGALG00000003521 . [P04268-4 ]
    GeneIDi 396366.
    KEGGi gga:396366.

    Organism-specific databases

    CTDi 7168.

    Phylogenomic databases

    eggNOGi NOG304012.
    GeneTreei ENSGT00550000074494.
    HOVERGENi HBG107404.
    KOi K10373.
    OMAi EASAEKY.
    OrthoDBi EOG7673C8.
    PhylomeDBi P04268.
    TreeFami TF351519.

    Miscellaneous databases

    EvolutionaryTracei P04268.
    NextBioi 20816411.
    PROi P04268.

    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 chicken gizzard gamma-tropomyosin."
      Lau S.Y.M., Sanders C., Smillie L.B.
      J. Biol. Chem. 260:7257-7263(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORM 1).
    2. "Complete nucleotide sequence of the fast-twitch isoform of chicken skeletal muscle alpha-tropomyosin."
      Gooding C., Reinach F.C., Macleod A.R.
      Nucleic Acids Res. 15:8105-8105(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    3. "The chicken gene encoding the alpha isoform of tropomyosin of fast-twitch muscle fibers: organization, expression and identification of the major proteins synthesized."
      Lemonnier M., Balvay L., Mouly V., Libri D., Fiszman M.Y.
      Gene 107:229-240(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 4; 5; 6 AND 7).
    4. "Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms."
      Fanning A.S., Wolenski J.S., Mooseker M.S., Izant J.G.
      Cell Motil. Cytoskeleton 29:29-45(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
      Tissue: Body wall.
    5. "Identification, characterization, and expression of a novel alpha-tropomyosin isoform in cardiac tissues in developing chicken."
      Denz C.R., Zajdel R.W., Dube S., Dube D.K.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart and Skeletal muscle.
    6. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
      Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
      , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
      Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Red jungle fowl.
    7. "Distinct alpha-tropomyosin mRNA sequences in chicken skeletal muscle."
      McLeod A.R.
      Eur. J. Biochem. 126:293-297(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-284 (ISOFORM 1).
    8. "Chick alpha tropomyosin gene contains three sets of mutually exclusive alternatively spliced exons."
      Lemonnier M., Libri D., Fiszman M.Y.
      Nucleic Acids Res. 17:5400-5400(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 189-213 (ISOFORM 4).
      Tissue: Muscle.
    9. "Peptides derived from the histidine-proline domain of the histidine-proline-rich glycoprotein bind to tropomyosin and have antiangiogenic and antitumor activities."
      Donate F., Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., Tel-Tsur Z., Shaw D.E., Morgan W.T., Mazar A.P.
      Cancer Res. 64:5812-5817(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRG.
    10. "Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-angiogenic signals through cell surface tropomyosin on endothelial cells."
      Guan X., Juarez J.C., Qi X., Shipulina N.V., Shaw D.E., Morgan W.T., McCrae K.R., Mazar A.P., Donate F.
      Thromb. Haemost. 92:403-412(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRG.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-81.

    Entry informationi

    Entry nameiTPM1_CHICK
    AccessioniPrimary (citable) accession number: P04268
    Secondary accession number(s): P02559
    , P08942, P18441, P18442, P49436, P49438, P49439, Q540N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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