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Q22866

- TPM1_CAEEL

UniProt

Q22866 - TPM1_CAEEL

Protein

Tropomyosin isoforms a/b/d/f

Gene

lev-11

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. Involved in muscle actin filament organization and muscle arm extension and morphology. Also has a role in male mating behavior by regulating the copulatory spicules. Binds to F-actin.4 Publications

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: UniProtKB
    2. locomotion Source: UniProtKB
    3. negative regulation of actin filament depolymerization Source: WormBase
    4. regulation of actin filament polymerization Source: WormBase
    5. regulation of protein binding Source: WormBase
    6. spicule insertion Source: UniProtKB

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin isoforms a/b/d/f
    Alternative name(s):
    Levamisole resistant protein 11
    Gene namesi
    Name:lev-11
    Synonyms:tmy-1
    ORF Names:Y105E8B.1
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome I

    Organism-specific databases

    WormBaseiY105E8B.1a; CE28782; WBGene00002978; lev-11.
    Y105E8B.1b; CE36223; WBGene00002978; lev-11.
    Y105E8B.1d; CE29060; WBGene00002978; lev-11.
    Y105E8B.1f; CE36224; WBGene00002978; lev-11.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. striated muscle thin filament Source: WormBase

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Worms have 50-75% embryonic lethality. Those that survive body wall interference have abnormal body morphology and uncoordinated movements, and those that survive pharynx interference have deformed pharynges and gut regions.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391E → K in lev-11-sy558; induces spicule protraction (Prc phenotype). Prc phenotype is suppressible by food deprivation. 1 Publication
    Mutagenesisi222 – 2221E → K in lev-11-rg1; disrupts most steps of male mating behavior except spicule insertion. 1 Publication
    Mutagenesisi234 – 2341E → K in lev-11-x12; confers levamisole resistance. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin isoforms a/b/d/fPRO_0000205645Add
    BLAST

    Proteomic databases

    PaxDbiQ22866.
    PRIDEiQ22866.

    2D gel databases

    World-2DPAGE0020:Q22866.

    Expressioni

    Tissue specificityi

    Isoform a and isoform d are expressed in body wall muscles, vulva, anus muscles and male tail muscles. Located to the myofibrils of thin actin filaments.2 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi38704. 28 interactions.
    DIPiDIP-27403N.
    IntActiQ22866. 30 interactions.
    MINTiMINT-1117333.

    Structurei

    3D structure databases

    ProteinModelPortaliQ22866.
    SMRiQ22866. Positions 1-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1 – 284284Add
    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.
    HOGENOMiHOG000231521.
    InParanoidiQ22866.
    KOiK10373.
    OMAiEASAEKY.
    PhylomeDBiQ22866.

    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

    Isoform a (identifier: Q22866-1) [UniParc]FASTAAdd to Basket

    Also known as: CeTM1, CeTMI

    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

    MDAIKKKMQA MKIEKDNALD RADAAEEKVR QITEKLERVE EELRDTQKKM    50
    TQTGDDLDKA QEDLSAATSK LEEKEKTVQE AEAEVASLNR RMTLLEEELE 100
    RAEERLKIAT EKLEEATHNV DESERVRKVM ENRSLQDEER ANTVEAQLKE 150
    AQLLAEEADR KYDEVARKLA MVEADLERAE ERAEAGENKI VELEEELRVV 200
    GNNLKSLEVS EEKALQREDS YEEQIRTVSS RLKEAETRAE FAERSVQKLQ 250
    KEVDRLEDEL VHEKERYKTI SEELDSTFQE LSGY 284
    Length:284
    Mass (Da):33,004
    Last modified:November 1, 1996 - v1
    Checksum:i02271C870E23D2AB
    GO
    Isoform b (identifier: Q22866-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-91: Missing.
         258-284: DELVHEKERYKTISEELDSTFQELSGY → ELRDAEVLKARQLQDELDHMVQELNSV

    Note: No experimental confirmation available.

    Show »
    Length:193
    Mass (Da):22,533
    Checksum:iD1C80E8B905C439B
    GO
    Isoform d (identifier: Q22866-2) [UniParc]FASTAAdd to Basket

    Also known as: CeTM2, CeTMII

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

    Show »
    Length:284
    Mass (Da):32,937
    Checksum:iD8D32CC6FB4E78F7
    GO
    Isoform f (identifier: Q22866-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         100-151: ERAEERLKIA...NTVEAQLKEA → NFSPRRLTAN...KRSCASLVIT
         152-284: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:151
    Mass (Da):17,385
    Checksum:i8C82011D1356E828
    GO
    Isoform e (identifier: Q27249-1) [UniParc]FASTAAdd to Basket

    Also known as: CeTM3, CeTMIII

    The sequence of this isoform can be found in the external entry Q27249.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:256
    Mass (Da):29,632
    GO
    Isoform c (identifier: Q27249-2) [UniParc]FASTAAdd to Basket

    Also known as: CeTM4, CeTMIV

    The sequence of this isoform can be found in the external entry Q27249.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:256
    Mass (Da):29,630
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti277 – 2793TFQ → NLP in BAA07540. (PubMed:7666414)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9191Missing in isoform b. CuratedVSP_020645Add
    BLAST
    Alternative sequencei100 – 15152ERAEE…QLKEA → NFSPRRLTANTTRSPVSSPW LKLILRELRSVPRPERTRSW SLKRSCASLVIT in isoform f. CuratedVSP_020646Add
    BLAST
    Alternative sequencei152 – 284133Missing in isoform f. CuratedVSP_020647Add
    BLAST
    Alternative sequencei258 – 28427DELVH…ELSGY → ELRDAEVLKARQLQDELDHM VQELNSV in isoform b and isoform d. 1 PublicationVSP_009425Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38539 Genomic DNA. Translation: BAA07540.1.
    D38539 Genomic DNA. Translation: BAA07541.1.
    D38540 mRNA. Translation: BAA07543.1.
    D38541 mRNA. Translation: BAA07544.1.
    AL132877 Genomic DNA. Translation: CAC70112.1.
    AL132877 Genomic DNA. Translation: CAC70113.2.
    AL132877 Genomic DNA. Translation: CAC70114.1.
    AL132877 Genomic DNA. Translation: CAE54913.1.
    PIRiS58921.
    S58922.
    RefSeqiNP_001021695.1. NM_001026524.5. [Q22866-1]
    NP_001021696.1. NM_001026525.5. [Q22866-3]
    NP_001021698.1. NM_001026527.1. [Q22866-2]
    NP_001021700.1. NM_001026529.4. [Q22866-4]
    UniGeneiCel.7812.

    Genome annotation databases

    EnsemblMetazoaiY105E8B.1a; Y105E8B.1a; WBGene00002978. [Q22866-1]
    GeneIDi173319.
    KEGGicel:CELE_Y105E8B.1.
    UCSCiY105E8B.1e.2. c. elegans. [Q22866-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38539 Genomic DNA. Translation: BAA07540.1 .
    D38539 Genomic DNA. Translation: BAA07541.1 .
    D38540 mRNA. Translation: BAA07543.1 .
    D38541 mRNA. Translation: BAA07544.1 .
    AL132877 Genomic DNA. Translation: CAC70112.1 .
    AL132877 Genomic DNA. Translation: CAC70113.2 .
    AL132877 Genomic DNA. Translation: CAC70114.1 .
    AL132877 Genomic DNA. Translation: CAE54913.1 .
    PIRi S58921.
    S58922.
    RefSeqi NP_001021695.1. NM_001026524.5. [Q22866-1 ]
    NP_001021696.1. NM_001026525.5. [Q22866-3 ]
    NP_001021698.1. NM_001026527.1. [Q22866-2 ]
    NP_001021700.1. NM_001026529.4. [Q22866-4 ]
    UniGenei Cel.7812.

    3D structure databases

    ProteinModelPortali Q22866.
    SMRi Q22866. Positions 1-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 38704. 28 interactions.
    DIPi DIP-27403N.
    IntActi Q22866. 30 interactions.
    MINTi MINT-1117333.

    2D gel databases

    World-2DPAGE 0020:Q22866.

    Proteomic databases

    PaxDbi Q22866.
    PRIDEi Q22866.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai Y105E8B.1a ; Y105E8B.1a ; WBGene00002978 . [Q22866-1 ]
    GeneIDi 173319.
    KEGGi cel:CELE_Y105E8B.1.
    UCSCi Y105E8B.1e.2. c. elegans. [Q22866-1 ]

    Organism-specific databases

    CTDi 173319.
    WormBasei Y105E8B.1a ; CE28782 ; WBGene00002978 ; lev-11.
    Y105E8B.1b ; CE36223 ; WBGene00002978 ; lev-11.
    Y105E8B.1d ; CE29060 ; WBGene00002978 ; lev-11.
    Y105E8B.1f ; CE36224 ; WBGene00002978 ; lev-11.

    Phylogenomic databases

    eggNOGi NOG304012.
    GeneTreei ENSGT00550000074494.
    HOGENOMi HOG000231521.
    InParanoidi Q22866.
    KOi K10373.
    OMAi EASAEKY.
    PhylomeDBi Q22866.

    Miscellaneous databases

    NextBioi 879141.

    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. "Genome structure, mapping and expression of the tropomyosin gene tmy-1 of Caenorhabditis elegans."
      Kagawa H., Sugimoto K., Matsumoto H., Inoue T., Imadzu H., Takuwa K., Sakube Y.
      J. Mol. Biol. 251:603-613(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND D), TISSUE SPECIFICITY.
      Strain: Bristol N2.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
      Strain: Bristol N2.
    3. "Mutations and expressions of the tropomyosin gene and the troponin C gene of Caenorhabditis elegans."
      Kagawa H., Takuwa K., Sakube Y.
      Cell Struct. Funct. 22:213-218(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLU-234.
    4. "Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics."
      Ono S., Ono K.
      J. Cell Biol. 156:1065-1076(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. Erratum
      Ono S., Ono K.
      J. Cell Biol. 157:727-727(2002)
    6. "Muscle arm development in Caenorhabditis elegans."
      Dixon S.J., Roy P.J.
      Development 132:3079-3092(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Integration of male mating and feeding behaviors in Caenorhabditis elegans."
      Gruninger T.R., Gualberto D.G., LeBoeuf B., Garcia L.R.
      J. Neurosci. 26:169-179(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLU-139 AND GLU-222.

    Entry informationi

    Entry nameiTPM1_CAEEL
    AccessioniPrimary (citable) accession number: Q22866
    Secondary accession number(s): Q22865
    , Q27284, Q7K6W7, Q95Q31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3