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Protein

Tropomyosin isoforms c/e

Gene

lev-11

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • actin filament binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • embryo development Source: UniProtKB
  • locomotion Source: UniProtKB
  • negative regulation of actin filament depolymerization Source: WormBase
  • regulation of actin filament polymerization Source: WormBase
  • regulation of protein binding Source: WormBase
  • spicule insertion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-CEL-445355. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin isoforms c/e
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
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiY105E8B.1c; CE29059; WBGene00002978; lev-11.
Y105E8B.1e; CE31733; WBGene00002978; lev-11.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • striated muscle thin filament Source: WormBase
Complete GO annotation...

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
Mutagenesisi194 – 1941E → K in lev-11-rg1; disrupts most steps of male mating behavior except spicule insertion. 1 Publication
Mutagenesisi206 – 2061E → K in lev-11-x12; confers levamisole resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Tropomyosin isoforms c/ePRO_0000205646Add
BLAST

Proteomic databases

EPDiQ27249.
PeptideAtlasiQ27249.
PRIDEiQ27249.

Expressioni

Tissue specificityi

Isoform e is expressed in the pharyngeal muscles, germline tissue and intestinal cells. Isoform c is expressed in the pharyngeal and intestinal cells.3 Publications

Gene expression databases

ExpressionAtlasiQ27249. baseline.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: UniProtKB

Protein-protein interaction databases

BioGridi38704. 28 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ27249.
SMRiQ27249. Positions 18-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 256256Add
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

GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.

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. AlignAdd to basket

Isoform e (identifier: Q27249-1) [UniParc]FASTAAdd to basket

Also known as: CeTM3, CeTMIII

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

        10         20         30         40         50
MSKVNKEGAQ QTSLLDVLKK KMRQAREEAE AAKDEADEVK RQLEEERKKR
60 70 80 90 100
EDAEAEVAAL NRRIVLVEED LERTEDRLKT ATSKLEQATK AADEADRARK
110 120 130 140 150
SMETRSQQDE ERANFLETQV DEAKVIAEDA DRKYEEVARK LAMVEADLER
160 170 180 190 200
AEERAEAGEN KIVELEEELR VVGNNLKSLE VSEEKALQRE DSYEEQIRTV
210 220 230 240 250
SSRLKEAETR AEFAERSVQK LQKEVDRLED ELLLEKERVR NLTEEIEQTV

QEIQGS
Length:256
Mass (Da):29,632
Last modified:November 1, 1996 - v1
Checksum:i84144312558238C5
GO
Isoform c (identifier: Q27249-2) [UniParc]FASTAAdd to basket

Also known as: CeTM4, CeTMIV

The sequence of this isoform differs from the canonical sequence as follows:
     98-134: ARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKY → SRRALSNQIDMDDDRCSDLERKLRECQSILHETENKA
     230-256: DELLLEKERVRNLTEEIEQTVQEIQGS → ELRDAEVLKARQLQDELDHMVQELNSV

Show »
Length:256
Mass (Da):29,630
Checksum:i72A5CD71CC97A5F6
GO
Isoform a (identifier: Q22866-1) [UniParc]FASTAAdd to basket

Also known as: CeTM1, CeTMI

The sequence of this isoform can be found in the external entry Q22866.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:284
Mass (Da):33,004
GO
Isoform d (identifier: Q22866-2) [UniParc]FASTAAdd to basket

Also known as: CeTM2, CeTMII

The sequence of this isoform can be found in the external entry Q22866.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:284
Mass (Da):32,937
GO
Isoform b (identifier: Q22866-3) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry Q22866.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.
Length:193
Mass (Da):22,533
GO
Isoform f (identifier: Q22866-4) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry Q22866.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.
Length:151
Mass (Da):17,385
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei98 – 13437ARKSM…ADRKY → SRRALSNQIDMDDDRCSDLE RKLRECQSILHETENKA in isoform c. 1 PublicationVSP_020648Add
BLAST
Alternative sequencei230 – 25627DELLL…EIQGS → ELRDAEVLKARQLQDELDHM VQELNSV in isoform c. 1 PublicationVSP_020649Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38542 mRNA. Translation: BAA07545.1.
D38539 Genomic DNA. Translation: BAA07542.1.
AF298180 mRNA. Translation: AAG10302.1.
AL132877 Genomic DNA. Translation: CAC70115.1.
AL132877 Genomic DNA. Translation: CAD45604.1.
PIRiS58923.
RefSeqiNP_001021697.1. NM_001026526.4. [Q27249-2]
NP_001021699.1. NM_001026528.3. [Q27249-1]
UniGeneiCel.7812.

Genome annotation databases

EnsemblMetazoaiY105E8B.1e.1; Y105E8B.1e.1; WBGene00002978. [Q27249-1]
Y105E8B.1e.2; Y105E8B.1e.2; WBGene00002978. [Q27249-1]
GeneIDi173319.
UCSCiY105E8B.1e.2. c. elegans. [Q27249-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38542 mRNA. Translation: BAA07545.1.
D38539 Genomic DNA. Translation: BAA07542.1.
AF298180 mRNA. Translation: AAG10302.1.
AL132877 Genomic DNA. Translation: CAC70115.1.
AL132877 Genomic DNA. Translation: CAD45604.1.
PIRiS58923.
RefSeqiNP_001021697.1. NM_001026526.4. [Q27249-2]
NP_001021699.1. NM_001026528.3. [Q27249-1]
UniGeneiCel.7812.

3D structure databases

ProteinModelPortaliQ27249.
SMRiQ27249. Positions 18-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38704. 28 interactions.

Proteomic databases

EPDiQ27249.
PeptideAtlasiQ27249.
PRIDEiQ27249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY105E8B.1e.1; Y105E8B.1e.1; WBGene00002978. [Q27249-1]
Y105E8B.1e.2; Y105E8B.1e.2; WBGene00002978. [Q27249-1]
GeneIDi173319.
UCSCiY105E8B.1e.2. c. elegans. [Q27249-1]

Organism-specific databases

CTDi173319.
WormBaseiY105E8B.1c; CE29059; WBGene00002978; lev-11.
Y105E8B.1e; CE31733; WBGene00002978; lev-11.

Phylogenomic databases

GeneTreeiENSGT00550000074494.
HOGENOMiHOG000231522.

Enzyme and pathway databases

ReactomeiR-CEL-445355. Smooth Muscle Contraction.

Gene expression databases

ExpressionAtlasiQ27249. baseline.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM E), TISSUE SPECIFICITY.
    Strain: Bristol N2.
  2. "The third and fourth tropomyosin isoforms of Caenorhabditis elegans are expressed in the pharynx and intestines and are essential for development and morphology."
    Anyanful A., Sakube Y., Takuwa K., Kagawa H.
    J. Mol. Biol. 313:525-537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), TISSUE SPECIFICITY.
  3. "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.
  4. "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-206.
  5. "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.
  6. Erratum
    Ono S., Ono K.
    J. Cell Biol. 157:727-727(2002)
  7. "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.
  8. "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-194.

Entry informationi

Entry nameiTPM3_CAEEL
AccessioniPrimary (citable) accession number: Q27249
Secondary accession number(s): Q9GSR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 91 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.