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Q22866 (TPM1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomyosin isoforms a/b/d/f
Alternative name(s):
Levamisole resistant protein 11
Gene names
Name:lev-11
Synonyms:tmy-1
ORF Names:Y105E8B.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.6 Ref.7

Subcellular location

Cytoplasm Ref.4.

Tissue specificity

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. Ref.1 Ref.4

Domain

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Disruption phenotype

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. Ref.6

Sequence similarities

Belongs to the tropomyosin family.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q22866-1)

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.
Isoform b (identifier: Q22866-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: Missing.
     258-284: DELVHEKERYKTISEELDSTFQELSGY → ELRDAEVLKARQLQDELDHMVQELNSV
Note: No experimental confirmation available.
Isoform d (identifier: Q22866-2)

Also known as: CeTM2; CeTMII;

The sequence of this isoform differs from the canonical sequence as follows:
     258-284: DELVHEKERYKTISEELDSTFQELSGY → ELRDAEVLKARQLQDELDHMVQELNSV
Isoform f (identifier: Q22866-4)

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.
Isoform e (identifier: Q27249-1)

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.
Isoform c (identifier: Q27249-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Tropomyosin isoforms a/b/d/f
PRO_0000205645

Regions

Coiled coil1 – 284284

Natural variations

Alternative sequence1 – 9191Missing in isoform b.
VSP_020645
Alternative sequence100 – 15152ERAEE…QLKEA → NFSPRRLTANTTRSPVSSPW LKLILRELRSVPRPERTRSW SLKRSCASLVIT in isoform f.
VSP_020646
Alternative sequence152 – 284133Missing in isoform f.
VSP_020647
Alternative sequence258 – 28427DELVH…ELSGY → ELRDAEVLKARQLQDELDHM VQELNSV in isoform b and isoform d.
VSP_009425

Experimental info

Mutagenesis1391E → K in lev-11-sy558; induces spicule protraction (Prc phenotype). Prc phenotype is suppressible by food deprivation. Ref.7
Mutagenesis2221E → K in lev-11-rg1; disrupts most steps of male mating behavior except spicule insertion. Ref.7
Mutagenesis2341E → K in lev-11-x12; confers levamisole resistance. Ref.3
Sequence conflict277 – 2793TFQ → NLP in BAA07540. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform a (CeTM1) (CeTMI) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 02271C870E23D2AB

FASTA28433,004
        10         20         30         40         50         60 
MDAIKKKMQA MKIEKDNALD RADAAEEKVR QITEKLERVE EELRDTQKKM TQTGDDLDKA 

        70         80         90        100        110        120 
QEDLSAATSK LEEKEKTVQE AEAEVASLNR RMTLLEEELE RAEERLKIAT EKLEEATHNV 

       130        140        150        160        170        180 
DESERVRKVM ENRSLQDEER ANTVEAQLKE AQLLAEEADR KYDEVARKLA MVEADLERAE 

       190        200        210        220        230        240 
ERAEAGENKI VELEEELRVV GNNLKSLEVS EEKALQREDS YEEQIRTVSS RLKEAETRAE 

       250        260        270        280 
FAERSVQKLQ KEVDRLEDEL VHEKERYKTI SEELDSTFQE LSGY 

« Hide

Isoform b [UniParc].

Checksum: D1C80E8B905C439B
Show »

FASTA19322,533
Isoform d (CeTM2) (CeTMII) [UniParc].

Checksum: D8D32CC6FB4E78F7
Show »

FASTA28432,937
Isoform f [UniParc].

Checksum: 8C82011D1356E828
Show »

FASTA15117,385
Isoform e (CeTM3) (CeTMIII) [UniParc].

See Q27249.

Isoform c (CeTM4) (CeTMIV) [UniParc].

See Q27249.

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS58921.
S58922.
RefSeqNP_001021695.1. NM_001026524.5.
NP_001021696.1. NM_001026525.5.
NP_001021698.1. NM_001026527.1.
NP_001021700.1. NM_001026529.4.
UniGeneCel.7812.

3D structure databases

ProteinModelPortalQ22866.
SMRQ22866. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid38704. 28 interactions.
DIPDIP-27403N.
IntActQ22866. 30 interactions.
MINTMINT-1117333.

2D gel databases

World-2DPAGE0020:Q22866.

Proteomic databases

PaxDbQ22866.
PRIDEQ22866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY105E8B.1a; Y105E8B.1a; Y105E8B.1. [Q22866-1]
GeneID173319.
KEGGcel:CELE_Y105E8B.1.
UCSCY105E8B.1e.2. c. elegans. [Q22866-1]

Organism-specific databases

CTD173319.
WormBaseY105E8B.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

eggNOGNOG304012.
HOGENOMHOG000231521.
InParanoidQ22866.
KOK10373.
OMAEASAEKY.
PhylomeDBQ22866.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio879141.

Entry information

Entry nameTPM1_CAEEL
AccessionPrimary (citable) accession number: Q22866
Secondary accession number(s): Q22865 expand/collapse secondary AC list , Q27284, Q7K6W7, Q95Q31
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase