TPM3_CAEEL
ID TPM3_CAEEL Reviewed; 256 AA.
AC Q27249; Q9GSR4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Tropomyosin isoforms c/e;
DE AltName: Full=Levamisole resistant protein 11;
GN Name=lev-11; Synonyms=tmy-1; ORFNames=Y105E8B.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM E), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=7666414; DOI=10.1006/jmbi.1995.0459;
RA Kagawa H., Sugimoto K., Matsumoto H., Inoue T., Imadzu H., Takuwa K.,
RA Sakube Y.;
RT "Genome structure, mapping and expression of the tropomyosin gene tmy-1 of
RT Caenorhabditis elegans.";
RL J. Mol. Biol. 251:603-613(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND TISSUE SPECIFICITY.
RX PubMed=11676537; DOI=10.1006/jmbi.2001.5052;
RA Anyanful A., Sakube Y., Takuwa K., Kagawa H.;
RT "The third and fourth tropomyosin isoforms of Caenorhabditis elegans are
RT expressed in the pharynx and intestines and are essential for development
RT and morphology.";
RL J. Mol. Biol. 313:525-537(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF GLU-206.
RX PubMed=9113409; DOI=10.1247/csf.22.213;
RA Kagawa H., Takuwa K., Sakube Y.;
RT "Mutations and expressions of the tropomyosin gene and the troponin C gene
RT of Caenorhabditis elegans.";
RL Cell Struct. Funct. 22:213-218(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11901171; DOI=10.1083/jcb.200110013;
RA Ono S., Ono K.;
RT "Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics.";
RL J. Cell Biol. 156:1065-1076(2002).
RN [6]
RP ERRATUM OF PUBMED:11901171.
RA Ono S., Ono K.;
RL J. Cell Biol. 157:727-727(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15930100; DOI=10.1242/dev.01883;
RA Dixon S.J., Roy P.J.;
RT "Muscle arm development in Caenorhabditis elegans.";
RL Development 132:3079-3092(2005).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLU-194.
RX PubMed=16399684; DOI=10.1523/jneurosci.3364-05.2006;
RA Gruninger T.R., Gualberto D.G., LeBoeuf B., Garcia L.R.;
RT "Integration of male mating and feeding behaviors in Caenorhabditis
RT elegans.";
RL J. Neurosci. 26:169-179(2006).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction. Involved in muscle actin filament organization and muscle
CC arm extension and morphology. Also has a role in male mating behavior
CC by regulating the copulatory spicules. Binds to F-actin.
CC {ECO:0000269|PubMed:11901171, ECO:0000269|PubMed:15930100,
CC ECO:0000269|PubMed:16399684, ECO:0000269|PubMed:9113409}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11901171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=e; Synonyms=CeTM3, CeTMIII;
CC IsoId=Q27249-1; Sequence=Displayed;
CC Name=c; Synonyms=CeTM4, CeTMIV;
CC IsoId=Q27249-2; Sequence=VSP_020648, VSP_020649;
CC Name=a; Synonyms=CeTM1, CeTMI;
CC IsoId=Q22866-1; Sequence=External;
CC Name=d; Synonyms=CeTM2, CeTMII;
CC IsoId=Q22866-2; Sequence=External;
CC Name=b;
CC IsoId=Q22866-3; Sequence=External;
CC Name=f;
CC IsoId=Q22866-4; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform e is expressed in the pharyngeal muscles,
CC germline tissue and intestinal cells. Isoform c is expressed in the
CC pharyngeal and intestinal cells. {ECO:0000269|PubMed:11676537,
CC ECO:0000269|PubMed:11901171, ECO:0000269|PubMed:7666414}.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC polypeptide chains. The sequence exhibits a prominent seven-residues
CC periodicity.
CC -!- DISRUPTION PHENOTYPE: Worms have 50-75% embryonic lethality. Those that
CC survive body wall interference have abnormal body morphology and
CC uncoordinated movements, and those that survive pharynx interference
CC have deformed pharynges and gut regions. {ECO:0000269|PubMed:15930100}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; D38542; BAA07545.1; -; mRNA.
DR EMBL; D38539; BAA07542.1; -; Genomic_DNA.
DR EMBL; AF298180; AAG10302.1; -; mRNA.
DR EMBL; AL132877; CAC70115.1; -; Genomic_DNA.
DR EMBL; AL132877; CAD45604.1; -; Genomic_DNA.
DR PIR; S58923; S58923.
DR RefSeq; NP_001021697.1; NM_001026526.4. [Q27249-2]
DR RefSeq; NP_001021699.1; NM_001026528.3.
DR AlphaFoldDB; Q27249; -.
DR SMR; Q27249; -.
DR BioGRID; 38704; 61.
DR EPD; Q27249; -.
DR PeptideAtlas; Q27249; -.
DR EnsemblMetazoa; Y105E8B.1c.1; Y105E8B.1c.1; WBGene00002978. [Q27249-2]
DR EnsemblMetazoa; Y105E8B.1e.1; Y105E8B.1e.1; WBGene00002978. [Q27249-1]
DR EnsemblMetazoa; Y105E8B.1e.2; Y105E8B.1e.2; WBGene00002978. [Q27249-1]
DR GeneID; 173319; -.
DR UCSC; Y105E8B.1e.2; c. elegans. [Q27249-1]
DR CTD; 173319; -.
DR WormBase; Y105E8B.1c; CE29059; WBGene00002978; lev-11. [Q27249-2]
DR WormBase; Y105E8B.1e; CE31733; WBGene00002978; lev-11. [Q27249-1]
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_2_0_1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002978; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q27249; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:WormBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:WormBase.
DR GO; GO:0043393; P:regulation of protein binding; IDA:WormBase.
DR GO; GO:0034609; P:spicule insertion; IMP:UniProtKB.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Muscle protein; Reference proteome.
FT CHAIN 1..256
FT /note="Tropomyosin isoforms c/e"
FT /id="PRO_0000205646"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..256
FT VAR_SEQ 98..134
FT /note="ARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKY -> SRRALSNQIDM
FT DDDRCSDLERKLRECQSILHETENKA (in isoform c)"
FT /evidence="ECO:0000303|PubMed:11676537"
FT /id="VSP_020648"
FT VAR_SEQ 230..256
FT /note="DELLLEKERVRNLTEEIEQTVQEIQGS -> ELRDAEVLKARQLQDELDHMV
FT QELNSV (in isoform c)"
FT /evidence="ECO:0000303|PubMed:11676537"
FT /id="VSP_020649"
FT MUTAGEN 194
FT /note="E->K: In lev-11-rg1; disrupts most steps of male
FT mating behavior except spicule insertion."
FT /evidence="ECO:0000269|PubMed:16399684"
FT MUTAGEN 206
FT /note="E->K: In lev-11-x12; confers levamisole resistance."
FT /evidence="ECO:0000269|PubMed:9113409"
SQ SEQUENCE 256 AA; 29632 MW; 84144312558238C5 CRC64;
MSKVNKEGAQ QTSLLDVLKK KMRQAREEAE AAKDEADEVK RQLEEERKKR EDAEAEVAAL
NRRIVLVEED LERTEDRLKT ATSKLEQATK AADEADRARK SMETRSQQDE ERANFLETQV
DEAKVIAEDA DRKYEEVARK LAMVEADLER AEERAEAGEN KIVELEEELR VVGNNLKSLE
VSEEKALQRE DSYEEQIRTV SSRLKEAETR AEFAERSVQK LQKEVDRLED ELLLEKERVR
NLTEEIEQTV QEIQGS
