TPM1_CAEEL
ID TPM1_CAEEL Reviewed; 284 AA.
AC Q22866; Q22865; Q27284; Q7K6W7; Q95Q31;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tropomyosin isoforms a/b/d/f;
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] (ISOFORMS A AND D), 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 [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 [3]
RP FUNCTION, AND MUTAGENESIS OF GLU-234.
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 [4]
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 [5]
RP ERRATUM OF PUBMED:11901171.
RA Ono S., Ono K.;
RL J. Cell Biol. 157:727-727(2002).
RN [6]
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 [7]
RP FUNCTION, AND MUTAGENESIS OF GLU-139 AND GLU-222.
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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17684058; DOI=10.1242/jcs.013516;
RA Yamashiro S., Gimona M., Ono S.;
RT "UNC-87, a calponin-related protein in C. elegans, antagonizes ADF/cofilin-
RT mediated actin filament dynamics.";
RL J. Cell Sci. 120:3022-3033(2007).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction (PubMed:9113409, PubMed:11901171). Involved in muscle actin
CC filament organization and muscle arm extension and morphology
CC (PubMed:15930100). Protects actin filaments from depolymerization by
CC unc-60 in vitro (PubMed:17684058). Also has a role in male mating
CC behavior by regulating the copulatory spicules (PubMed:16399684). Binds
CC to F-actin (PubMed:11901171). {ECO:0000269|PubMed:11901171,
CC ECO:0000269|PubMed:15930100, ECO:0000269|PubMed:16399684,
CC ECO:0000269|PubMed:17684058, ECO:0000269|PubMed:9113409}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11901171}.
CC Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:17684058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=a; Synonyms=CeTM1, CeTMI;
CC IsoId=Q22866-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q22866-3; Sequence=VSP_020645, VSP_009425;
CC Name=d; Synonyms=CeTM2, CeTMII;
CC IsoId=Q22866-2; Sequence=VSP_009425;
CC Name=f;
CC IsoId=Q22866-4; Sequence=VSP_020646, VSP_020647;
CC Name=e; Synonyms=CeTM3, CeTMIII;
CC IsoId=Q27249-1; Sequence=External;
CC Name=c; Synonyms=CeTM4, CeTMIV;
CC IsoId=Q27249-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform a and isoform d are expressed in body wall
CC muscles, vulva, anus muscles and male tail muscles (PubMed:7666414).
CC Located to the myofibrils of thin actin filaments (PubMed:11901171,
CC PubMed:17684058). {ECO:0000269|PubMed:11901171,
CC ECO:0000269|PubMed:17684058, 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
CC (PubMed:15930100). Those that survive body wall interference have
CC abnormal body morphology and uncoordinated movements, and those that
CC survive pharynx interference have deformed pharynges and gut regions
CC (PubMed:15930100). RNAi-mediated knockdown results in a wavy appearance
CC of the actin filaments in adult body wall muscles (PubMed:17684058).
CC {ECO:0000269|PubMed:15930100, ECO:0000269|PubMed:17684058}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; D38539; BAA07540.1; -; Genomic_DNA.
DR EMBL; D38539; BAA07541.1; -; Genomic_DNA.
DR EMBL; D38540; BAA07543.1; -; mRNA.
DR EMBL; D38541; BAA07544.1; -; mRNA.
DR EMBL; AL132877; CAC70112.1; -; Genomic_DNA.
DR EMBL; AL132877; CAC70113.2; -; Genomic_DNA.
DR EMBL; AL132877; CAC70114.1; -; Genomic_DNA.
DR EMBL; AL132877; CAE54913.1; -; Genomic_DNA.
DR PIR; S58921; S58921.
DR PIR; S58922; S58922.
DR RefSeq; NP_001021695.1; NM_001026524.5. [Q22866-1]
DR RefSeq; NP_001021696.1; NM_001026525.5.
DR RefSeq; NP_001021698.1; NM_001026527.1.
DR RefSeq; NP_001021700.1; NM_001026529.4.
DR AlphaFoldDB; Q22866; -.
DR SMR; Q22866; -.
DR BioGRID; 38704; 61.
DR DIP; DIP-27403N; -.
DR IntAct; Q22866; 47.
DR STRING; 6239.Y105E8B.1a; -.
DR iPTMnet; Q22866; -.
DR World-2DPAGE; 0020:Q22866; -.
DR EPD; Q22866; -.
DR PeptideAtlas; Q22866; -.
DR EnsemblMetazoa; Y105E8B.1a.1; Y105E8B.1a.1; WBGene00002978. [Q22866-1]
DR EnsemblMetazoa; Y105E8B.1b.1; Y105E8B.1b.1; WBGene00002978. [Q22866-3]
DR EnsemblMetazoa; Y105E8B.1d.1; Y105E8B.1d.1; WBGene00002978. [Q22866-2]
DR EnsemblMetazoa; Y105E8B.1f.1; Y105E8B.1f.1; WBGene00002978. [Q22866-4]
DR GeneID; 173319; -.
DR KEGG; cel:CELE_Y105E8B.1; -.
DR UCSC; Y105E8B.1e.2; c. elegans. [Q22866-1]
DR CTD; 173319; -.
DR WormBase; Y105E8B.1a; CE28782; WBGene00002978; lev-11. [Q22866-1]
DR WormBase; Y105E8B.1b; CE36223; WBGene00002978; lev-11. [Q22866-3]
DR WormBase; Y105E8B.1d; CE29060; WBGene00002978; lev-11. [Q22866-2]
DR WormBase; Y105E8B.1f; CE36224; WBGene00002978; lev-11. [Q22866-4]
DR eggNOG; KOG1003; Eukaryota.
DR HOGENOM; CLU_055027_0_2_1; -.
DR InParanoid; Q22866; -.
DR OrthoDB; 1576041at2759; -.
DR PhylomeDB; Q22866; -.
DR Reactome; R-CEL-9013424; RHOV GTPase cycle.
DR SignaLink; Q22866; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002978; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q22866; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
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: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:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
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..284
FT /note="Tropomyosin isoforms a/b/d/f"
FT /id="PRO_0000205645"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT VAR_SEQ 1..91
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020645"
FT VAR_SEQ 100..151
FT /note="ERAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEA
FT -> NFSPRRLTANTTRSPVSSPWLKLILRELRSVPRPERTRSWSLKRSCASLVIT (in
FT isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_020646"
FT VAR_SEQ 152..284
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_020647"
FT VAR_SEQ 258..284
FT /note="DELVHEKERYKTISEELDSTFQELSGY -> ELRDAEVLKARQLQDELDHMV
FT QELNSV (in isoform b and isoform d)"
FT /evidence="ECO:0000303|PubMed:7666414"
FT /id="VSP_009425"
FT MUTAGEN 139
FT /note="E->K: In lev-11-sy558; induces spicule protraction
FT (Prc phenotype). Prc phenotype is suppressible by food
FT deprivation."
FT /evidence="ECO:0000269|PubMed:16399684"
FT MUTAGEN 222
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 234
FT /note="E->K: In lev-11-x12; confers levamisole resistance."
FT /evidence="ECO:0000269|PubMed:9113409"
FT CONFLICT 277..279
FT /note="TFQ -> NLP (in Ref. 1; BAA07540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 33004 MW; 02271C870E23D2AB CRC64;
MDAIKKKMQA MKIEKDNALD RADAAEEKVR QITEKLERVE EELRDTQKKM TQTGDDLDKA
QEDLSAATSK LEEKEKTVQE AEAEVASLNR RMTLLEEELE RAEERLKIAT EKLEEATHNV
DESERVRKVM ENRSLQDEER ANTVEAQLKE AQLLAEEADR KYDEVARKLA MVEADLERAE
ERAEAGENKI VELEEELRVV GNNLKSLEVS EEKALQREDS YEEQIRTVSS RLKEAETRAE
FAERSVQKLQ KEVDRLEDEL VHEKERYKTI SEELDSTFQE LSGY
