TPM_CAEBR
ID TPM_CAEBR Reviewed; 256 AA.
AC Q60UW4; A8XWA7; H8WHA7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tropomyosin;
DE AltName: Full=Levamisole resistant protein 11;
GN Name=lev-11 {ECO:0000250|UniProtKB:Q27249}; ORFNames=CBG19793;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q27249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q27249}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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DR EMBL; HE601474; CCG58661.1; -; Genomic_DNA.
DR RefSeq; XP_002640726.1; XM_002640680.1.
DR AlphaFoldDB; Q60UW4; -.
DR SMR; Q60UW4; -.
DR EnsemblMetazoa; CBG19793h.1; CBG19793h.1; WBGene00038957.
DR GeneID; 8582720; -.
DR KEGG; cbr:CBG_19793; -.
DR CTD; 8582720; -.
DR WormBase; CBG19793a; CBP39999; WBGene00038957; Cbr-lev-11.
DR HOGENOM; CLU_055027_2_0_1; -.
DR InParanoid; Q60UW4; -.
DR OMA; DEASRMC; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 3: Inferred from homology;
KW Actin-binding; Coiled coil; Cytoplasm; Muscle protein; Reference proteome.
FT CHAIN 1..256
FT /note="Tropomyosin"
FT /id="PRO_0000274536"
FT REGION 23..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..256
FT /evidence="ECO:0000255"
SQ SEQUENCE 256 AA; 29630 MW; 7599F445015ADB48 CRC64;
MSKVNKEGAQ QTSLLDVLKK KMRQAREEAE AAKDEADEVK RQLEEERKKR EDAEAEVAAL
NRRIVLVEED LERTEDRLKV ATSKLEQATK AADEADRARK SMETRSQQDE ERANFLETQV
DEAKVIAEDA DRKYEEVARK LAMVEADLER AEERAEAGEN KIVELEEELR VVGNNLKSLE
VSEEKALQRE DSYEEQIRTV SSRLKEAETR AEFAERSVQK LQKEVDRLED ELLLEKERVR
NLTEEIEQTV QEIQGS
