ID TPM_ECHGR Reviewed; 278 AA. AC O16127; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 3. DT 27-MAR-2024, entry version 46. DE RecName: Full=Tropomyosin A; DE Short=EgTrpA; DE Flags: Fragment; OS Echinococcus granulosus (Hydatid tapeworm). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda; OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus; OC Echinococcus granulosus group. OX NCBI_TaxID=6210; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Esteves A., Senorale M., Fernandez C., Bruzzone H., Ehrlich R.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays CC a central role in the calcium dependent regulation of muscle CC contraction. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. 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 -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF011923; AAB65799.4; -; mRNA. DR AlphaFoldDB; O16127; -. DR SMR; O16127; -. DR Gene3D; 1.20.5.170; -; 2. DR Gene3D; 1.20.5.340; -; 1. DR InterPro; IPR000533; Tropomyosin. DR PANTHER; PTHR19269; TROPOMYOSIN; 1. DR PANTHER; PTHR19269:SF45; TROPOMYOSIN-1, ISOFORMS 33_34; 1. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR SUPFAM; SSF57997; Tropomyosin; 1. PE 2: Evidence at transcript level; KW Coiled coil; Repeat. FT CHAIN <1..278 FT /note="Tropomyosin A" FT /id="PRO_0000205652" FT REGION 92..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED <1..270 FT /evidence="ECO:0000250" FT COMPBIAS 105..134 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 SQ SEQUENCE 278 AA; 32269 MW; 5227AEEB1B358885 CRC64; IMMAMKLEKE NALEKAINLE NQLKEKAKDF EKKEEEMNDW LSKVKNIQTE VDTVQESLQE AISKLEETEK RATNAEAEVA AMTRRIRLLE EDFEQSSGRL TETSTKLDDA SKAAEESERN RKTLETRSIS DDERMAQLEE QVKEAKYIAE DAERKYDEAA RRLAVTEVDL ERAESRLETS ESKIVELEEE LRIVGNNMKS LEVSEQESLQ REESYEETIR DLTERLKTAE QRAAEAERQV SKLQNEVDRL EDELLSEKER YRAISGELDT TFAELTSF //