TPM_ECHGR
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 25-MAY-2022, entry version 44.
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}.
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DR EMBL; AF011923; AAB65799.4; -; mRNA.
DR AlphaFoldDB; O16127; -.
DR SMR; O16127; -.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
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