TPM_ECHMU
ID TPM_ECHMU Reviewed; 284 AA.
AC Q95PU1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Tropomyosin;
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hubert K., Frosch M., Brehm K.;
RT "Characterisation of a E. multilocularis tropomyosin encoding mRNA.";
RL Submitted (MAY-2001) 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; AJ314792; CAC85552.1; -; mRNA.
DR AlphaFoldDB; Q95PU1; -.
DR SMR; Q95PU1; -.
DR eggNOG; KOG1003; Eukaryota.
DR OMA; TEKRATN; -.
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..284
FT /note="Tropomyosin"
FT /id="PRO_0000205653"
FT REGION 97..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT COMPBIAS 111..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32987 MW; 01431F074BF8A73A CRC64;
MDSIKKKMMA MKLEKENALE KAINLENQLK EKAKDFEKKE EEMNDWLSKV KNIQTEVDTV
QESLQEAISK LEETEKRATN AEAEVAAMTR RIRLLEEDFE QSSGRLTETS TKLDDASKAA
EESERNRKTL ETRSISDDER MAQLEEQVKE AKYIAEDAER KYDEAARRLA VTEVDLERAE
SRLETSESKI VELEEELRIV GNNMKSLEVS EQESLQREES YEETIRDLTE RLKTAEQRAA
EAERQVSKLQ NEVDRLEDEL LSEKERYRAI SGELDTTFAE LTSF