TPM_TRISP
ID TPM_TRISP Reviewed; 284 AA.
AC Q95VA8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Tropomyosin;
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12590666; DOI=10.1079/joh2002153;
RA Nakada T., Nagano I., Wu Z., Takahashi Y.;
RT "Molecular cloning and expression of the full-length tropomyosin gene from
RT Trichinella spiralis.";
RL J. Helminthol. 77:57-63(2003).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction.
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; AF419300; AAL14704.1; -; mRNA.
DR AlphaFoldDB; Q95VA8; -.
DR SMR; Q95VA8; -.
DR STRING; 6334.EFV49100; -.
DR eggNOG; KOG1003; Eukaryota.
DR HOGENOM; CLU_055027_0_2_1; -.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin"
FT /id="PRO_0000205650"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
SQ SEQUENCE 284 AA; 33231 MW; 24519CE24AFAF6E9 CRC64;
MDAIKKKMQA MKIEKDNAMD RADAAEEKAR QQQERVEKLE EELRDTQKKM MQVENELDKA
QEELTGANAQ LEEKEKKVQE AEAEVAALNR RIQLLEEDFE RAEERLIIAT EKLGEASQTA
DESERVRKVM ENRSLQDEER VYQLEAQLKE AQLLAEEADR KYDEVARKLA MVEADLERAE
ERAEAGENKI VELEEELRVV GNNLKSLEVS EEKALQREDS YEEQIRLLTQ RLKEAETRAE
FAERSVQKLQ KEVDRLEDEL VHEKEKYKAI SEELDQTFQE LSGY