TPM_SCHHA
ID TPM_SCHHA Reviewed; 284 AA.
AC Q26503;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Tropomyosin;
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nicholson L.J., Karim A.M., Loverde P.T.;
RT "Comparison of the amino acid sequences for Schistosoma haematobium
RT tropomyosin and S. japonicum tropomyosin with that of S. mansoni
RT tropomyosin.";
RL Submitted (FEB-1996) 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; L76202; AAA88530.1; -; mRNA.
DR AlphaFoldDB; Q26503; -.
DR SMR; Q26503; -.
DR PRIDE; Q26503; -.
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_0000205654"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
SQ SEQUENCE 284 AA; 32982 MW; 8E0FAA7EA9ABD446 CRC64;
MDGIKKKMIA MKLEKENAME RAVQYEELLK KKEEEREKRE SEIAELNTKM KQAQIDCDEV
QETLQEQMNK LEETDKRATN AEAEVAAMTR RIRLLEEDLE VSSSRLTETL TKLEEASKTA
EESERGRKDL EIRSIADDER LNQLEDQQKE AKYIAEDADR KYDEAARKLA IAEVDFKRAE
ARLEAAESKI VELEEELRVI GNNMKALEIS EQESAQREES YEETIRDLTE RLKAAEQRAT
EAERQVSKLQ NEVDHLEDDL LAEKERYKAL SGELDQTFAE LTGY