ID   TPM_PERVI               Reviewed;         284 AA.
AC   Q9GZ70;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Tropomyosin {ECO:0000303|PubMed:11246417};
DE   AltName: Allergen=Per v 1 {ECO:0000303|PubMed:11246417};
OS   Perna viridis (Asian green mussel) (Mytilus viridis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Perna.
OX   NCBI_TaxID=73031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC   TISSUE=Adductor muscle {ECO:0000303|PubMed:11246417};
RX   PubMed=11246417; DOI=10.1007/s101260000035;
RA   Chu K.H., Wong S.H., Leung P.S.;
RT   "Tropomyosin Is the Major Mollusk Allergen: Reverse Transcriptase
RT   Polymerase Chain Reaction, Expression and IgE Reactivity.";
RL   Mar. Biotechnol. 2:499-509(2000).
CC   -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC       a central role in the calcium dependent regulation of muscle
CC       contraction. {ECO:0000250|UniProtKB:Q22866}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A2V735}.
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. {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       patients allergic to shellfish (mollusks and crustaceans).
CC       {ECO:0000269|PubMed:11246417}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; AF216519; AAG08988.1; -; mRNA.
DR   AlphaFoldDB; Q9GZ70; -.
DR   SMR; Q9GZ70; -.
DR   Allergome; 823; Per v 1.
DR   PRIDE; Q9GZ70; -.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   1: Evidence at protein level;
KW   Allergen; Coiled coil; Muscle protein; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin"
FT                   /id="PRO_0000205671"
FT   REGION          110..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..273
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  32749 MW;  EE0B6FB4B2CB3D06 CRC64;
     MDAIKKKMVA MKMEKKNALD RAEQLEQKLR ETEEAKAKIE DDYNSLVKKN IQTENDYDNC
     NTQLQDVQAK YERAEKQIQE HEQEIQSLTR KISLLEEGIM KAEERFTTAS GKLEEASKAA
     DESERNRKVL ENLNSGNDER IDQLEKQLTE AKWIAEEADK KYEEAARKLA ITEVDLERAE
     ARLEAAEAKV IDLEEQLTVV GANIKTLQVQ NDQASQREDS YEETIRDLTN RLKDAENRAT
     EAERTVSKLQ KEVDRLEDEL LTEKEKYKAI SDELDATFAE LAGY