ID   TPM_LEPSA               Reviewed;         284 AA.
AC   Q8T380;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Tropomyosin Lep s 1.0101 {ECO:0000305};
DE   AltName: Full=Allergen Lep s 1 {ECO:0000303|PubMed:15836758};
DE   AltName: Full=Tropomyosin Lep s 1 {ECO:0000303|PubMed:15836758};
DE   AltName: Allergen=Lep s 1.0101 {ECO:0000305};
OS   Lepisma saccharina (Silverfish).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Zygentoma;
OC   Lepismatidae; Lepisma.
OX   NCBI_TaxID=50586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=15836758; DOI=10.1111/j.1365-2222.2005.02214.x;
RA   Barletta B., Butteroni C., Puggioni E.M., Iacovacci P., Afferni C.,
RA   Tinghino R., Ariano R., Panzani R.C., Pini C., Di Felice G.;
RT   "Immunological characterization of a recombinant tropomyosin from a new
RT   indoor source, Lepisma saccharina.";
RL   Clin. Exp. Allergy 35:483-489(2005).
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 in 7% of
CC       the 133 patients allergic to arthropods including shrimp, house fly,
CC       household insects, mosquito, cockroach, spider and mites. Induces
CC       histamine release from basophils that are passively sensitized with IgE
CC       from silverfish tropomyosin-allergic patient.
CC       {ECO:0000269|PubMed:15836758}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; AJ309202; CAC84590.2; -; mRNA.
DR   AlphaFoldDB; Q8T380; -.
DR   SMR; Q8T380; -.
DR   Allergome; 3352; Lep s 1.0101.
DR   Allergome; 852; Lep s 1.
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 Lep s 1.0101"
FT                   /id="PRO_0000205687"
FT   REGION          155..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..273
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  32471 MW;  A8DC638E35C33D54 CRC64;
     MEAIKKKMQA MKLEKDNAMD KADALEAQAR DANRKADKIL EEVQDLKKKP SQVETDFTTT
     KENLATANKN LEDKEKTLTN TESEVASLNR KVQMIEENLE RSEERLGTAL TKLGEASHAA
     DEASRMCKVL ENRSQQDEER MDQLTNQLKE ARMLAEDADG KSDEVSRKMA QVEDDLEVAE
     DRVKSGDSKI MELEEELKVV GNSLKSLEVS EEKANQRVEE YKRQIKTLTV KLKEAEARAE
     YAEKYVKKLQ KEVDRLEDEL GINKDRYRAL ADEMDQTFAE LSGY