ID TPM_CHIKI Reviewed; 285 AA. AC O96764; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 2. DT 27-MAR-2024, entry version 49. DE RecName: Full=Tropomyosin {ECO:0000303|PubMed:15013982}; DE AltName: Full=Allergen Chi k 10 {ECO:0000303|PubMed:15013982}; DE AltName: Allergen=Chi k 10.0101 {ECO:0000305}; OS Chironomus kiiensis (Midge). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae; OC Chironominae; Chironomus. OX NCBI_TaxID=84408; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN. RX PubMed=15013982; DOI=10.1128/cdli.11.2.320-324.2004; RA Jeong K.Y., Yum H.Y., Lee I.Y., Ree H.I., Hong C.S., Kim D.S., Yong T.S.; RT "Molecular cloning and characterization of tropomyosin, a major allergen of RT Chironomus kiiensis, a dominant species of nonbiting midges in Korea."; RL Clin. Diagn. Lab. Immunol. 11:320-324(2004). 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 81% of CC the 21 patients tested allergic to adult non-biting midge C.kiiensis. CC {ECO:0000269|PubMed:15013982}. CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ012184; CAA09938.2; -; mRNA. DR AlphaFoldDB; O96764; -. DR SMR; O96764; -. DR Allergome; 200; Chi k 10. DR Allergome; 3191; Chi k 10.0101. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB. DR Gene3D; 1.20.5.170; -; 2. DR Gene3D; 1.20.5.340; -; 1. DR InterPro; IPR000533; Tropomyosin. DR PANTHER; PTHR19269; TROPOMYOSIN; 1. DR PANTHER; PTHR19269:SF45; TROPOMYOSIN-1, ISOFORMS 33_34; 1. DR Pfam; PF00261; Tropomyosin; 2. DR PRINTS; PR00194; TROPOMYOSIN. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS00326; TROPOMYOSIN; 1. PE 1: Evidence at protein level; KW Allergen; Coiled coil; Muscle protein; Repeat. FT CHAIN 1..285 FT /note="Tropomyosin" FT /id="PRO_0000205683" FT COILED 1..273 FT /evidence="ECO:0000255" SQ SEQUENCE 285 AA; 32533 MW; DCA3FE9C05809FF4 CRC64; MDAIKKKMQA MKLEKDNALD RALLCENQAR DANLRAEKAE EEARTLQKKI QTIENDLDQT QGQETLVNGK LEGKEKALQN AESEVAALNR RIQLLGEDLD RSEERLASAT AKLSEASAAA DESERARKIL ENRSLADEER MDALENQLKE ARFLAEEADK KYDEVARKLA MVEADLERAE ERAEAGEAKI VELEEELRVV GNNLKSLEVS EEKANQREEE YKNQIKTLTT RLKEAEARAE FAERSVQKLQ KEVDRLEDEL VSEKEKYREI GDDLDTAFVE LILKE //