ID   TPM_PANBO               Reviewed;         284 AA.
AC   P86704; E5BBS3;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Tropomyosin {ECO:0000303|PubMed:23075760};
DE   AltName: Allergen=Pan b 1 {ECO:0000303|PubMed:23075760};
GN   Name=TM1 {ECO:0000250|UniProtKB:O44119};
OS   Pandalus borealis (Northern red shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC   Pandaloidea; Pandalidae; Pandalus.
OX   NCBI_TaxID=6703;
RN   [1] {ECO:0000312|EMBL:CBY17558.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN, AND MASS SPECTROMETRY.
RC   TISSUE=Tail muscle {ECO:0000312|EMBL:CBY17558.1};
RX   PubMed=23075760; DOI=10.1159/000339740;
RA   Myrset H.R., Barletta B., Di Felice G., Egaas E., Dooper M.M.B.W.;
RT   "Structural and Immunological Characterization of Recombinant Pan b 1, a
RT   Major Allergen of Northern Shrimp, Pandalus borealis.";
RL   Int. Arch. Allergy Immunol. 160:221-232(2013).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RA   Abdel Rahman A.M., Kamath S., Robinson J.J., Lopata A.L., Helleur R.J.;
RL   Submitted (JUL-2010) to UniProtKB.
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   -!- MASS SPECTROMETRY: Mass=32756; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23075760};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:23075760}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000255}.
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DR   EMBL; FR728681; CBY17558.1; -; mRNA.
DR   AlphaFoldDB; P86704; -.
DR   SMR; P86704; -.
DR   Allergome; 1277; Pan b 1.
DR   Allergome; 9076; Pan b 1.0101.
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   Acetylation; Allergen; Coiled coil; Direct protein sequencing; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin"
FT                   /id="PRO_0000413031"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..284
FT                   /evidence="ECO:0000250|UniProtKB:O44119"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   284 AA;  32753 MW;  BC1121B82F4492A8 CRC64;
     MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANNRAEKSE EEVFGLQKKL QQLENDLDSV
     QEALLKANQH LEEKDKALSN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAETGESKI VELEEELRVV GNNLKSLEVS EEKANQREEA YKEQIKTLTN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEKEKYKSI TDELDQTFSE LSGY