ID   TPM_ERISI               Reviewed;         284 AA.
AC   A4URH3;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Tropomyosin {ECO:0000303|PubMed:20564455, ECO:0000303|Ref.1};
DE   AltName: Allergen=Eri s 1.0101 {ECO:0000305};
OS   Eriocheir sinensis (Chinese mitten crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Eriocheir.
OX   NCBI_TaxID=95602 {ECO:0000312|EMBL:ABO71783.1};
RN   [1] {ECO:0000312|EMBL:ABO71783.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Muscle {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.foodchem.2008.05.023;
RA   Liang Y.-L., Cao M.-J., Su W.-J., Zhang L.-J., Huang Y.-Y., Liu G.-M.;
RT   "Identification and characterisation of the major allergen of Chinese
RT   mitten crab (Eriocheir sinensis).";
RL   Food Chem. 111:998-1003(2008).
RN   [2]
RP   TISSUE SPECIFICITY, AND ALLERGEN.
RX   PubMed=20564455; DOI=10.1002/jsfa.3988;
RA   Liu G.M., Cao M.J., Huang Y.Y., Cai Q.F., Weng W.Y., Su W.J.;
RT   "Comparative study of in vitro digestibility of major allergen tropomyosin
RT   and other food proteins of Chinese mitten crab (Eriocheir sinensis).";
RL   J. Sci. Food Agric. 90:1614-1620(2010).
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   -!- TISSUE SPECIFICITY: Muscle (at protein level) (Ref.1, PubMed:20564455).
CC       Expressed in leg and chest protection muscle (at protein level)
CC       (PubMed:20564455). Expressed in claw muscle (Ref.1).
CC       {ECO:0000269|PubMed:20564455, ECO:0000269|Ref.1}.
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 (Ref.1,
CC       PubMed:20564455). Binds to IgE in 100% of the 21 patients tested
CC       allergic to crustaceans (Ref.1). Allergenicity of this protein is
CC       reduced by pepsin or chymotrypsin, and most effectively by trypsin,
CC       digestion in vitro (PubMed:20564455). {ECO:0000269|PubMed:20564455,
CC       ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC       {ECO:0000255|RuleBase:RU004515, ECO:0000305}.
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DR   EMBL; EF471314; ABO71783.1; -; mRNA.
DR   AlphaFoldDB; A4URH3; -.
DR   SMR; A4URH3; -.
DR   Allergome; 3759; Eri s 1.
DR   Allergome; 4086; Eri s 1.0101.
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_0000447993"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..273
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  32788 MW;  06F34E81FDA5EF80 CRC64;
     MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANNRAEKTE EEIRATQKKM QQVENELDQA
     QEQLSAANTK LDEKEKALQN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAESGESKI VELEEELRVV GNNLKSLEVS EEKANQREET YKEQIKTLAN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEKEKYKSI TDELDQTFSE LSGY