ID   TPM_CHAFE               Reviewed;         264 AA.
AC   Q9N2R3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Tropomyosin Cha f 1.0101 {ECO:0000305};
DE   AltName: Full=Major allergen Cha f 1 {ECO:0000303|PubMed:23393908, ECO:0000303|PubMed:9819304};
DE   AltName: Allergen=Cha f 1.0101 {ECO:0000305};
DE   Flags: Fragment;
OS   Charybdis feriata (Crucifix crab) (Cancer feriatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Portunidae; Charybdis.
OX   NCBI_TaxID=65693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Muscle {ECO:0000303|PubMed:9819304};
RX   PubMed=9819304; DOI=10.1016/s0091-6749(98)70027-2;
RA   Leung P.S.C., Chen Y.C., Gershwin M.E., Wong S.H., Kwan H.S., Chu K.H.;
RT   "Identification and molecular characterization of Charybdis feriatus
RT   tropomyosin, the major crab allergen.";
RL   J. Allergy Clin. Immunol. 102:847-852(1998).
RN   [2]
RP   TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=23393908;
RA   Misnan R., Murad S., Yadzir Z.H., Abdullah N.;
RT   "Identification of the major allergens of Charybdis feriatus (red crab) and
RT   its cross-reactivity with Portunus pelagicus (blue crab).";
RL   Asian Pac. J. Allergy Immunol. 30:285-293(2012).
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: Expressed in muscle (at protein level)
CC       (PubMed:23393908). Expressed in claw muscles (PubMed:9819304).
CC       {ECO:0000269|PubMed:23393908, ECO:0000269|PubMed:9819304}.
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. Natural and recombinant
CC       protein binds to IgE of patients allergic to crabs (PubMed:9819304,
CC       PubMed:23393908). Recombinant protein binds to IgE in all 10 patients
CC       tested allergic to crustaceans. Cross-reacts with greasyback shrimp
CC       topomyosin allergen Met e 1.0101 and Chinese spiny lobster tropomyosin
CC       allergen Pan s 1 (PubMed:9819304). Cross-reacts with blue swimmer crab
CC       tropomyosin allergen Por p 1 (PubMed:23393908).
CC       {ECO:0000269|PubMed:23393908, ECO:0000269|PubMed:9819304}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR   EMBL; AF061783; AAF35431.1; -; mRNA.
DR   AlphaFoldDB; Q9N2R3; -.
DR   SMR; Q9N2R3; -.
DR   Allergome; 196; Cha f 1.
DR   Allergome; 3185; Cha f 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; Muscle protein; Repeat.
FT   CHAIN           1..>264
FT                   /note="Tropomyosin Cha f 1.0101"
FT                   /id="PRO_0000205673"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..>264
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:A1KYZ2"
FT   NON_TER         264
SQ   SEQUENCE   264 AA;  30436 MW;  9A376620B2D36910 CRC64;
     MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANLRAEKTE EEIRATQKKM QQVENELDQA
     QEQLSAANTK LDEKEKALQN AEGEVAALNR RIQLPEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAESGESKI VELEEELRVV GNNLKSLEVS EEKANQREET YKEQIKTLAN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEK