ID   TPM_PORPE               Reviewed;         284 AA.
AC   M1H607;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Tropomyosin Por p 1.0101 {ECO:0000305};
DE   AltName: Full=Major allergen Por p 1 {ECO:0000303|PubMed:23840718};
DE   AltName: Allergen=Por p 1.0101 {ECO:0000303|PubMed:23840718};
OS   Portunus pelagicus (Blue swimmer crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Portunidae; Portunus.
OX   NCBI_TaxID=80836 {ECO:0000312|EMBL:AGE44125.1};
RN   [1] {ECO:0000312|EMBL:AGE44125.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 77-90; 92-101;
RP   141-149; 168-178; 190-198 AND 252-264, TISSUE SPECIFICITY, IDENTIFICATION
RP   BY MASS SPECTROMETRY, AND ALLERGEN.
RC   TISSUE=Muscle {ECO:0000303|PubMed:23840718, ECO:0000312|EMBL:AGE44125.1};
RX   PubMed=23840718; DOI=10.1371/journal.pone.0067487;
RA   Abramovitch J.B., Kamath S., Varese N., Zubrinich C., Lopata A.L.,
RA   O'Hehir R.E., Rolland J.M.;
RT   "IgE Reactivity of Blue Swimmer Crab (Portunus pelagicus) Tropomyosin, Por
RT   p 1, and Other Allergens; Cross-Reactivity with Black Tiger Prawn and
RT   Effects of Heating.";
RL   PLoS ONE 8:E67487-E67487(2013).
RN   [2]
RP   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).
RN   [3]
RP   TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=23018510;
RA   Rosmilah M., Shahnaz M., Zailatul H.M., Noormalin A., Normilah I.;
RT   "Identification of tropomyosin and arginine kinase as major allergens of
RT   Portunus pelagicus (blue swimming crab).";
RL   Trop. Biomed. 29:467-478(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:23840718, PubMed:23018510). Expressed in pincer muscles
CC       (PubMed:23840718). {ECO:0000269|PubMed:23018510,
CC       ECO:0000269|PubMed:23840718}.
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:23840718,
CC       PubMed:23393908, PubMed:23018510). Recombinant protein binds to IgE in
CC       75% of the 12 shellfish-allergic patients tested. Heating increases
CC       IgE-binding activity. Cross-reacts with giant tiger prawn tropomyosin
CC       allergen Pen m 1.0101 (PubMed:23840718). Cross-reacts with crucifix
CC       crab tropomyosin allergen Cha f 1 (PubMed:23393908).
CC       {ECO:0000269|PubMed:23018510, ECO:0000269|PubMed:23393908,
CC       ECO:0000269|PubMed:23840718}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC       {ECO:0000255|RuleBase:RU004515}.
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DR   EMBL; JX874982; AGE44125.1; -; Genomic_DNA.
DR   SMR; M1H607; -.
DR   Allergome; 10220; Por p 1.
DR   Allergome; 10421; Por p 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;
KW   Muscle protein; Repeat.
FT   CHAIN           1..284
FT                   /note="Tropomyosin Por p 1.0101"
FT                   /id="PRO_0000455647"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..280
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:A1KYZ2"
FT   CONFLICT        79
FT                   /note="S -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  32809 MW;  AE46831B20E6468C CRC64;
     MDAIKKKMQA MKLEKDDAMD RADTLEQQNK EANIRAEKAE EEVHNLQKRM QQLENDLDQV
     QESLLKANTQ LEEKDKALSN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
     DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
     ERAETGESKI VELEEELRVV GNNLKSLEVS EEKANQREEA YKEQIKTLTN KLKAAEARAE
     FAERSVQKLQ KEVDRLEDEL VNEKEKYKST TDELDQAFSE LSGY