TPM_PENAT
ID TPM_PENAT Reviewed; 284 AA.
AC Q3Y8M6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Tropomyosin Pen a 1.0102 {ECO:0000305};
DE AltName: Full=Allergen Pen a 1 {ECO:0000303|PubMed:11893851, ECO:0000303|PubMed:16339577, ECO:0000303|PubMed:16630158};
DE AltName: Full=Tropomyosin Pen a 1 {ECO:0000303|PubMed:11893851, ECO:0000303|PubMed:16339577};
DE AltName: Allergen=Pen a 1.0102 {ECO:0000305};
OS Penaeus aztecus (Brown shrimp) (Farfantepenaeus aztecus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6690 {ECO:0000312|EMBL:AAZ76743.1};
RN [1] {ECO:0000312|EMBL:AAZ76743.1}
RP NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN, MISCELLANEOUS, REGIONS, MUTAGENESIS
RP OF LEU-46; LEU-53; LEU-95; SER-136; GLU-145; VAL-191; VAL-199; ARG-255;
RP LEU-260; SER-269; THR-277 AND PHE-278, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Tail muscle {ECO:0000312|EMBL:AAZ76743.1};
RX PubMed=16339577; DOI=10.4049/jimmunol.175.12.8354;
RA Reese G., Viebranz J., Leong-Kee S.M., Plante M., Lauer I., Randow S.,
RA Moncin M.S., Ayuso R., Lehrer S.B., Vieths S.;
RT "Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen
RT Pen a 1 (tropomyosin).";
RL J. Immunol. 175:8354-8364(2005).
RN [2] {ECO:0000312|EMBL:AAZ76743.1}
RP NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Tail muscle {ECO:0000312|EMBL:AAZ76743.1};
RX PubMed=16630158; DOI=10.1111/j.1365-2222.2006.02454.x;
RA Reese G., Schicktanz S., Lauer I., Randow S., Luettkopf D., Vogel L.,
RA Lehrer S.B., Vieths S.;
RT "Structural, immunological and functional properties of natural recombinant
RT Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus.";
RL Clin. Exp. Allergy 36:517-524(2006).
RN [3]
RP ALLERGEN, AND REGIONS.
RX PubMed=11893851; DOI=10.1159/000048166;
RA Ayuso R., Lehrer S.B., Reese G.;
RT "Identification of continuous, allergenic regions of the major shrimp
RT allergen Pen a 1 (tropomyosin).";
RL Int. Arch. Allergy Immunol. 127:27-37(2002).
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 of atopic
CC shrimp-allergic patients (PubMed:16339577, PubMed:16630158,
CC PubMed:11893851). Binds to IgE in 100% of the 18 patients tested
CC (PubMed:11893851). Causes release of beta-hexosaminidase from wild-type
CC and humanized rat basophil leukemia (RBL) cells (PubMed:16339577,
CC PubMed:16630158). {ECO:0000269|PubMed:11893851,
CC ECO:0000269|PubMed:16339577, ECO:0000269|PubMed:16630158}.
CC -!- MISCELLANEOUS: Constructed epitope mutant has significantly reduced
CC allergenic potency, and hence could represent a candidate vaccine for
CC treatment of shrimp food allergy. {ECO:0000269|PubMed:16339577}.
CC -!- SIMILARITY: Belongs to the tropomyosin family.
CC {ECO:0000255|RuleBase:RU004515, ECO:0000305}.
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DR EMBL; DQ151457; AAZ76743.1; -; mRNA.
DR AlphaFoldDB; Q3Y8M6; -.
DR SMR; Q3Y8M6; -.
DR Allergome; 3929; Pen a 1.0102.
DR Allergome; 515; Pen a 1.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
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; IgE-binding protein; Muscle protein; Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin Pen a 1.0102"
FT /id="PRO_0000447228"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..57
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11893851,
FT ECO:0000269|PubMed:16339577"
FT REGION 85..105
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11893851,
FT ECO:0000269|PubMed:16339577"
FT REGION 133..153
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11893851,
FT ECO:0000269|PubMed:16339577"
FT REGION 187..202
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11893851,
FT ECO:0000269|PubMed:16339577"
FT REGION 247..284
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11893851"
FT REGION 249..260
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:16339577"
FT REGION 266..281
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:16339577"
FT COILED 1..273
FT /evidence="ECO:0000255"
FT MUTAGEN 46
FT /note="L->M: Nearly complete loss of allergenicity; when
FT associated with T-53, V-95, L-136, D-145, S-191, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 53
FT /note="L->T: Nearly complete loss of allergenicity; when
FT associated with M-46, V-95, L-136, D-145, S-191, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 95
FT /note="L->V: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, L-136, D-145, S-191, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 136
FT /note="S->L: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, D-145, S-191, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 145
FT /note="E->D: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, S-191, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 191
FT /note="V->S: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, N-199, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 199
FT /note="V->N: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, D-
FT 255, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 255
FT /note="R->D: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, N-
FT 199, V-260, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 260
FT /note="L->V: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, N-
FT 199, D-255, F-269, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 269
FT /note="S->F: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, N-
FT 199, D-255, V-260, A-277 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 277
FT /note="T->A: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, N-
FT 199, D-255, V-260, F-269 and L-278."
FT /evidence="ECO:0000269|PubMed:16339577"
FT MUTAGEN 278
FT /note="F->L: Nearly complete loss of allergenicity; when
FT associated with M-46, T-53, V-95, L-136, D-145, S-191, N-
FT 199, D-255, V-260, F-269 and A-277."
FT /evidence="ECO:0000269|PubMed:16339577"
SQ SEQUENCE 284 AA; 32849 MW; BE53B602C37E85E2 CRC64;
MDAIKKKMQA MKLEKDNAMD RADTLEQQNK EANNRAEKSE EEVHNLQKRM QQLENDLDQV
QESLLKANIQ LVEKDKALSN AEGEVAALNR RIQLLEEDLE RSEERLNTAT TKLAEASQAA
DESERMRKVL ENRSLSDEER MDALENQLKE ARFLAEEADR KYDEVARKLA MVEADLERAE
ERAETGESKI VELEEELRVV GNNLKSLEVS EEKANQREEA YKEQIKTLTN KLKAAEARAE
FAERSVQKLQ KEVDRLEDEL VNEKEKYKSI TDELDQTFSE LSGY
