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TPM03_CRAGI
ID   TPM03_CRAGI             Reviewed;         233 AA.
AC   Q95WY0;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Tropomyosin {ECO:0000303|PubMed:11529900, ECO:0000312|EMBL:AAK96889.1};
DE   AltName: Full=Allergen Cra g 1.03 {ECO:0000303|PubMed:11529900};
DE   AltName: Allergen=Cra g 1 {ECO:0000305};
DE   Flags: Fragment;
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000312|EMBL:AAK96889.1};
RN   [1] {ECO:0000312|EMBL:AAK96889.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=11529900; DOI=10.1046/j.1365-2222.2001.01165.x;
RA   Leung P.S., Chu K.H.;
RT   "cDNA cloning and molecular identification of the major oyster allergen
RT   from the Pacific oyster Crassostrea gigas.";
RL   Clin. Exp. Allergy 31:1287-1294(2001).
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 in 80% of
CC       the 15 patients tested allergic to oysters.
CC       {ECO:0000269|PubMed:11529900}.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC       {ECO:0000255|RuleBase:RU004515, ECO:0000305}.
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DR   EMBL; AF239173; AAK96889.1; -; mRNA.
DR   AlphaFoldDB; Q95WY0; -.
DR   SMR; Q95WY0; -.
DR   Allergome; 247; Cra g 1.
DR   Proteomes; UP000005408; Unassembled WGS sequence.
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; Reference proteome; Repeat.
FT   CHAIN           <1..233
FT                   /note="Tropomyosin"
FT                   /id="PRO_0000447282"
FT   REGION          48..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          6..222
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAK96889.1"
SQ   SEQUENCE   233 AA;  26867 MW;  8F741877ACD4A137 CRC64;
     NSARGFDTVN EKYQECQTKM EEAEKTASEA EQEIQSLNRR IQLLEEDMER SEERLQTATE
     KLEEASKAAD ESERNRKVLE NLNNASEERT DVLEKQLTEA KLIAEEADKK YDEAARKLAI
     TEVDLERAEA RLEAAEAKVL ELEEELKVVG NNMKSLEISE QEASQREDSY EETIRDLTQR
     LKDAENRATE AERTVSKLQK EVDRLEDELL AEKERYKAIS DELDQTFAEL AGY
 
 
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