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PRVB_TRAJP
ID   PRVB_TRAJP              Reviewed;         107 AA.
AC   Q3C2C4;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Parvalbumin beta {ECO:0000305};
DE   AltName: Full=Dark muscle parvalbumin {ECO:0000303|PubMed:16436146, ECO:0000312|EMBL:BAE46763.1};
DE            Short=aji-DPA {ECO:0000312|EMBL:BAE46763.1};
DE   AltName: Full=White muscle parvalbumin {ECO:0000303|PubMed:16436146, ECO:0000312|EMBL:BAE46762.1};
DE            Short=aji-WPA {ECO:0000312|EMBL:BAE46762.1};
DE   AltName: Allergen=Tra j 1 {ECO:0000305};
OS   Trachurus japonicus (Japanese jack mackerel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Trachurus.
OX   NCBI_TaxID=83875 {ECO:0000312|EMBL:BAE46763.1};
RN   [1] {ECO:0000312|EMBL:BAE46763.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Muscle {ECO:0000303|PubMed:16436146};
RX   PubMed=16436146; DOI=10.1111/j.1398-9995.2006.00966.x;
RA   Kobayashi A., Tanaka H., Hamada Y., Ishizaki S., Nagashima Y., Shiomi K.;
RT   "Comparison of allergenicity and allergens between fish white and dark
RT   muscles.";
RL   Allergy 61:357-363(2006).
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions.
CC       {ECO:0000250|UniProtKB:P86432}.
CC   -!- TISSUE SPECIFICITY: Expressed in both white and dark muscles (at
CC       protein level). About five times lower expression in the dark muscle
CC       than in the white muscle (at protein level).
CC       {ECO:0000269|PubMed:16436146}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in
CC       patients allergic to fish parvalbumin. {ECO:0000269|PubMed:16436146}.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000255,
CC       ECO:0000305}.
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DR   EMBL; AB211364; BAE46762.1; -; mRNA.
DR   EMBL; AB211365; BAE46763.1; -; mRNA.
DR   AlphaFoldDB; Q3C2C4; -.
DR   SMR; Q3C2C4; -.
DR   Allergome; 2713; Tra j 1.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR008080; Parvalbumin.
DR   PANTHER; PTHR11653; PTHR11653; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Metal-binding; Muscle protein; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09227"
FT   CHAIN           2..107
FT                   /note="Parvalbumin beta"
FT                   /id="PRO_0000447296"
FT   DOMAIN          37..72
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          76..107
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P59747"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         89
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P59747,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   107 AA;  11340 MW;  8BCFCF7BAC76472B CRC64;
     MAFKGVLNDA DVTAALDGCK SAFDHKAFFK ACGLAAKSAD DIKKAFAIID QDKSGFIEED
     ELKLFLQNFC AGARALSDAE TKAFLKAGDS DGDGKIGVDE FAAMVKH
 
 
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