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PRVB_GADMO
ID   PRVB_GADMO              Reviewed;         109 AA.
AC   Q90YK9;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Parvalbumin beta;
DE   AltName: Allergen=Gad m 1;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12431393; DOI=10.1016/s0161-5890(02)00200-6;
RA   Van Do T., Hordvik I., Endresen C., Elsayed S.;
RT   "The major allergen (parvalbumin) of codfish is encoded by at least two
RT   isotypic genes: cDNA cloning, expression and antibody binding of the
RT   recombinant allergens.";
RL   Mol. Immunol. 39:595-602(2003).
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions (By
CC       similarity). {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   EMBL; AY035585; AAK63087.1; -; mRNA.
DR   PDB; 2MBX; NMR; -; A=1-109.
DR   PDBsum; 2MBX; -.
DR   AlphaFoldDB; Q90YK9; -.
DR   BMRB; Q90YK9; -.
DR   SMR; Q90YK9; -.
DR   STRING; 8049.ENSGMOP00000004296; -.
DR   Allergome; 358; Gad m 1.
DR   Allergome; 6106; Gad m 1.0201.
DR   PRIDE; Q90YK9; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   3D-structure; Acetylation; Allergen; Calcium; Metal-binding;
KW   Muscle protein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..109
FT                   /note="Parvalbumin beta"
FT                   /id="PRO_0000073609"
FT   DOMAIN          39..74
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          78..109
FT                   /note="EF-hand 2"
FT                   /evidence="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:P02621,
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:P02621,
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:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621,
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:P02621,
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:P02621,
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:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         102
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   HELIX           9..18
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           41..51
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           80..90
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2MBX"
FT   HELIX           100..108
FT                   /evidence="ECO:0007829|PDB:2MBX"
SQ   SEQUENCE   109 AA;  11551 MW;  6AA896E03EF52A74 CRC64;
     MAFAGILNDA DITAALAACK AEGSFDHKAF FTKVGLAAKS PADIKKVFEI IDQDKSDFVE
     EDELKLFLQN FSAGARALSD AETKVFLKAG DSDGDGKIGV DEFGAMIKA
 
 
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