PRVB_SCOJP
ID PRVB_SCOJP Reviewed; 109 AA.
AC P59747; Q3C2C3; Q7ZW61;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Parvalbumin beta {ECO:0000305};
DE AltName: Full=Dark muscle parvalbumin {ECO:0000303|PubMed:16436146, ECO:0000312|EMBL:BAE46764.1};
DE Short=saba-DPA {ECO:0000312|EMBL:BAE46764.1};
DE AltName: Full=White muscle parvalbumin {ECO:0000303|PubMed:16436146};
DE AltName: Allergen=Sco j 1 {ECO:0000303|PubMed:29215073, ECO:0000303|Ref.6};
OS Scomber japonicus (Chub mackerel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Scomber.
OX NCBI_TaxID=13676;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-72 AND 98-108, PTM, AND
RP ALLERGEN.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:12842183};
RX PubMed=12842183; DOI=10.1016/s0278-6915(03)00074-7;
RA Hamada Y., Tanaka H., Ishizaki S., Ishida M., Nagashima Y., Shiomi K.;
RT "Purification, reactivity with IgE and cDNA cloning of parvalbumin as the
RT major allergen of mackerels.";
RL Food Chem. Toxicol. 41:1149-1156(2003).
RN [2] {ECO:0000312|EMBL:BAE46764.1}
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).
RN [3] {ECO:0000312|EMBL:ABJ98932.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hong K., Choi K.;
RT "Genomic DNA Sequence of Parvalbumin in Mackerel and Development of a PCR
RT for Rapid Detection of Allergenic Mackerel Ingredients in Food.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ALLERGEN.
RX DOI=10.1111/j.1440-1592.2004.00344.x;
RA Hamada Y., Tanaka H., Sato A., Ishizaki S., Nagashima Y., Shiomi K.;
RT "Expression and evaluation of IgE-binding capacity of recombinant Pacific
RT mackerel parvalbumin.";
RL Allergol. Int. 53:271-278(2004).
RN [5]
RP ALLERGEN, AND MUTAGENESIS OF ASP-52 AND ASP-91.
RX DOI=10.1111/j.1444-2906.2008.01538.x;
RA Tomura S., Ishizaki S., Nagashima Y., Shiomi K.;
RT "Reduction in the IgE reactivity of Pacific mackerel parvalbumin by
RT mutations at Ca2+-binding sites.";
RL Fish. Sci. 74:411-417(2008).
RN [6]
RP ALLERGEN, REGION, AND MUTAGENESIS OF SER-24; HIS-27; LYS-28; LYS-29;
RP LYS-32; CYS-34; LEU-36 AND LYS-39.
RX DOI=10.1016/j.foodchem.2008.04.062;
RA Yoshida S., Ichimura A., Shiomi K.;
RT "Elucidation of a major IgE epitope of Pacific mackerel parvalbumin.";
RL Food Chem. 111:857-861(2008).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ALLERGEN.
RX PubMed=27041301; DOI=10.1016/j.foodchem.2016.03.043;
RA Kubota H., Kobayashi A., Kobayashi Y., Shiomi K., Hamada-Sato N.;
RT "Reduction in IgE reactivity of Pacific mackerel parvalbumin by heat
RT treatment.";
RL Food Chem. 206:78-84(2016).
RN [8]
RP STRUCTURE BY NMR IN COMPLEX WITH CALCIUM.
RX PubMed=29215073; DOI=10.1038/s41598-017-17281-6;
RA Kumeta H., Nakayama H., Ogura K.;
RT "Solution structure of the major fish allergen parvalbumin Sco j 1 derived
RT from the Pacific mackerel.";
RL Sci. Rep. 7:17160-17160(2017).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. Not degraded by heating at 140 degrees Celsius
CC for 20 min. {ECO:0000269|PubMed:27041301};
CC -!- TISSUE SPECIFICITY: Expressed in both white and dark muscles (at
CC protein level). About eight and a half times lower expression in the
CC dark muscle than in the white muscle (at protein level).
CC {ECO:0000269|PubMed:16436146}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12842183}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12842183,
CC PubMed:16436146, Ref.4, Ref.5, Ref.6, PubMed:27041301). Binds to IgE in
CC patients allergic to fish parvalbumin (PubMed:16436146,
CC PubMed:27041301, Ref.4, Ref.6). Binds to IgE in 80% of 5 fish-allergic
CC patients tested (PubMed:12842183). IgE reactivity linearly decreases
CC with the increase in heating temperature (from 40 to 140 degrees
CC Celsius). More than 50% reduction of allergenicity by heating at 80
CC degrees Celsius and almost complete loss of allergenicity by heating at
CC 140 degrees Celsius (PubMed:27041301). IgE reactivity of 12 fish-
CC allergic patients tested is significantly reduced (60-100% reduction)
CC in the presence of EGTA as a result of Ca(2+) depletion (Ref.5).
CC {ECO:0000269|PubMed:12842183, ECO:0000269|PubMed:16436146,
CC ECO:0000269|PubMed:27041301, ECO:0000269|Ref.4, ECO:0000269|Ref.5,
CC ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; AB091470; BAC66618.1; -; mRNA.
DR EMBL; AB211366; BAE46764.1; -; mRNA.
DR EMBL; EF016113; ABJ98932.1; -; Genomic_DNA.
DR PDB; 5XND; NMR; -; A=1-109.
DR PDBsum; 5XND; -.
DR AlphaFoldDB; P59747; -.
DR SMR; P59747; -.
DR Allergome; 1097; Sco j 1.
DR GO; GO:0005509; F:calcium ion binding; IDA: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 3D-structure; Acetylation; Allergen; Calcium; Direct protein sequencing;
KW Metal-binding; Muscle protein; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09227"
FT CHAIN 2..109
FT /note="Parvalbumin beta"
FT /id="PRO_0000073621"
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 REGION 22..41
FT /note="IgE-binding"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29215073,
FT ECO:0007744|PDB:5XND"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
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 ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:29215073, ECO:0007744|PDB:5XND"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT MUTAGEN 24
FT /note="S->A: More than 50% reduction in IgE reactivity of 4
FT patients sera out of 11 patients sera tested."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 27
FT /note="H->A: More than 50% reduction in IgE reactivity of 7
FT patients sera out of 11 patients sera tested."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 28
FT /note="K->A: Complete loss and more than 50% reduction of
FT IgE reactivity of 3 patients and 9 patients sera out of 11
FT patients sera tested, respectively."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 29
FT /note="K->A: Complete loss and more than 50% reduction of
FT IgE reactivity of 5 patients and 10 patients sera out of 11
FT patients sera tested, respectively."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 32
FT /note="K->A: More than 50% reduction in IgE reactivity of 6
FT patients sera out of 11 patients sera tested."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 34
FT /note="C->A: Complete loss and more than 50% reduction of
FT IgE reactivity of 7 patients and 9 patients sera out of 11
FT patients sera tested, respectively."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 36
FT /note="L->A: More than 50% reduction in IgE reactivity of 7
FT patients sera out of 11 patients sera tested."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 39
FT /note="K->A: Complete loss and more than 50% reduction of
FT IgE reactivity of 5 patients and 10 patients sera out of 11
FT patients sera tested, respectively."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 52
FT /note="D->A: Loss or very weak IgE reactivity of 12
FT patients sera tested; when associated with A-91."
FT /evidence="ECO:0000269|Ref.5"
FT MUTAGEN 91
FT /note="D->A: Loss or very weak IgE reactivity of 12
FT patients sera tested; when associated with A-52."
FT /evidence="ECO:0000269|Ref.5"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:5XND"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:5XND"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5XND"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:5XND"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:5XND"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:5XND"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5XND"
SQ SEQUENCE 109 AA; 11545 MW; 10869A774DFD6899 CRC64;
MAFASVLKDA EVTAALDGCK AAGSFDHKKF FKACGLSGKS TDEVKKAFAI IDQDKSGFIE
EEELKLFLQN FKAGARALSD AETKAFLKAG DSDGDGKIGI DEFAAMIKG
