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   27-MAR-2024, entry version 82.
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   CDD; cd16255; EFh_parvalbumin_beta; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
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:SF12; PARVALBUMIN; 1.
DR   PANTHER; PTHR11653; PARVALBUMIN ALPHA; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR01697; PARVALBUMIN.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 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
//