PRVB_SCOSC
ID PRVB_SCOSC Reviewed; 109 AA.
AC D3GME4; E0WD95;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Parvalbumin beta {ECO:0000312|EMBL:CBA35346.1};
DE AltName: Allergen=Sco s 1 {ECO:0000303|PubMed:28479332};
GN Name=pvalb {ECO:0000312|EMBL:CBA35346.1};
OS Scomber scombrus (Atlantic mackerel) (Scomber vernalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Scomber.
OX NCBI_TaxID=13677 {ECO:0000312|EMBL:CAX32965.1};
RN [1] {ECO:0000312|EMBL:CAX32965.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle {ECO:0000312|EMBL:CAX32965.1};
RA Kuehn A., Hilger C., Hentges F.;
RT "IgE reactivity to different alpha- and beta-parvalbumins in fish allergic
RT patients.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CBA35346.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000312|EMBL:CBA35346.1};
RA Kuehn A., Graf T., Hilger C., Hentges F.;
RT "Rapid fish detection and fish identification in food using parvalbumin-
RT specific PCR.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 21-28; 56-65 AND 98-106, PTM, AND ALLERGEN.
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 [4] {ECO:0000305}
RP ALLERGEN.
RX PubMed=28479332; DOI=10.1016/j.jaci.2017.03.043;
RA Soerensen M., Kuehn A., Mills E.N.C., Costello C.A., Ollert M.,
RA Smaabrekke L., Primicerio R., Wickman M., Klingenberg C.;
RT "Cross-reactivity in Fish Allergy: A Double-Blind Placebo-Controlled Food
RT Challenge Trial.";
RL J. Allergy Clin. Immunol. 140:1170-1172(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:P86431}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12842183}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE
CC (PubMed:12842183, PubMed:28479332). Binds to IgE in 80% of 5 fish-
CC allergic patients tested (PubMed:12842183).
CC {ECO:0000269|PubMed:12842183, ECO:0000269|PubMed:28479332}.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000255}.
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DR EMBL; FM994926; CAX32965.1; -; mRNA.
DR EMBL; FN544077; CBA35346.1; -; Genomic_DNA.
DR AlphaFoldDB; D3GME4; -.
DR SMR; D3GME4; -.
DR Allergome; 1098; Sco s 1.
DR Allergome; 6118; Sco s 1.0101.
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 Acetylation; Allergen; Calcium; Direct protein sequencing; Metal-binding;
KW 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 /evidence="ECO:0000305"
FT /id="PRO_0000441099"
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 ECO:0000255|PROSITE-ProRule:PRU00448"
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|UniProtKB:P02621"
FT CONFLICT 84
FT /note="K -> E (in Ref. 2; CBA35346)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> S (in Ref. 2; CBA35346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 11531 MW; 828C92E3E2C73AFE CRC64;
MAFASVLKDA EITAALDGCK AAGSFDHKKF FKACGLSGKS ADEVKKAFAI IDQDKSGYIE
EEELKLFLQN FKAGARALSD AETKAFLKAG DSDGDGKIGV DEFAAMIKG
