PRVB_GADMC
ID PRVB_GADMC Reviewed; 113 AA.
AC P02622;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Parvalbumin beta;
DE AltName: Full=Allergen Gad c I {ECO:0000303|PubMed:9449503};
DE AltName: Full=Allergen M;
DE AltName: Allergen=Gad c 1.0101 {ECO:0000305};
OS Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8053;
RN [1]
RP PROTEIN SEQUENCE OF 1-75, AND ACETYLATION AT ALA-1.
RX PubMed=1145128; DOI=10.1111/j.1365-3083.1975.tb02618.x;
RA Elsayed S., Bennich H.;
RT "The primary structure of allergen M from cod.";
RL Scand. J. Immunol. 4:203-208(1975).
RN [2]
RP PROTEIN SEQUENCE OF 76-113.
RX PubMed=4423465; DOI=10.1111/j.1365-3083.1974.tb01303.x;
RA Elsayed S., von Bahr-Lindstroem H., Bennich H.;
RT "The primary structure of fragment TM2 of allergen M from cod.";
RL Scand. J. Immunol. 3:683-686(1974).
RN [3]
RP CALCIUM-BINDING.
RX PubMed=3440123; DOI=10.1016/0301-4622(87)80093-5;
RA Permyakov E.A., Ostrovsky A.V., Kalinichenko L.P.;
RT "Stopped-flow kinetic studies of Ca(II) and Mg(II) dissociation in cod
RT parvalbumin and bovine alpha-lactalbumin.";
RL Biophys. Chem. 28:225-233(1987).
RN [4]
RP TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=9449503; DOI=10.1016/s0091-6749(98)70195-2;
RA Bugajska-Schretter A., Elfman L., Fuchs T., Kapiotis S., Rumpold H.,
RA Valenta R., Spitzauer S.;
RT "Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes
RT sensitive to periodate treatment and Ca2+ depletion.";
RL J. Allergy Clin. Immunol. 101:67-74(1998).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- TISSUE SPECIFICITY: Muscle (at protein level).
CC {ECO:0000269|PubMed:9449503}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in all 28
CC patients tested allergic to fish. IgE-binding is greatly reduced by
CC treatment with periodate indicating the presence of carbohydrate-
CC containing epitopes. Calcium depletion results in more than 50%
CC reduction in IgE-binding in 9 patients out of 14 tested. Assays
CC performed under reducing conditions do not affect IgE-binding.
CC {ECO:0000269|PubMed:9449503}.
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.40.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A94236; PVCD.
DR AlphaFoldDB; P02622; -.
DR SMR; P02622; -.
DR Allergome; 3290; Gad c 1.0101.
DR Allergome; 357; Gad c 1.
DR iPTMnet; P02622; -.
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 Acetylation; Allergen; Calcium; Direct protein sequencing; Glycoprotein;
KW Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..113
FT /note="Parvalbumin beta"
FT /id="PRO_0000073608"
FT DOMAIN 38..73
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 77..112
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 51
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 53
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 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 62
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 90
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 92
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 94
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 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
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 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1145128"
FT CARBOHYD 18
FT /note="S-linked (Glc) cysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 113 AA; 12108 MW; 4CD4E3DC5CCAE94F CRC64;
AFKGILSNAD IKAAEAACFK EGSFDEDGFY AKVGLDAFSA DELKKLFKIA DEDKEGFIEE
DELKLFLIAF AADLRALTDA ETKAFLKAGD SDGDGKIGVD EFGALVDKWG AKG
