2SS_JUGRE
ID 2SS_JUGRE Reviewed; 139 AA.
AC P93198;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=2S seed storage albumin protein;
DE AltName: Full=2S albumin {ECO:0000303|PubMed:11799381, ECO:0000303|PubMed:19540419, ECO:0000303|PubMed:24206692, ECO:0000303|PubMed:25388987};
DE AltName: Full=2S albumin seed storage protein {ECO:0000303|PubMed:11799381, ECO:0000303|PubMed:9648708};
DE AltName: Full=Allergen Jug r 1 {ECO:0000303|PubMed:11799381, ECO:0000303|PubMed:19540419, ECO:0000303|PubMed:27597723, ECO:0000303|PubMed:28552380, ECO:0000303|PubMed:31175720, ECO:0000303|PubMed:32283362, ECO:0000303|PubMed:9648708};
DE AltName: Allergen=Jug r 1.0101 {ECO:0000305};
DE Contains:
DE RecName: Full=2S albumin seed storage protein small subunit {ECO:0000303|PubMed:11799381, ECO:0000303|PubMed:9648708};
DE Contains:
DE RecName: Full=2S albumin seed storage protein large subunit {ECO:0000303|PubMed:11799381, ECO:0000303|PubMed:9648708};
DE Flags: Precursor; Fragment;
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000312|EMBL:AAB41308.1};
RN [1] {ECO:0000312|EMBL:AAB41308.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND ALLERGEN.
RC STRAIN=cv. Sunland {ECO:0000303|PubMed:9648708,
RC ECO:0000312|EMBL:AAB41308.1};
RC TISSUE=Somatic embryo {ECO:0000303|PubMed:9648708};
RX PubMed=9648708; DOI=10.1016/s0091-6749(98)70308-2;
RA Teuber S.S., Dandekar A.M., Peterson W.R., Sellers C.L.;
RT "Cloning and sequencing of a gene encoding a 2S albumin seed storage
RT protein precursor from English walnut (Juglans regia), a major food
RT allergen.";
RL J. Allergy Clin. Immunol. 101:807-814(1998).
RN [2]
RP PROTEIN SEQUENCE OF 19-33; 22-33; 23-33; 24-33; 25-33; 26-33; 27-33; 28-33;
RP 40-45; 54-65; 56-74; 57-74; 59-74; 65-74; 96-106 AND 117-137, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, ALLERGEN, BIOTECHNOLOGY,
RP REGIONS, AND 3D-STRUCTURE MODELING.
RC TISSUE=Seed {ECO:0000269|PubMed:32283362};
RX PubMed=32283362; DOI=10.1016/j.foodchem.2020.126711;
RA Guo X., Jiang S., Li X., Yang S., Cheng L., Qiu J., Che H.;
RT "Sequence analysis of digestion-resistant peptides may be an efficient
RT strategy for studying the linear epitopes of Jug r 1, the major walnut
RT allergen.";
RL Food Chem. 322:126711-126711(2020).
RN [3]
RP PROTEIN SEQUENCE OF 35-40; 36-45; 41-45; 46-57; 62-71; 76-94; 99-107;
RP 100-119; 108-119 AND 120-131, SUBUNIT, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RC STRAIN=cv. Chandler {ECO:0000303|PubMed:25388987};
RC TISSUE=Seed {ECO:0000303|PubMed:25388987};
RX PubMed=25388987; DOI=10.1021/jf504672m;
RA Downs M.L., Semic-Jusufagic A., Simpson A., Bartra J., Fernandez-Rivas M.,
RA Rigby N.M., Taylor S.L., Baumert J.L., Mills E.N.;
RT "Characterization of low molecular weight allergens from English walnut
RT (Juglans regia).";
RL J. Agric. Food Chem. 62:11767-11775(2014).
RN [4]
RP ALLERGEN, REGIONS, SITE, AND MUTAGENESIS OF GLN-104; GLY-105; LEU-106;
RP ARG-107; GLY-108; GLU-109; GLU-110; MET-111; GLU-112; GLU-113; MET-114 AND
RP VAL-115.
RX PubMed=11799381; DOI=10.1067/mai.2002.120558;
RA Robotham J.M., Teuber S.S., Sathe S.K., Roux K.H.;
RT "Linear IgE epitope mapping of the English walnut (Juglans regia) major
RT food allergen, Jug r 1.";
RL J. Allergy Clin. Immunol. 109:143-149(2002).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY, ALLERGEN,
RP BIOTECHNOLOGY, REGIONS, 3D-STRUCTURE MODELING, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=19540419; DOI=10.1016/j.peptides.2009.03.007;
RA Sordet C., Culerrier R., Granier C., Rance F., Didier A., Barre A.,
RA Rouge P.;
RT "Expression of Jug r 1, the 2S albumin allergen from walnut (Juglans
RT regia), as a correctly folded and functional recombinant protein.";
RL Peptides 30:1213-1221(2009).
RN [6]
RP ALLERGEN, AND REGIONS.
RX PubMed=22042002; DOI=10.1159/000327841;
RA Rosenfeld L., Shreffler W., Bardina L., Niggemann B., Wahn U.,
RA Sampson H.A., Beyer K.;
RT "Walnut allergy in peanut-allergic patients: significance of sequential
RT epitopes of walnut homologous to linear epitopes of Ara h 1, 2 and 3 in
RT relation to clinical reactivity.";
RL Int. Arch. Allergy Immunol. 157:238-245(2012).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=24206692; DOI=10.1016/j.foodchem.2013.09.013;
RA Wang H., Li G., Wu Y., Yuan F., Chen Y.;
RT "Development of an indirect competitive immunoassay for walnut protein
RT component in food.";
RL Food Chem. 147:106-110(2014).
RN [8]
RP ALLERGEN.
RX PubMed=27597723; DOI=10.1016/j.jaci.2016.07.026;
RA Blankestijn M.A., Blom W.M., Otten H.G., Baumert J.L., Taylor S.L.,
RA Bruijnzeel-Koomen C.A., Houben G.F., Knulst A.C., Klemans R.J.;
RT "Specific IgE to Jug r 1 has no additional value compared with extract-
RT based testing in diagnosing walnut allergy in adults.";
RL J. Allergy Clin. Immunol. 139:688-690(2017).
RN [9]
RP ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=28552380; DOI=10.1016/j.jaip.2017.04.025;
RA Sato S., Yamamoto M., Yanagida N., Ito K., Ohya Y., Imai T., Nagao M.,
RA Borres M.P., Moverare R., Ebisawa M.;
RT "Jug r 1 sensitization is important in walnut-allergic children and
RT youth.";
RL J. Allergy Clin. Immunol. Pract. 5:1784-1786(2017).
RN [10]
RP ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=31175720; DOI=10.12932/ap-161118-0443;
RA Lee J., Jeong K., Jeon S.A., Lee S.;
RT "Component resolved diagnosis of walnut allergy in young children: Jug r 1
RT as a major walnut allergen.";
RL Asian Pac. J. Allergy Immunol. 39:190-196(2021).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:19540419,
CC ECO:0000305|PubMed:25388987, ECO:0000305|PubMed:32283362}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Resistant to heat. Retains its alpha-helical fold after heating at 90
CC degrees Celsius and subsequent cooling to 20 degrees Celsius.
CC {ECO:0000269|PubMed:19540419};
CC -!- SUBUNIT: The mature protein consists of a small chain and a large chain
CC linked by disulfide bonds. {ECO:0000269|PubMed:19540419,
CC ECO:0000269|PubMed:25388987, ECO:0000269|PubMed:9648708}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level)
CC (PubMed:25388987, PubMed:19540419, PubMed:32283362). Expressed in the
CC peel of mature seed (PubMed:19540419). {ECO:0000269|PubMed:19540419,
CC ECO:0000269|PubMed:25388987, ECO:0000269|PubMed:32283362}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation.
CC {ECO:0000269|PubMed:19540419}.
CC -!- MASS SPECTROMETRY: Mass=12617.2; Method=MALDI; Note=The measured mass
CC is that of an intact non-reduced protein.;
CC Evidence={ECO:0000269|PubMed:25388987};
CC -!- MASS SPECTROMETRY: [2S albumin seed storage protein small subunit]:
CC Mass=4640.1; Method=MALDI; Evidence={ECO:0000269|PubMed:25388987};
CC -!- MASS SPECTROMETRY: [2S albumin seed storage protein large subunit]:
CC Mass=8440.72; Method=MALDI; Evidence={ECO:0000269|PubMed:25388987};
CC -!- MASS SPECTROMETRY: [2S albumin seed storage protein small subunit]:
CC Mass=3437; Method=MALDI; Evidence={ECO:0000269|PubMed:19540419};
CC -!- MASS SPECTROMETRY: [2S albumin seed storage protein large subunit]:
CC Mass=8009; Method=MALDI; Evidence={ECO:0000269|PubMed:19540419};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to walnuts (PubMed:9648708, PubMed:25388987,
CC PubMed:11799381, PubMed:19540419, PubMed:22042002, PubMed:27597723,
CC PubMed:28552380, PubMed:31175720, PubMed:32283362). Binds to IgE of
CC patients allergic to peanuts (PubMed:22042002). Binds to IgE in 97% of
CC the 32 Korean babies and children tested allergic to walnuts
CC (PubMed:31175720). Native protein binds to IgE in 100% of the 6 Chinese
CC walnut-allergic patients tested (PubMed:32283362). Native protein binds
CC to IgE in 45% of the 11 walnut-allergic patients tested living in Spain
CC or England (PubMed:25388987). Recombinant protein binds to IgE in 75%
CC of the 16 walnut-allergic patients tested (PubMed:9648708). Recombinant
CC protein binds to IgE in 100% of the 20 walnut-allergic patients tested
CC (PubMed:11799381). Recombinant protein binds to IgE in 55% and 61% of
CC the 33 walnut-allergic adult patients living in Netherlands tested by
CC ImmunoCAP and ImmunoCAP ISAC, respectively (PubMed:27597723). Contains
CC linear and conformational IgE-binding epitopes (PubMed:11799381).
CC Cross-reacts with sesame seed allergens Ses i 1 and Ses i 2. IgE-
CC binding is lost in the presence of pepsin after 1 hour incubation at pH
CC 1.5 and 37 degrees Celsius in vitro, but it is not affected in the
CC presence of trypsin and chymotrypsin after 2 hour incubation in vitro
CC at pH 8 and 37 degrees Celsius. Induces in vitro degranulation of the
CC humanized rat basophilic leukemia (RBL) cells and release of beta-
CC hexosaminidase from them (PubMed:19540419).
CC {ECO:0000269|PubMed:11799381, ECO:0000269|PubMed:19540419,
CC ECO:0000269|PubMed:22042002, ECO:0000269|PubMed:25388987,
CC ECO:0000269|PubMed:27597723, ECO:0000269|PubMed:28552380,
CC ECO:0000269|PubMed:31175720, ECO:0000269|PubMed:32283362,
CC ECO:0000269|PubMed:9648708}.
CC -!- BIOTECHNOLOGY: The recombinant protein could be used for a reliable
CC component-resolved diagnosis of walnut allergy as it has the same
CC properties and virtually identical IgE-binding reactivity as the native
CC protein even that it is unprocessed and hence lacking the proteolytic
CC cleavages of the mature protein (PubMed:19540419). A rapid, highly
CC specific and relatively sensitive indirect competitive enzyme-linked
CC immunosorbent assay (ELISA) for detection and quantification of walnut
CC protein component in processed foods has been developed using
CC polyclonal antibodies against this protein (PubMed:24206692). Testing
CC young patients specific IgE-reactivity of this protein is a better
CC approach in diagnosing clinical walnut allergy in children and youth
CC compared to the walnut extract-based testing due to its improved
CC specificity as shown by the receiver operating characteristic (ROC)
CC statistical analysis (PubMed:28552380, PubMed:31175720). The strategy
CC of synthesizing digestion-resistant peptides instead of overlapping
CC peptides, and verifying them using sera from walnut-allergic patients,
CC can significantly reduce workload and serum requirement, enhance
CC pertinence, and improve efficiency in studying linear epitopes of this
CC protein (PubMed:32283362). {ECO:0000269|PubMed:19540419,
CC ECO:0000269|PubMed:24206692, ECO:0000269|PubMed:28552380,
CC ECO:0000269|PubMed:31175720, ECO:0000269|PubMed:32283362}.
CC -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC {ECO:0000305}.
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DR EMBL; U66866; AAB41308.1; -; mRNA.
DR AlphaFoldDB; P93198; -.
DR SMR; P93198; -.
DR Allergome; 3334; Jug r 1.0101.
DR Allergome; 424; Jug r 1.
DR PRIDE; P93198; -.
DR EnsemblPlants; Jr09_14980_p1; cds.Jr09_14980_p1; Jr09_14980.
DR Gramene; Jr09_14980_p1; cds.Jr09_14980_p1; Jr09_14980.
DR Proteomes; UP000235220; Genome assembly.
DR GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IC:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
DR CDD; cd00261; AAI_SS; 1.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR044723; AAI_SS_dom.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000617; Napin/2SS/CON.
DR PANTHER; PTHR35496; PTHR35496; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00496; NAPIN.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Reference proteome;
KW Seed storage protein; Signal; Storage protein.
FT SIGNAL <1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..31
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11799381"
FT /id="PRO_0000451111"
FT CHAIN 32..57
FT /note="2S albumin seed storage protein small subunit"
FT /evidence="ECO:0000305|PubMed:11799381"
FT /id="PRO_0000451112"
FT PROPEP 58..71
FT /evidence="ECO:0000305|PubMed:11799381"
FT /id="PRO_0000451113"
FT CHAIN 72..135
FT /note="2S albumin seed storage protein large subunit"
FT /evidence="ECO:0000305|PubMed:11799381"
FT /id="PRO_0000451114"
FT PROPEP 136..139
FT /evidence="ECO:0000305|PubMed:11799381"
FT /id="PRO_0000451115"
FT REGION 16..30
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:32283362"
FT REGION 29..34
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:19540419"
FT REGION 64..78
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:22042002"
FT REGION 65..73
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:19540419"
FT REGION 95..103
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:19540419"
FT REGION 99..111
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11799381"
FT REGION 102..114
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11799381"
FT REGION 104..115
FT /note="Immunodominant epitope. IgE-binding; binds to IgE in
FT 75% of the 20 walnut-allergic patients tested"
FT /evidence="ECO:0000269|PubMed:11799381"
FT REGION 105..117
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11799381"
FT REGION 107..110
FT /note="Minimally required for IgE-binding by the
FT immunodominant epitope"
FT /evidence="ECO:0000269|PubMed:11799381"
FT REGION 112..126
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:22042002"
FT REGION 125..139
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:32283362"
FT REGION 125..136
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:19540419"
FT SITE 113
FT /note="Necessary for maximum IgE-binding by the
FT immunodominant epitope"
FT /evidence="ECO:0000269|PubMed:11799381"
FT DISULFID 39..88
FT /note="Interchain (between small and large chains)"
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 52..77
FT /note="Interchain (between small and large chains)"
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 78..125
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT DISULFID 90..132
FT /evidence="ECO:0000250|UniProtKB:P04403"
FT MUTAGEN 104
FT /note="Q->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 105
FT /note="G->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 106
FT /note="L->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 107
FT /note="R->A: Loss of IgE-binding by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 108
FT /note="G->A: Loss of IgE-binding by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 109
FT /note="E->A: Loss of IgE-binding by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 110
FT /note="E->A: Loss of IgE-binding by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 111
FT /note="M->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 112
FT /note="E->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 113
FT /note="E->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 114
FT /note="M->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT MUTAGEN 115
FT /note="V->A: IgE-binding is retained by the immunodominant
FT epitope."
FT /evidence="ECO:0000269|PubMed:11799381"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAB41308.1"
SQ SEQUENCE 139 AA; 16373 MW; 02D0E55E67164F23 CRC64;
AALLVALLFV ANAAAFRTTI TTMEIDEDID NPRRRGEGCR EQIQRQQNLN HCQYYLRQQS
RSGGYDEDNQ RQHFRQCCQQ LSQMDEQCQC EGLRQVVRRQ QQQQGLRGEE MEEMVQSARD
LPNECGISSQ RCEIRRSWF
