VCL2_JUGRE
ID VCL2_JUGRE Reviewed; 593 AA.
AC Q9SEW4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Vicilin Jug r 2.0101 {ECO:0000305};
DE AltName: Full=7S globulin {ECO:0000303|PubMed:10589017, ECO:0000303|PubMed:22042002, ECO:0000303|PubMed:25388987};
DE AltName: Full=7S seed storage protein {ECO:0000303|PubMed:10589017, ECO:0000303|PubMed:25388987};
DE AltName: Full=Allergen Jug r 2 {ECO:0000303|PubMed:10589017, ECO:0000303|PubMed:21883278, ECO:0000303|PubMed:22042002, ECO:0000303|PubMed:25772597, ECO:0000303|PubMed:30054513};
DE AltName: Full=Vicilin Jug r 2 {ECO:0000303|PubMed:21883278};
DE AltName: Full=Vicilin-like Jug r 2 {ECO:0000303|PubMed:10589017, ECO:0000303|PubMed:25388987, ECO:0000303|PubMed:25772597, ECO:0000303|PubMed:30054513};
DE AltName: Allergen=Jug r 2.0101 {ECO:0000305};
DE Flags: 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:AAF18269.1};
RN [1] {ECO:0000312|EMBL:AAF18269.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 173-185, TISSUE
RP SPECIFICITY, ALLERGEN, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=cv. Sunland {ECO:0000312|EMBL:AAF18269.1};
RC TISSUE=Somatic embryo {ECO:0000303|PubMed:10589017,
RC ECO:0000312|EMBL:AAF18269.1};
RX PubMed=10589017; DOI=10.1016/s0091-6749(99)70029-1;
RA Teuber S.S., Jarvis K.C., Dandekar A.M., Peterson W.R., Ansari A.A.;
RT "Identification and cloning of a complementary DNA encoding a vicilin-like
RT proprotein, jug r 2, from english walnut kernel (Juglans regia), a major
RT food allergen.";
RL J. Allergy Clin. Immunol. 104:1311-1320(1999).
RN [2]
RP PROTEIN SEQUENCE OF 20-26; 52-58; 76-85; 88-96; 89-96; 103-108; 104-108;
RP 117-125; 129-139 AND 130-139, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=cv. Chandler {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 [3]
RP PROTEIN SEQUENCE OF 172-179, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=30054513; DOI=10.1038/s41598-018-29656-4;
RA Dubiela P., Kabasser S., Smargiasso N., Geiselhart S., Bublin M.,
RA Hafner C., Mazzucchelli G., Hoffmann-Sommergruber K.;
RT "Jug r 6 is the allergenic vicilin present in walnut responsible for IgE
RT cross-reactivities to other tree nuts and seeds.";
RL Sci. Rep. 8:11366-11366(2018).
RN [4]
RP TISSUE SPECIFICITY, ALLERGEN, AND REGIONS.
RX PubMed=21883278; DOI=10.1111/j.1398-9995.2011.02692.x;
RA Maleki S.J., Teuber S.S., Cheng H., Chen D., Comstock S.S., Ruan S.,
RA Schein C.H.;
RT "Computationally predicted IgE epitopes of walnut allergens contribute to
RT cross-reactivity with peanuts.";
RL Allergy 66:1522-1529(2011).
RN [5]
RP ALLERGEN, AND REGION.
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 [6]
RP ALLERGEN, AND REGIONS.
RX PubMed=25772597; DOI=10.1016/j.jaci.2015.01.029;
RA Archila L.D., Jeong D., Pascal M., Bartra J., Juan M., Robinson D.,
RA Farrington M.L., Kwok W.W.;
RT "Jug r 2-reactive CD4(+) T cells have a dominant immune role in walnut
RT allergy.";
RL J. Allergy Clin. Immunol. 136:983-992(2015).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305|PubMed:10589017,
CC ECO:0000305|PubMed:21883278, ECO:0000305|PubMed:25388987,
CC ECO:0000305|PubMed:30054513}.
CC -!- TISSUE SPECIFICITY: Expressed in seed (at protein level).
CC {ECO:0000269|PubMed:10589017, ECO:0000269|PubMed:21883278,
CC ECO:0000269|PubMed:25388987, ECO:0000269|PubMed:30054513}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000269|PubMed:10589017}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to walnuts (PubMed:10589017, PubMed:30054513,
CC PubMed:21883278, PubMed:22042002, PubMed:25772597). Binds to IgE of
CC patients allergic to peanuts (PubMed:21883278, PubMed:22042002).
CC Recombinant protein binds to IgE in 60% of the 15 patients tested
CC allergic to walnuts (PubMed:10589017). Natural protein binds to IgE in
CC 67% of the 6 patients tested allergic to peanuts and/or walnuts
CC (PubMed:21883278). Binds to IgE in 53% of the 17 patients tested
CC allergic to walnuts. Provokes CD4(+) T-cell responses. The central
CC memory CD4(+) T-cells are the most prevalent phenotype detected in the
CC peripheral blood of the patients. T-helper 2 (Th2) cells are prominent
CC among the terminal effector T-cells, but T-helper 17 (Th17) and
CC Th2/Th17 cells are also detected (PubMed:25772597).
CC {ECO:0000269|PubMed:10589017, ECO:0000269|PubMed:21883278,
CC ECO:0000269|PubMed:22042002, ECO:0000269|PubMed:25772597,
CC ECO:0000269|PubMed:30054513}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether cleavage occurs at Arg-172 or Glu-173.
CC {ECO:0000305|PubMed:10589017, ECO:0000305|PubMed:30054513}.
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DR EMBL; AF066055; AAF18269.1; -; mRNA.
DR PDB; 7LVE; NMR; -; A=117-161.
DR PDB; 7LVF; NMR; -; A=1-56.
DR PDB; 7LVG; NMR; -; A=69-111.
DR PDBsum; 7LVE; -.
DR PDBsum; 7LVF; -.
DR PDBsum; 7LVG; -.
DR AlphaFoldDB; Q9SEW4; -.
DR SMR; Q9SEW4; -.
DR Allergome; 3335; Jug r 2.0101.
DR Allergome; 425; Jug r 2.
DR PRIDE; Q9SEW4; -.
DR Proteomes; UP000235220; Genome assembly.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR006792; Vicilin_N.
DR Pfam; PF00190; Cupin_1; 2.
DR Pfam; PF04702; Vicilin_N; 1.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Coiled coil; Copper; Direct protein sequencing;
KW Glycoprotein; Metal-binding; Reference proteome; Seed storage protein;
KW Storage protein.
FT CHAIN <1..593
FT /note="Vicilin Jug r 2.0101"
FT /id="PRO_0000450861"
FT DOMAIN 187..341
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 386..556
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 46..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..58
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21883278"
FT REGION 76..85
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21883278"
FT REGION 101..110
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21883278"
FT REGION 140..149
FT /note="IgE-binding. Involved in cross-reactivity with
FT peanut allergen Ara h 2; able to inhibit binding of IgE
FT from a peanut-allergic patient to Ara h 2"
FT /evidence="ECO:0000269|PubMed:21883278"
FT REGION 150..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..193
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 206..225
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 246..265
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 302..321
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 318..337
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 382..401
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 414..433
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 438..457
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 463..470
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:21883278"
FT REGION 478..497
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 541..555
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:22042002"
FT REGION 542..561
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT REGION 558..577
FT /note="T-cell epitope; recognized by the HLA-DRB1-
FT restricted CD4(+) T-cells"
FT /evidence="ECO:0000269|PubMed:25772597"
FT COILED 529..556
FT /evidence="ECO:0000255"
FT COMPBIAS 150..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:B3STU4"
FT BINDING 456
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:B3STU4"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:B3STU4"
FT BINDING 500
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:B3STU4"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAF18269.1"
SQ SEQUENCE 593 AA; 69990 MW; 9BA127E19B18C0D8 CRC64;
RGRDDDDEEN PRDPREQYRQ CQEYCRRQGQ GQRQQQQCQI RCEERLEEDQ RSQEERERRR
GRDVDDQNPR DPEQRYEQCQ QQCERQRRGQ EQTLCRRRCE QRRQQEERER QRGRDRQDPQ
QQYHRCQRRC QIQEQSPERQ RQCQQRCERQ YKEQQGRERG PEASPRRESR GREEEQQRHN
PYYFHSQSIR SRHESEEGEV KYLERFTERT ELLRGIENYR VVILDANPNT SMLPHHKDAE
SVAVVTRGRA TLTLVSQETR ESFNLECGDV IRVPAGATVY VINQDSNERL EMVKLLQPVN
NPGQFREYYA AGAKSPDQSY LRVFSNDILV AALNTPRDRL ERFFDQQEQR EGVIIRASQE
KLRALSQHAM SAGQRPWGRR SSGGPISLKS ESPSYSNQFG QFFEACPEEH RQLQEMDVLV
NYAEIKRGAM MVPHYNSKAT VVVYVVEGTG RYEMACPHVS SQSYEGQGRR EQEEEESTGR
FQKVTARLAR GDIFVIPAGH PIAITASQNE NLRLLGFDIN GENNQRDFLA GQNNIINQLE
REAKELSFNM PREEIEEIFE SQMESYFVPT ERQSRRGQGR DHPLASILDF AFF
