ID   JUGR4_JUGRE             Reviewed;         507 AA.
AC   Q2TPW5;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=11S globulin seed storage protein Jug r 4 {ECO:0000305};
DE   AltName: Allergen=Jug r 4 {ECO:0000303|PubMed:17032053, ECO:0000303|PubMed:29904971};
DE   Contains:
DE     RecName: Full=11S globulin seed storage protein Jug r 4 acidic chain {ECO:0000305};
DE   Contains:
DE     RecName: Full=11S globulin seed storage protein Jug r 4 basic chain {ECO:0000305};
DE   Flags: Precursor;
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;
RN   [1] {ECO:0000312|EMBL:AAW29810.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PTM,
RP   ALLERGEN, AND MOTIF.
RC   STRAIN=cv. Chandler {ECO:0000303|PubMed:17032053};
RC   TISSUE=Embryo {ECO:0000303|PubMed:17032053};
RX   PubMed=17032053; DOI=10.1021/jf061329s;
RA   Wallowitz M., Peterson W.R., Uratsu S., Comstock S.S., Dandekar A.M.,
RA   Teuber S.S.;
RT   "Jug r 4, a legumin group food allergen from walnut (Juglans regia Cv.
RT   Chandler).";
RL   J. Agric. Food Chem. 54:8369-8375(2006).
RN   [2] {ECO:0000312|Proteomes:UP000235220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chandler {ECO:0000312|Proteomes:UP000235220};
RX   PubMed=27145194; DOI=10.1111/tpj.13207;
RA   Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA   Stevens K.A., Paul R., Butterfield T.S., Britton M.T., Reagan R.L.,
RA   Chakraborty S., Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R.A.,
RA   Pratt K., Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M.,
RA   Salzberg S.L., Wegrzyn J.L., Langley C.H., Neale D.B.;
RT   "The walnut (Juglans regia) genome sequence reveals diversity in genes
RT   coding for the biosynthesis of non-structural polyphenols.";
RL   Plant J. 87:507-532(2016).
RN   [3]
RP   ALLERGEN, AND REGIONS.
RX   PubMed=19631385; DOI=10.1016/j.molimm.2009.06.020;
RA   Robotham J.M., Hoffman G.G., Teuber S.S., Beyer K., Sampson H.A.,
RA   Sathe S.K., Roux K.H.;
RT   "Linear IgE-epitope mapping and comparative structural homology modeling of
RT   hazelnut and English walnut 11S globulins.";
RL   Mol. Immunol. 46:2975-2984(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND ALLERGEN.
RX   PubMed=29904971; DOI=10.1111/cea.13208;
RA   Blankestijn M.A., den Hartog Jager C.F., Blom W.M., Otten H.G.,
RA   de Jong G.A.H., Gaspari M., Houben G.F., Knulst A.C., Verhoeckx K.C.M.;
RT   "A subset of walnut allergic adults is sensitized to walnut 11S globulin
RT   Jug r 4.";
RL   Clin. Exp. Allergy 48:1206-1213(2018).
CC   -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC       ECO:0000305|PubMed:17032053, ECO:0000305|PubMed:29904971}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds. {ECO:0000269|PubMed:17032053,
CC       ECO:0000269|PubMed:29904971}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during seed development.
CC       {ECO:0000269|PubMed:17032053, ECO:0000269|PubMed:29904971}.
CC   -!- PTM: Proteolytically processed from a single precursor to produce an
CC       acidic and a basic chain that are linked by a disulfide bond.
CC       {ECO:0000269|PubMed:17032053}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:17032053, ECO:0000269|PubMed:19631385,
CC       ECO:0000269|PubMed:29904971}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR   EMBL; AY692446; AAW29810.1; -; mRNA.
DR   RefSeq; XP_018827329.1; XM_018971784.1.
DR   AlphaFoldDB; Q2TPW5; -.
DR   SMR; Q2TPW5; -.
DR   STRING; 51240.Q2TPW5; -.
DR   Allergome; 1105; Jug r 4.
DR   Allergome; 3574; Jug r 4.0101.
DR   PRIDE; Q2TPW5; -.
DR   EnsemblPlants; Jr01_32050_p1; cds.Jr01_32050_p1; Jr01_32050.
DR   GeneID; 108996042; -.
DR   Gramene; Jr01_32050_p1; cds.Jr01_32050_p1; Jr01_32050.
DR   KEGG; jre:108996042; -.
DR   OrthoDB; 603461at2759; -.
DR   Proteomes; UP000235220; Chromosome 1.
DR   GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0048316; P:seed development; IEP:UniProtKB.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; IgE-binding protein; Reference proteome;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|RuleBase:RU003681"
FT   CHAIN           24..315
FT                   /note="11S globulin seed storage protein Jug r 4 acidic
FT                   chain"
FT                   /evidence="ECO:0000305|PubMed:17032053"
FT                   /id="PRO_0000446017"
FT   CHAIN           316..507
FT                   /note="11S globulin seed storage protein Jug r 4 basic
FT                   chain"
FT                   /evidence="ECO:0000305|PubMed:17032053"
FT                   /id="PRO_0000446018"
FT   DOMAIN          41..254
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          328..477
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..15
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          57..71
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          89..103
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          105..119
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          121..143
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          145..159
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          191..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..223
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          233..247
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          257..295
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          281..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..327
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          377..399
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          417..439
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          465..479
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          481..503
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:19631385"
FT   REGION          484..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           315..320
FT                   /note="NGXEET; peptidase recognition motif"
FT                   /evidence="ECO:0000305|PubMed:17032053"
FT   COMPBIAS        200..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        36..69
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
FT   DISULFID        112..322
FT                   /note="Interchain (between acidic and basic chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
SQ   SEQUENCE   507 AA;  58144 MW;  C587BAB906711472 CRC64;
     MAKPILLSIY LFLIVALFNG CLAQSGGRQQ QQFGQCQLNR LDALEPTNRI EAEAGVIESW
     DPNNQQFQCA GVAVVRRTIE PNGLLLPQYS NAPQLVYIAR GRGITGVLFP GCPETFEESQ
     RQSQQGQSRE FQQDRHQKIR HFREGDIIAF PAGVAHWSYN DGSNPVVAIS LLDTNNNANQ
     LDQNPRNFYL AGNPDDEFRP QGQQEYEQHR RQQQRQQRPG EHGQQQRGLG NNVFSGFDAD
     FLADAFNVDT ETARRLQSEN DHRRSIVRVE GRQLQVIRPR WSREEQEREE RKERERERES
     ESERRQSRRG GRDDNGLEET ICTLRLRENI GDPSRADIYT EEAGRISTVN SHTLPVLRWL
     QLSAERGALY SDALYVPHWN LNAHSVVYAL RGRAEVQVVD NFGQTVFDDE LREGQLLTIP
     QNFAVVKRAR NEGFEWVSFK TNENAMVSPL AGRTSAIRAL PEEVLATAFQ IPREDARRLK
     FNRQESTLVR SRPSRSRSSR SERRAEV