ID   JUGN4_JUGNI             Reviewed;         510 AA.
AC   A0A1L6K371;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=11S globulin {ECO:0000303|PubMed:27936684};
DE   AltName: Full=11S legumin {ECO:0000303|PubMed:27936684, ECO:0000312|EMBL:APR62629.1};
DE   AltName: Allergen=Jug n 4 {ECO:0000303|PubMed:27936684};
DE   Contains:
DE     RecName: Full=11S globulin acidic chain {ECO:0000303|PubMed:27936684};
DE   Contains:
DE     RecName: Full=11S globulin basic chain {ECO:0000303|PubMed:27936684};
DE   Flags: Precursor;
OS   Juglans nigra (Black walnut) (Wallia nigra).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Juglans.
OX   NCBI_TaxID=16719 {ECO:0000312|EMBL:APR62629.1};
RN   [1] {ECO:0000312|EMBL:APR62629.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PTM, ALLERGEN, MOTIF, AND CIRCULAR
RP   DICHROISM ANALYSIS.
RC   STRAIN=cv. Sparrow {ECO:0000303|PubMed:27936684};
RC   TISSUE=Endosperm {ECO:0000303|PubMed:27936684};
RX   PubMed=27936684; DOI=10.1021/acs.jafc.6b04387;
RA   Zhang Y.Z., Du W.X., Fan Y., Yi J., Lyu S.C., Nadeau K.C., Thomas A.L.,
RA   McHugh T.;
RT   "Purification and Characterization of a Black Walnut (Juglans nigra)
RT   Allergen, Jug n 4.";
RL   J. Agric. Food Chem. 65:454-462(2017).
CC   -!- FUNCTION: Seed storage protein. {ECO:0000255|RuleBase:RU003681,
CC       ECO:0000305|PubMed:27936684}.
CC   -!- SUBUNIT: Homohexamer. Can assemble in other multimeric configurations.
CC       {ECO:0000269|PubMed:27936684}.
CC   -!- TISSUE SPECIFICITY: Expressed in endosperm of the seed.
CC       {ECO:0000269|PubMed:27936684}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during seed development.
CC       {ECO:0000269|PubMed:27936684}.
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:27936684}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:27936684}.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC       {ECO:0000255|RuleBase:RU003681, ECO:0000305}.
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DR   EMBL; KX891230; APR62629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L6K371; -.
DR   SMR; A0A1L6K371; -.
DR   Allergome; 11992; Jug n 4.
DR   Allergome; 11993; Jug n 4.0101.
DR   GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR   GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; 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; Direct protein sequencing; Disulfide bond; Seed storage protein;
KW   Signal; Storage protein.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:27936684"
FT   CHAIN           24..318
FT                   /note="11S globulin acidic chain"
FT                   /evidence="ECO:0000305|PubMed:27936684"
FT                   /id="PRO_0000445789"
FT   CHAIN           319..510
FT                   /note="11S globulin basic chain"
FT                   /evidence="ECO:0000305|PubMed:27936684"
FT                   /id="PRO_0000445790"
FT   DOMAIN          38..257
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          331..480
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          194..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           318..323
FT                   /note="NGXEET; peptidase recognition motif"
FT                   /evidence="ECO:0000305|PubMed:27936684"
FT   COMPBIAS        203..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        35..68
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
FT   DISULFID        111..325
FT                   /note="Interchain (between acidic and basic chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P04776"
SQ   SEQUENCE   510 AA;  58056 MW;  9F3C3B585FF31DDE CRC64;
     MAKPILLSIS LCLVALVNGC LAQSGGRQQP RFGECKLKRL VALEPSNRIE AEAGVIESWD
     PNNQQFQCAG VAVVRRTIEP NGLLLPQYSN APQLLYIVKG RGITGVLFPG CPETFEESQQ
     GQSRIRPSLR SASFQRDRHQ KIRHFREGDV IAFPAGVAHW CYNDGDTPVV AVALMDTTNN
     ANQLDQNPRN FYLAGNPDDE FRPQGQQEYE QHRRQQQHQQ RHGEPGQQQR GSGNNVFSGF
     DADFLADAFN VDTETARRLQ SENDHRRSIV RVEGRQLQVI RPRWSREEQE REERKERERE
     RESESERRQS RRGGRDDNGL EETICTLRLR ENIGDPSRAD IYTEEAGRIS TANSHTLPVL
     RWLQLSAERG ALYSDALYVP HWNLNAHSVV YALRGRAEVQ VVDNFGQTVF DDELREGQLL
     TIPQNFAVVK RARNEGFEWV SFKTNENAMV SPLAGRTSAI RALPEEVLAN ALQIPREDAR
     RLKFNRQEST LVRSRPSSSR SSRSERRAEV