ID   CONG2_LUPAN             Reviewed;         445 AA.
AC   F5B8W7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 2.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Gamma conglutin 2 {ECO:0000303|PubMed:21457583};
DE   AltName: Allergen=Lup an gamma-conglutin {ECO:0000305};
DE   Contains:
DE     RecName: Full=Gamma conglutin 2 beta subunit {ECO:0000305};
DE     AltName: Full=Gamma conglutin 2 small subunit {ECO:0000305};
DE   Contains:
DE     RecName: Full=Gamma conglutin 2 alpha subunit {ECO:0000305};
DE     AltName: Full=Gamma conglutin 2 large subunit {ECO:0000305};
DE   Flags: Precursor;
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil; TISSUE=Seedling;
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-445, AND ALLERGEN.
RC   STRAIN=cv. Tanjil; TISSUE=Seed;
RX   PubMed=21457583; DOI=10.1186/1471-2229-11-59;
RA   Foley R.C., Gao L.-L., Spriggs A., Soo L.Y.C., Goggin D.E., Smith P.M.C.,
RA   Atkins C.A., Singh K.B.;
RT   "Identification and characterisation of seed storage protein transcripts
RT   from Lupinus angustifolius.";
RL   BMC Plant Biol. 11:59-59(2011).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=cv. Zeus;
RX   PubMed=22264085; DOI=10.1021/jf2042592;
RA   Czubinski J., Dwiecki K., Siger A., Kachlicki P., Neunert G.,
RA   Lampart-Szczapa E., Nogala-Kalucka M.;
RT   "Release of flavonoids from lupin globulin proteins during digestion in a
RT   model system.";
RL   J. Agric. Food Chem. 60:1830-1836(2012).
CC   -!- FUNCTION: Sulfur-rich seed storage protein that remains undegraded at
CC       germination. {ECO:0000250|UniProtKB:Q9FSH9}.
CC   -!- SUBUNIT: Two-subunit monomeric unit made of alpha and beta subunits
CC       coupled by disulfide bonds (at pH 4.5 and under non-reducing
CC       conditions) (By similarity). Can also form oligomers including dimer,
CC       tetramer and cyclic hexamer (trimer of dimers) (at pH > 5.5) (By
CC       similarity). Component of globulins complexes which accumulate in seeds
CC       (Probable). Interacts with flavonoids (e.g. apigenin glucosides)
CC       present in globulins complexes (Probable).
CC       {ECO:0000250|UniProtKB:Q42369, ECO:0000250|UniProtKB:Q9FSH9,
CC       ECO:0000305|PubMed:22264085}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q9FEX1}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during seed development.
CC       {ECO:0000269|PubMed:21457583}.
CC   -!- PTM: Glycosylated on alpha chain. {ECO:0000250|UniProtKB:Q42369}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000305|PubMed:21457583}.
CC   -!- BIOTECHNOLOGY: May be used in antidiabetic therapies and diets for type
CC       2 diabetes (T2D). {ECO:0000250|UniProtKB:Q42369}.
CC   -!- MISCELLANEOUS: Capable of reducing glycaemia in mammals.
CC       {ECO:0000250|UniProtKB:Q42369}.
CC   -!- MISCELLANEOUS: Resistant to pancreatin-mediated digestion.
CC       {ECO:0000269|PubMed:22264085}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; CM007362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; HQ670417; AEB33720.1; -; mRNA.
DR   RefSeq; XP_019423133.1; XM_019567588.1.
DR   AlphaFoldDB; F5B8W7; -.
DR   SMR; F5B8W7; -.
DR   GeneID; 109332601; -.
DR   KEGG; lang:109332601; -.
DR   OrthoDB; 536577at2759; -.
DR   Proteomes; UP000188354; Chromosome LG02.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT   CHAIN           34..445
FT                   /note="Gamma conglutin 2"
FT                   /id="PRO_0000446141"
FT   CHAIN           34..293
FT                   /note="Gamma conglutin 2 alpha subunit"
FT                   /id="PRO_0000446142"
FT   CHAIN           294..445
FT                   /note="Gamma conglutin 2 beta subunit"
FT                   /id="PRO_0000446143"
FT   DOMAIN          60..425
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   SITE            293..294
FT                   /note="Cleavage; partial"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        88..178
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        102..115
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        107..133
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        118..128
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        222
FT                   /note="Interchain (between alpha and beta chains, with C-
FT                   436 in beta chain)"
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        346..387
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   DISULFID        436
FT                   /note="Interchain (between alpha and beta chains, with C-
FT                   222 in alpha chain)"
FT                   /evidence="ECO:0000250|UniProtKB:Q42369"
FT   CONFLICT        156
FT                   /note="A -> P (in Ref. 2; AEB33720)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  48741 MW;  FEC6AF1C2FDB0E15 CRC64;
     MAQNMAPIFH FIAISLSCSF LFVLSSSQDS QSLHYPLPTS SSKPSLLVLP IQQDASTGLH
     WANIHKRTPL MQVPVLLDLN GKHLWVTCSY HYSSSTYQAP FCHSTQCSRA NSHQCFTCTD
     SATTRPGCHN NTCALMTSNP VTQEAGFGEL AQDVLAIHST HGSKLGPMVK VLQFLFSCAP
     SFLAQKGLPN NIQGALGLGH APISLPNQLF SHFGLRRQFT MCLSRYPTSN GAILFGDIYD
     PNNNYIDNSV EVLLDMVYTP LGISLQGEYL MQVSAIRVNK HIVVPTKNPS MLSSNHGDSR
     IGGVMITTTN PYTILHHSIY EVFTQVFANN IPKQAQVEAV GPFGLCFDSK KISGGIPNVE
     FVMDSPDDVW RISEENLMVQ AQNGVSCLGF VDGGMHTRTE IALGAHQLEE NLVVFDFAKS
     RVEFNSNPLK SHGKTCANLF DLNNA