CONG2_LUPAL
ID CONG2_LUPAL Reviewed; 448 AA.
AC Q9FEX1;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Gamma conglutin 2 {ECO:0000305};
DE AltName: Full=Conglutin gamma 48 {ECO:0000303|PubMed:11406286};
DE AltName: Allergen=Lup a 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|PubMed:11406286};
DE Contains:
DE RecName: Full=Gamma conglutin 2 alpha subunit {ECO:0000305};
DE AltName: Full=Gamma conglutin 2 large subunit {ECO:0000305|PubMed:11406286};
DE Flags: Precursor;
OS Lupinus albus (White lupine) (Lupinus termis).
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=3870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 100-138; 199-214;
RP 297-303 AND 342-348, PROTEOLYTIC CLEAVAGE, TISSUE SPECIFICITY, INDUCTION BY
RP HEAT, SUBCELLULAR LOCATION, FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Ultra;
RX PubMed=11406286; DOI=10.1016/s0167-4781(01)00225-1;
RA Scarafoni A., Di Cataldo A., Vassilevskaia T.D., Bekman E.P.,
RA Rodrigues-Pousada C., Ceciliani F., Duranti M.;
RT "Cloning, sequencing and expression in the seeds and radicles of two
RT Lupinus albus conglutin gamma genes.";
RL Biochim. Biophys. Acta 1519:147-151(2001).
CC -!- FUNCTION: Sulfur-rich seed storage protein that remains undegraded at
CC germination. {ECO:0000303|PubMed:11406286}.
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 (By similarity). Interacts with flavonoids (e.g. apigenin glucosides)
CC present in globulins complexes (By similarity).
CC {ECO:0000250|UniProtKB:Q42369, ECO:0000250|UniProtKB:Q9FSH9}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000303|PubMed:11406286}. Note=Present in the extracellular spaces
CC of germinating cotyledons and in the young roots.
CC {ECO:0000303|PubMed:11406286}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds and in the young
CC roots and cotyledons of germinating seeds and young seedlings.
CC {ECO:0000269|PubMed:11406286}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during seed development.
CC {ECO:0000269|PubMed:11406286}.
CC -!- INDUCTION: Secreted in high amounts upon heat treatment of mature
CC seeds. {ECO:0000303|PubMed:11406286}.
CC -!- PTM: Glycosylated on alpha chain. {ECO:0000250|UniProtKB:Q42369}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000250|UniProtKB:Q42369}.
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:0000250|UniProtKB:Q42369}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; AJ297568; CAC17729.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9FEX1; -.
DR SMR; Q9FEX1; -.
DR Allergome; 2686; Lup a gamma_Conglutin.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000250|UniProtKB:Q9FSH9"
FT CHAIN 34..448
FT /note="Gamma conglutin 2"
FT /id="PRO_0000446146"
FT CHAIN 34..296
FT /note="Gamma conglutin 2 alpha subunit"
FT /id="PRO_0000446147"
FT CHAIN 297..448
FT /note="Gamma conglutin 2 beta subunit"
FT /id="PRO_0000446148"
FT DOMAIN 63..428
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT SITE 296..297
FT /note="Cleavage; partial"
FT /evidence="ECO:0000269|PubMed:11406286"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 91..181
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 105..118
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 110..136
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 121..131
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 225
FT /note="Interchain (between alpha and beta chains, with C-
FT 439 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 349..390
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 439
FT /note="Interchain (between alpha and beta chains, with C-
FT 225 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
SQ SEQUENCE 448 AA; 49513 MW; EC92D46B17F42ADA CRC64;
MAKNMAQIFP FIAVFLSCSF IFVLSSSQNS QSLYHNPQST SSSSSKPSLL VLPIQQDAST
GLHWANIHKR TPLMQVPVLL DLNGKHLWVT CSYHYSSSTY QAPFCHSTQC SRANSHHCFT
CTDSATSRPG CHNNTCALMS SNPVTQEAGF GELAQDVLAI HSTHGSKLGP MVRVLQYLFS
CAPSFLAQKG LPNNVQGPLG LGHAPISLQN QLFSHFGLKR QFAMCLSRYP TSNGAILFGD
IYDLDNNYIH NSIDVLIDMV YTPLRISQQG EYFMQVNAIR VNKHMVVPTK NPSMLSSYHG
DSRIGGAMIT TTNPYTILHH SIFEVFTQVF ANNMPKEAQV ESVGPFGLCY DSRKLSGGIP
SVEFVMDSHD DVWRISDENL MVQAQNGVSC LGFVDGGMHT RTEIVLGTHQ LEENMVVFDL
ERSRVEFNSN SLKSHGKTCA NIFDLNNA
