CONG1_LUPAL
ID CONG1_LUPAL Reviewed; 452 AA.
AC Q9FSH9;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Gamma conglutin 1 {ECO:0000305};
DE AltName: Full=Conglutin gamma 32 {ECO:0000303|PubMed:11406286};
DE AltName: Allergen=Lup a gamma-conglutin {ECO:0000305};
DE Contains:
DE RecName: Full=Gamma conglutin 1 beta subunit {ECO:0000305};
DE AltName: Full=Gamma conglutin 1 17 kDa subunit {ECO:0000305|PubMed:19962718};
DE AltName: Full=Gamma conglutin 1 small subunit {ECO:0000305|PubMed:11406286};
DE Contains:
DE RecName: Full=Gamma conglutin 1 alpha subunit {ECO:0000305};
DE AltName: Full=Gamma conglutin 1 29 kDa subunit {ECO:0000305|PubMed:19962718};
DE AltName: Full=Gamma conglutin 1 large subunit {ECO:0000305|PubMed:11406286};
DE Flags: Precursor;
GN Name=Cgamma {ECO:0000303|PubMed:24894193};
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 34-60; 69-81;
RP 98-136; 197-212; 301-307 AND 346-352, PROTEOLYTIC CLEAVAGE, TISSUE
RP SPECIFICITY, INDUCTION BY HEAT, SUBCELLULAR LOCATION, FUNCTION, AND
RP 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).
RN [2]
RP SUBUNIT.
RC TISSUE=Seed;
RX PubMed=20670643; DOI=10.1016/j.ijbiomac.2010.07.005;
RA Capraro J., Spotti P., Magni C., Scarafoni A., Duranti M.;
RT "Spectroscopic studies on the pH-dependent structural dynamics of gamma-
RT conglutin, the blood glucose-lowering protein of lupin seeds.";
RL Int. J. Biol. Macromol. 47:502-507(2010).
RN [3]
RP INDUCTION BY CHITOSAN, AND CAUTION.
RC STRAIN=cv. Multitalia;
RX PubMed=19962718; DOI=10.1016/j.phytochem.2009.11.001;
RA Scarafoni A., Ronchi A., Duranti M.;
RT "gamma-Conglutin, the Lupinus albus XEGIP-like protein, whose expression is
RT elicited by chitosan, lacks of the typical inhibitory activity against GH12
RT endo-glucanases.";
RL Phytochemistry 71:142-148(2010).
RN [4]
RP BIOTECHNOLOGY, AND MISCELLANEOUS.
RX PubMed=21605639; DOI=10.1016/j.fitote.2011.05.007;
RA Bertoglio J.C., Calvo M.A., Hancke J.L., Burgos R.A., Riva A.,
RA Morazzoni P., Ponzone C., Magni C., Duranti M.;
RT "Hypoglycemic effect of lupin seed gamma-conglutin in experimental animals
RT and healthy human subjects.";
RL Fitoterapia 82:933-938(2011).
RN [5]
RP BIOTECHNOLOGY, MISCELLANEOUS, AND SUBUNIT.
RC STRAIN=cv. Multitalia;
RX PubMed=21733318; DOI=10.1017/s0007114511002601;
RA Lovati M.R., Manzoni C., Castiglioni S., Parolari A., Magni C., Duranti M.;
RT "Lupin seed gamma-conglutin lowers blood glucose in hyperglycaemic rats and
RT increases glucose consumption of HepG2 cells.";
RL Br. J. Nutr. 107:67-73(2012).
RN [6]
RP BIOTECHNOLOGY, AND MISCELLANEOUS.
RX PubMed=23872149; DOI=10.1016/j.bbrc.2013.07.026;
RA Capraro J., Magni C., Faoro F., Maffi D., Scarafoni A., Tedeschi G.,
RA Maffioli E., Parolari A., Manzoni C., Lovati M.R., Duranti M.;
RT "Internalisation and multiple phosphorylation of gamma-Conglutin, the lupin
RT seed glycaemia-lowering protein, in HepG2 cells.";
RL Biochem. Biophys. Res. Commun. 437:648-652(2013).
RN [7]
RP GLYCOSYLATION AT ASN-131, PTM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24069245; DOI=10.1371/journal.pone.0073906;
RA Schiarea S., Arnoldi L., Fanelli R., De Combarieu E., Chiabrando C.;
RT "In-depth glycoproteomic characterization of gamma-conglutin by high-
RT resolution accurate mass spectrometry.";
RL PLoS ONE 8:E73906-E73906(2013).
RN [8]
RP BIOTECHNOLOGY, AND MISCELLANEOUS.
RC STRAIN=cv. Multitalia;
RX PubMed=24394732; DOI=10.1039/c3fo60583c;
RA Capraro J., Magni C., Scarafoni A., Caramanico R., Rossi F.,
RA Morlacchini M., Duranti M.;
RT "Pasta supplemented with isolated lupin protein fractions reduces body
RT weight gain and food intake of rats and decreases plasma glucose
RT concentration upon glucose overload trial.";
RL Food Funct. 5:375-380(2014).
RN [9]
RP SUBUNIT, BIOTECHNOLOGY, AND MISCELLANEOUS.
RX PubMed=24894193; DOI=10.1007/s11130-014-0424-y;
RA Vargas-Guerrero B., Garcia-Lopez P.M., Martinez-Ayala A.L.,
RA Dominguez-Rosales J.A., Gurrola-Diaz C.M.;
RT "Administration of Lupinus albus gamma conglutin (Cgamma) to n5 STZ rats
RT augmented Ins-1 gene expression and pancreatic insulin content.";
RL Plant Foods Hum. Nutr. 69:241-247(2014).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 360-SER--GLY-362 AND HIS-439.
RX PubMed=26741537; DOI=10.1016/j.plaphy.2015.11.008;
RA Scarafoni A., Consonni A., Pessina S., Balzaretti S., Capraro J.,
RA Galanti E., Duranti M.;
RT "Structural basis of the lack of endo-glucanase inhibitory activity of
RT Lupinus albus gamma-conglutin.";
RL Plant Physiol. Biochem. 99:79-85(2016).
RN [11]
RP BIOTECHNOLOGY, AND MISCELLANEOUS.
RX PubMed=28101822; DOI=10.1007/s11130-016-0597-7;
RA Gonzalez-Santiago A.E., Vargas-Guerrero B., Garcia-Lopez P.M.,
RA Martinez-Ayala A.L., Dominguez-Rosales J.A., Gurrola-Diaz C.M.;
RT "Lupinus albus conglutin gamma modifies the gene expressions of enzymes
RT involved in glucose hepatic production in vivo.";
RL Plant Foods Hum. Nutr. 72:134-140(2017).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=30312772; DOI=10.1016/j.bbapap.2018.10.005;
RA Scire A., Baldassarre M., Tanfani F., Capraro J., Duranti M., Scarafoni A.;
RT "Interaction of gamma-conglutin from Lupinus albus with model phospholipid
RT membranes: Investigations on structure, thermal stability and
RT oligomerization status.";
RL Biochim. Biophys. Acta 1866:1242-1248(2018).
CC -!- FUNCTION: Sulfur-rich seed storage protein that remains undegraded at
CC germination (PubMed:11406286). The uncleaved form exhibits some
CC inhibitory activity against GH11 xylanase from T.longibrachiatum, more
CC at pH 7 than at pH 5.3, but not against GH12 xyloglucan-specific
CC endoglucanase (XEG) from A.aculeatus (PubMed:26741537). Binds to model
CC phospholipid membranes containing dimyristoyl phosphatidylglycerol
CC (DMPG), dioleoyl phosphatidic acid (DOPA) or mixture of dimyristoyl
CC phosphatidylcholine and dimyristoyl phosphatidylglycerol (DMPC:DMPG),
CC or mixture of dioleoyl phosphatidic acid and dioleoyl
CC phosphatidylcholine (DOPC:DOPA) (PubMed:30312772).
CC {ECO:0000269|PubMed:26741537, ECO:0000269|PubMed:30312772,
CC 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) (PubMed:20670643, PubMed:21733318, PubMed:24894193).
CC Monomeric alpha and beta subunits in reducing conditions
CC (PubMed:21733318, PubMed:24894193, PubMed:30312772). Can also form
CC oligomers including dimer, tetramer and cyclic hexamer (trimer of
CC dimers) (at pH > 5.5) (PubMed:20670643, PubMed:30312772). Component of
CC globulins complexes which accumulate in seeds (By similarity).
CC Interacts with flavonoids (e.g. apigenin glucosides) present in
CC globulins complexes (By similarity). {ECO:0000250|UniProtKB:Q42369,
CC ECO:0000269|PubMed:20670643, ECO:0000269|PubMed:21733318,
CC ECO:0000269|PubMed:24894193, ECO:0000269|PubMed:30312772}.
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 seeds
CC (PubMed:11406286). Strongly induced by chitosan in the cotyledons of
CC germinating seeds (PubMed:19962718). {ECO:0000269|PubMed:19962718,
CC ECO:0000303|PubMed:11406286}.
CC -!- PTM: Glycosylated on alpha chain at Asn-131; identified N-glycans bound
CC are Man(2)(Xyl)(Fuc)GlcNAc(2), Man(3)(Xyl)(Fuc)GlcNAc(2),
CC GlcNAcMan(3)(Xyl)(Fuc)GlcNAc(2) and GlcNAc(2)Man(3)(Xyl)(Fuc)GlcNAc(2).
CC {ECO:0000269|PubMed:24069245}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000250|UniProtKB:Q42369}.
CC -!- BIOTECHNOLOGY: Being internalized and phosphorylated in liver
CC hepatocellular cells, stimulating pancreatic insulin accumulation, and
CC exhibiting hypoglycemic effect on human and rat, may be used in
CC antidiabetic therapies and diets (e.g. lupin flour or enriched pasta)
CC for type 2 diabetes (T2D). {ECO:0000269|PubMed:21605639,
CC ECO:0000269|PubMed:21733318, ECO:0000269|PubMed:23872149,
CC ECO:0000269|PubMed:24394732, ECO:0000269|PubMed:24894193,
CC ECO:0000269|PubMed:28101822}.
CC -!- MISCELLANEOUS: Resistant to pancreatin-mediated digestion.
CC {ECO:0000250|UniProtKB:Q42369}.
CC -!- MISCELLANEOUS: Mediates a dose-dependent decrease of blood plasma
CC glucose and increased Ins1 expression and pancreatic insulin levels in
CC hyperglycaemic/diabetic rats daily fed with gamma conglutin 1 or
CC supplemented pasta (PubMed:21605639, PubMed:21733318, PubMed:24394732,
CC PubMed:24894193, PubMed:28101822). Involved in reducing rat hepatic
CC glucose production, mainly through G6pc inhibition in impaired glucose
CC metabolism disorders, but without leading to hypoglycemia
CC (PubMed:28101822). Triggers an increased glucose consumption of human
CC liver hepatocellular HepG2 cells and potentiates the activity of
CC insulin and metformin in cell glucose consumption (PubMed:21733318).
CC Internalized by and subsequently phosphorylated at Thr-69, Thr-182,
CC Thr-331, Tyr-354, Ser-360 and Ser-442 in HepG2 cells cytoplasm
CC (PubMed:23872149). Exhibits hypoglycemic effect when orally
CC administered 30 minutes before carbohydrate supply in human trials, but
CC insulin concentrations are not affected (PubMed:21605639).
CC {ECO:0000269|PubMed:21605639, ECO:0000269|PubMed:21733318,
CC ECO:0000269|PubMed:23872149, ECO:0000269|PubMed:24394732,
CC ECO:0000269|PubMed:24894193, ECO:0000269|PubMed:28101822}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
CC -!- CAUTION: Despite homology with xyloglucan-specific endo-beta-1,4-
CC glucanase inhibitor proteins (XEGIPs) and T.aestivum xylanase inhibitor
CC (TAXI-I), fails to inhibit representative fungal endo-glucanases and
CC other cell wall-degrading enzymes. {ECO:0000269|PubMed:19962718}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Dark horse - Issue 211 of
CC February 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/211/";
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DR EMBL; AJ297490; CAC16394.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FSH9; -.
DR SMR; Q9FSH9; -.
DR Allergome; 2686; Lup a gamma_Conglutin.
DR iPTMnet; Q9FSH9; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA: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:0000269|PubMed:11406286"
FT CHAIN 34..452
FT /note="Gamma conglutin 1"
FT /id="PRO_5004329433"
FT CHAIN 34..300
FT /note="Gamma conglutin 1 alpha subunit"
FT /id="PRO_0000446144"
FT CHAIN 301..452
FT /note="Gamma conglutin 1 beta subunit"
FT /id="PRO_0000446145"
FT DOMAIN 61..432
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT SITE 296..297
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000269|PubMed:11406286"
FT SITE 298..299
FT /note="Cleavage; alternate"
FT /evidence="ECO:0000269|PubMed:11406286"
FT SITE 300..301
FT /note="Cleavage; partial"
FT /evidence="ECO:0000269|PubMed:11406286"
FT SITE 439
FT /note="Required for inhibitory activity against GH11
FT glucanase"
FT /evidence="ECO:0000269|PubMed:26741537"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:24069245"
FT DISULFID 89..179
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 103..116
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 108..134
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 119..129
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 223
FT /note="Interchain (between alpha and beta chains, with C-
FT 443 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 353..394
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT DISULFID 443
FT /note="Interchain (between alpha and beta chains, with C-
FT 223 in alpha chain)"
FT /evidence="ECO:0000250|UniProtKB:Q42369"
FT MUTAGEN 360..362
FT /note="SGG->LGNNLGGYA: In MuT; the uncleaved form exhibits
FT some inhibitory activity against GH11 glucanase from
FT T.longibrachiatum, both at pH 5.3 and pH 7, but not against
FT GH12 xyloglucan-specific endoglucanase (XEG) from
FT A.aculeatus. In MuT-H/S; loss of inhibitory activity
FT against GH11 glucanase from T.longibrachiatum; when
FT associated with S-439."
FT /evidence="ECO:0000269|PubMed:26741537"
FT MUTAGEN 360..362
FT /note="SGG->VSTRVGPA: In MuX; the uncleaved form exhibits
FT some inhibitory activity against GH11 glucanase from
FT T.longibrachiatum, more at pH 5.3 than at pH 7, but not
FT against GH12 xyloglucan-specific endoglucanase (XEG) from
FT A.aculeatus. In MuX-H/S; loss of inhibitory activity
FT against GH11 glucanase from T.longibrachiatum; when
FT associated with S-439."
FT /evidence="ECO:0000269|PubMed:26741537"
FT MUTAGEN 439
FT /note="H->S: In MuX-H/S; loss of inhibitory activity
FT against GH11 glucanase from T.longibrachiatum; when
FT associated with 360-VSTRVGPA-367. In MuT-H/S; loss of
FT inhibitory activity against GH11 glucanase from
FT T.longibrachiatum; when associated with 360-LGNNLGGYA-368."
FT /evidence="ECO:0000269|PubMed:26741537"
SQ SEQUENCE 452 AA; 49219 MW; C343BA283BE752FF CRC64;
MAKNMAPILH ILVISLSYSF LFVTSSSQNS QSLYHNSQPT SSSKPNLLVL PIQQDASTKL
HWGNILKRTP LMQVPVLLDL NGKHLWVTCS QHYSSSTYQA PFCHSTQCSR ANTHQCFTCT
DSTTSRPGCH NNTCGLISSN PVTQESGLGE LAQDVLALHS THGSKLGSLV KIPQFLFSCA
PTFLTQKGLP NNVQGALGLG HAPISLPNQL FSHFGLKRQF TMCLSSYPTS NGAILFGDIN
DPNNNNYIHN SLDVLHDMVY TPLTISKQGE YFIQVSAIRV NKHMVIPTKN PSMFPSSSSS
SYHESSEIGG AMITTTNPYT VLRHSIFEVF TQVFANNVPK QAQVKAVGPF GLCYDTKKIS
GGVPSVDLIM DKSDVVWRIS GENLMVQAQD GVSCLGFVDG GVHTRAGIAL GTHQLEENLV
VFDLARSRVG FNTNSLKSHG KSCSNLFDLN NP
