CONG1_LUPAN
ID CONG1_LUPAN Reviewed; 449 AA.
AC Q42369; A0A1J7HL10;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Gamma conglutin 1 {ECO:0000303|PubMed:21457583};
DE AltName: Full=Conglutin gamma {ECO:0000303|PubMed:8425065, ECO:0000303|PubMed:9247543};
DE AltName: Allergen=Lup an gamma-conglutin {ECO:0000305};
DE Contains:
DE RecName: Full=Gamma conglutin 1 beta subunit {ECO:0000303|PubMed:29635768};
DE AltName: Full=Gamma conglutin 1 small subunit {ECO:0000305};
DE Contains:
DE RecName: Full=Gamma conglutin 1 alpha subunit {ECO:0000303|PubMed:29635768};
DE AltName: Full=Gamma conglutin 1 large subunit {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=LOC109345795 {ECO:0000312|EMBL:OIW13559.1};
GN ORFNames=TanjilG_29300 {ECO:0000312|EMBL:OIW13559.1};
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 [MRNA].
RC STRAIN=cv. Unicrop; TISSUE=Cotyledon;
RX PubMed=8425065; DOI=10.1007/bf00019956;
RA Kolivas S., Gayler K.R.;
RT "Structure of the cDNA coding for conglutin gamma, a sulphur-rich protein
RT from Lupinus angustifolius.";
RL Plant Mol. Biol. 21:397-401(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP SULFUR DEFICIENCY.
RA Ilgoutz S.C., Gayler K.R.;
RT "Isolation of the conglutin gamma gene from Lupinus angustifolius L.";
RL (er) Plant Gene Register PGR95-024(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, 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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 34-36 AND 296-298, PROTEOLYTIC CLEAVAGE, N-TERMINUS
RP PROTEIN SEQUENCING, IDENTIFICATION BY MASS SPECTROMETRY, PTM, SUBUNIT,
RP DISULFIDE BOND, AND GLYCOSYLATION.
RC STRAIN=cv. Zeus; TISSUE=Seed;
RX PubMed=29635768; DOI=10.1002/jsfa.9057;
RA Czubinski J., Montowska M., Fornal E.;
RT "Post-translational cleavage pattern of Lupinus angustifolius gamma-
RT conglutin.";
RL J. Sci. Food Agric. 98:5212-5219(2018).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Unicrop;
RX PubMed=9247543; DOI=10.1023/a:1005868105651;
RA Ilgoutz S.C., Knittel N., Lin J.M., Sterle S., Gayler K.R.;
RT "Transcription of genes for conglutin gamma and a leginsulin-like protein
RT in narrow-leafed lupin.";
RL Plant Mol. Biol. 34:613-627(1997).
RN [7]
RP SUBUNIT, AND GLYCOSYLATION.
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).
RN [8]
RP SUBUNIT.
RC STRAIN=cv. Zeus;
RX PubMed=24054261; DOI=10.1016/j.foodchem.2013.08.015;
RA Czubinski J., Dwiecki K., Siger A., Neunert G., Lampart-Szczapa E.;
RT "Characterisation of different digestion susceptibility of lupin seed
RT globulins.";
RL Food Chem. 143:418-426(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Coromup;
RX PubMed=28863333; DOI=10.1016/j.jchromb.2017.08.025;
RA Mane S., Bringans S., Johnson S., Pareek V., Utikar R.;
RT "Reverse phase HPLC method for detection and quantification of lupin seed
RT gamma-conglutin.";
RL J. Chromatogr. B 1063:123-129(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 33-449, PROTEIN SEQUENCE OF
RP 296-301, GLYCOSYLATION AT ASN-130, DISULFIDE BONDS, SUBUNIT, BIOTECHNOLOGY,
RP PROTEOLYTIC CLEAVAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Zeus; TISSUE=Seed;
RX PubMed=25664733; DOI=10.1107/s1399004714025073;
RA Czubinski J., Barciszewski J., Gilski M., Szpotkowski K., Debski J.,
RA Lampart-Szczapa E., Jaskolski M.;
RT "Structure of gamma-conglutin: insight into the quaternary structure of 7S
RT basic globulins from legumes.";
RL Acta Crystallogr. D 71:224-238(2015).
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) (PubMed:29635768, PubMed:25664733, PubMed:22264085). Can
CC also form oligomers including dimer, tetramer and cyclic hexamer
CC (trimer of dimers) (at pH > 5.5) (PubMed:22264085, PubMed:25664733).
CC Component of globulins complexes which accumulate in seeds
CC (PubMed:22264085). Interacts with flavonoids (e.g. apigenin glucosides)
CC present in globulins complexes (PubMed:22264085, PubMed:24054261).
CC Forms a static complex with vitexin (PubMed:24054261).
CC {ECO:0000269|PubMed:22264085, ECO:0000269|PubMed:24054261,
CC ECO:0000269|PubMed:25664733, ECO:0000269|PubMed:29635768}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9FEX1}.
CC -!- TISSUE SPECIFICITY: Expressed in developing cotyledons and in the
CC embryonic axis of germinating seeds (PubMed:9247543). Accumulates in
CC seeds, especially in the protein bodies of developing cotyledonary
CC cells (at protein level) (Ref.2, PubMed:28863333). Also detected, at
CC low levels, in plumules and radicles (PubMed:9247543).
CC {ECO:0000269|PubMed:28863333, ECO:0000269|PubMed:9247543,
CC ECO:0000269|Ref.2}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during seed development
CC (PubMed:21457583, PubMed:9247543). In seeds, localized to the embryo
CC tissues and to a layer of cells adjacent to the seed coat
CC (PubMed:9247543). {ECO:0000269|PubMed:21457583,
CC ECO:0000269|PubMed:9247543}.
CC -!- INDUCTION: By sulfur deficiency. {ECO:0000269|Ref.2}.
CC -!- PTM: Undergoes very complex post-translational maturation; the
CC proteolytic processing leading to the formation of two alpha and beta
CC subunits is incomplete, leaving a certain amount of the protein in an
CC uncut form. {ECO:0000269|PubMed:25664733, ECO:0000269|PubMed:29635768}.
CC -!- PTM: Glycosylated on alpha chain. {ECO:0000269|PubMed:22264085,
CC ECO:0000269|PubMed:29635768}.
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:0000305|PubMed:25664733}.
CC -!- MISCELLANEOUS: Capable of reducing glycaemia in mammals.
CC {ECO:0000305|PubMed:25664733}.
CC -!- MISCELLANEOUS: Resistant to pancreatin-mediated digestion.
CC {ECO:0000269|PubMed:22264085, ECO:0000269|PubMed:24054261}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OIW13559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X65601; CAA46552.1; -; mRNA.
DR EMBL; L39786; AAB53771.1; -; Genomic_DNA.
DR EMBL; HQ670416; AEB33719.1; -; mRNA.
DR EMBL; KV861538; OIW13559.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM007364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S21426; S21426.
DR RefSeq; XP_019440547.1; XM_019585002.1.
DR PDB; 4PPH; X-ray; 2.01 A; A/B/C/D/E/F=33-449.
DR PDBsum; 4PPH; -.
DR AlphaFoldDB; Q42369; -.
DR SMR; Q42369; -.
DR Allergome; 7699; Lup an gamma_Conglutin.
DR iPTMnet; Q42369; -.
DR EnsemblPlants; OIW13559; OIW13559; TanjilG_29300.
DR GeneID; 109345795; -.
DR Gramene; OIW13559; OIW13559; TanjilG_29300.
DR KEGG; lang:109345795; -.
DR OrthoDB; 536577at2759; -.
DR Proteomes; UP000188354; Chromosome LG04.
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; 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 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:29635768"
FT CHAIN 34..449
FT /note="Gamma conglutin 1"
FT /id="PRO_5015097557"
FT CHAIN 34..295
FT /note="Gamma conglutin 1 alpha subunit"
FT /id="PRO_0000446139"
FT CHAIN 296..449
FT /note="Gamma conglutin 1 beta subunit"
FT /id="PRO_0000446140"
FT DOMAIN 60..429
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT SITE 295..296
FT /note="Cleavage; partial"
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0000269|PubMed:29635768"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:25664733, ECO:0007744|PDB:4PPH"
FT DISULFID 88..178
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 102..115
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 107..133
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 118..128
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 222
FT /note="Interchain (between alpha and beta chains, with C-
FT 440 in beta chain)"
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 350..391
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT DISULFID 440
FT /note="Interchain (between alpha and beta chains, with C-
FT 222 in alpha chain)"
FT /evidence="ECO:0000269|PubMed:25664733,
FT ECO:0007744|PDB:4PPH"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4PPH"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4PPH"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:4PPH"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 145..161
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 164..179
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:4PPH"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:4PPH"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:4PPH"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:4PPH"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:4PPH"
SQ SEQUENCE 449 AA; 48916 MW; 348BE0FCFBD084F3 CRC64;
MARNMAHILH ILVISLSYSF LFVSSSSQDS QSLYHNSQPT SSKPNLLVLP VQEDASTGLH
WANIHKRTPL MQVPLLLDLN GKHLWVTCSQ HYSSSTYQAP FCHSTQCSRA NTHQCFTCTD
STTTRPGCHN NTCGLLSSNP VTQESGLGEL AQDVLAIHST HGSKLGPMVK VPQFLFSCAP
SFLAQKGLPN NVQGALGLGQ APISLQNQLF SHFGLKRQFS VCLSRYSTSN GAILFGDIND
PNNNNYIHNS LDVLHDLVYT PLTISKQGEY FIQVNAIRVN KHLVIPTKNP FISPSSTSYH
GSGEIGGALI TTTHPYTVLS HSIFEVFTQV FANNMPKQAQ VKAVGPFGLC YDSRKISGGA
PSVDLILDKN DAVWRISSEN FMVQAQDGVS CLGFVDGGVH ARAGIALGAH HLEENLVVFD
LERSRVGFNS NSLKSYGKTC SNLFDLNNP
