CONB1_LUPAN
ID CONB1_LUPAN Reviewed; 611 AA.
AC F5B8V9;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Conglutin beta 1 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Flags: Precursor;
GN Name=BETA1 {ECO:0000303|PubMed:21457583};
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], FUNCTION, AND DEVELOPMENTAL STAGE.
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 [2]
RP ALLERGEN.
RX PubMed=18620408; DOI=10.1021/jf800840u;
RA Goggin D.E., Mir G., Smith W.B., Stuckey M., Smith P.M.;
RT "Proteomic analysis of lupin seed proteins to identify conglutin Beta as an
RT allergen, Lup an 1.";
RL J. Agric. Food Chem. 56:6370-6377(2008).
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).
RN [4]
RP 3D-STRUCTURE MODELING.
RX DOI=10.1007/978-3-319-16483-0_10;
RA Jimenez-Lopez J.C., Lima-Cabello E., Melser S., Foley R.C., Singh K.B.;
RT "Lupin allergy: Uncovering structural features and epitopes of b-conglutin
RT proteins in Lupinus angustifolius L. with a focus on cross-allergenic
RT reactivity to peanut and other legumes.";
RL (In) Ortuno F., Rojas I. (eds.);
RL Bioinformatics and Biomedical Engineering, LNCS 9043, pp.96-107, Springer
RL international publishing, Switzerland (2015).
CC -!- FUNCTION: Seed storage protein. Accumulates during seed development and
CC is hydrolyzed after germination to provide a carbon and nitrogen source
CC for the developing seedling. {ECO:0000269|PubMed:21457583}.
CC -!- SUBUNIT: Component of globulins complexes which accumulate in seeds.
CC {ECO:0000305|PubMed:22264085}.
CC -!- DEVELOPMENTAL STAGE: Increased expression during seed filling, with a
CC maximum between 33 and 38 days after anthesis.
CC {ECO:0000269|PubMed:21457583}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Lup an 1 is the major
CC lupin allergen. {ECO:0000269|PubMed:18620408}.
CC -!- MISCELLANEOUS: The variability of the residues taking part of IgE-
CC binding epitopes might be responsible of the difference in cross-
CC reactivity among legumes. {ECO:0000305|Ref.4}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; HQ670409; AEB33712.1; -; mRNA.
DR RefSeq; XP_019432143.1; XM_019576598.1.
DR AlphaFoldDB; F5B8V9; -.
DR SMR; F5B8V9; -.
DR Allergome; 4015; Lup an 1.
DR PRIDE; F5B8V9; -.
DR EnsemblPlants; OIW21011; OIW21011; TanjilG_27356.
DR GeneID; 109339187; -.
DR Gramene; OIW21011; OIW21011; TanjilG_27356.
DR KEGG; lang:109339187; -.
DR OrthoDB; 1072107at2759; -.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Allergen; Glycoprotein; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..611
FT /note="Conglutin beta 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003326254"
FT DOMAIN 186..344
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 403..569
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 32..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 611 AA; 71926 MW; 9B6147810F865A1E CRC64;
MAKMRVRLPM LILLLGVVFL LAASIGIAYG EKDFTKNPPK EREEEEHEPR QQPRPRQQEE
QEREHRREEK HDGEPSRGRS QSEESQEEEH ERRREHHRER EQEQQPRPQR RQEEEEEEEE
WQPRRQRPQS RREEREEREQ EQGSSSGSQR GSGDERRQHR ERRVHREERE QEQDSRSDSR
RQRNPYHFSS NRFQTYYRNR NGQIRVLERF NQRTNRLENL QNYRIIEFQS KPNTLILPKH
SDADFILVVL NGRATITIVN PDKRQVYNLE QGDALRLPAG TTSYILNPDD NQNLRVAKLA
IPINNPGKLY DFYPSTTKDQ QSYFSGFSKN TLEATFNTRY EEIERVLLGD DELQENEKQR
RGQEQSHQDE GVIVRVSKKQ IQELRKHAQS SSGEGKPSES GPFNLRSNKP IYSNKFGNFY
EITPDINPQF QDLNISLTFT EINEGALLLP HYNSKAIFIV VVDEGEGNYE LVGIRDQQRQ
QDEQEEEYEQ GEEEVRRYSD KLSKGDVFII PAGHPLSINA SSNLRLLGFG INANENQRNF
LAGSEDNVIK QLDREVKELT FPGSIEDVER LIKNQQQSYF ANAQPQQQQQ REKEGRRGRR
GPISSILNAL Y
