CONB3_LUPAN
ID CONB3_LUPAN Reviewed; 580 AA.
AC F5B8W1;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Conglutin beta 3 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Flags: Precursor;
GN Name=BETA3 {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; HQ670411; AEB33714.1; -; mRNA.
DR AlphaFoldDB; F5B8W1; -.
DR SMR; F5B8W1; -.
DR Allergome; 4015; Lup an 1.
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..580
FT /note="Conglutin beta 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435265"
FT DOMAIN 164..322
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 381..538
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 37..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 580 AA; 68180 MW; 70323722F5A312D4 CRC64;
MAKMRVRFPT LVLLLGIVFL MAVSIGIAYG EKNVLKNHER PQEREQEERD PRQQPRPHHQ
EEQEREHRRE SEESQEEERE QRREPRRERE QEQQPQHGRR EEEEEWQPRR QRPQSRREER
EQEQGSSSSS RRQSGYERRE QREEREQEQE QGSRSDSRRQ RNPYYFSSER FQTLYRNRNG
QIRVLERFDQ RTNRLENLQN YRIVEFQSKP NTLILPKHSD ADYILVVLNG SATITIVNPD
KRQSYNLENG DALRLPAGTT SYILNPDDNQ NLRVVKLAIP INNPGNFYDF YPSSSKDQQS
YFSGFSKNTL EATFNTRYEE IQSILLGNED EQEDDEQWHG QEQSHQDEGV IVRVSKEQVQ
ELRKYAQSSS RKGKPYESGP FNLRSNKPIY SNKFGNFYEI TPDRNPQAQD LDISLTFIEI
NEGALLLPHY NSKAIFVVVV DEGEGNYELV GIRDQQRQQD EQEVRRYSAR LSEGDIFVIP
AGHPISINAS SNLRLLGFGI NADENQRNFL AGSEDNVIRQ LDREVKGLIF PGSAEDVERL
IKNQQQSYFA NAQPQQQQQR EREGRHGRRG HISSILSTLY
