CONB4_LUPAN
ID CONB4_LUPAN Reviewed; 590 AA.
AC F5B8W2;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Conglutin beta 4 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Flags: Precursor;
GN Name=BETA4 {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; HQ670412; AEB33715.1; -; mRNA.
DR AlphaFoldDB; F5B8W2; -.
DR SMR; F5B8W2; -.
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..590
FT /note="Conglutin beta 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435266"
FT DOMAIN 174..332
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 391..548
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 38..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 590 AA; 69407 MW; CFE2FF4D47B8494A CRC64;
MIKMRVRFPT LVLLLGIVFL MAVSIGIAYG EKNVIKNHER PQEREQEERD PRQQPRPHHQ
EEQEREHRRE EERDREPSRG RSESEESREE EREQRREPRR EREQEQQPQH GRREEEEEWQ
PRRQRPQSRR EEREQEQGSS SSSRRQSGYE RREEREQEQE QGSRSDSRRQ RNPYYFSSER
FQTLYRNRNG QIRVLERFDQ RTDRLENLQN YRIVEFQSKP NTLILPKHSD ADYILVVLNG
SATITIVNPD KRQSYNLENG DALRLPAGTT SYILNPDDNQ NLRVVKLAIP INNPGNFYDF
YPSSSKDQQS YFSGFSRNTL EATFNTRYEE IQRILLGNED EQEDDEQRHG QEQSHQDEGV
IVRVSKEQVQ ELRKYAQSSS RKGKPSKSGP FNLRSNKPIY SNKFGNFYEI TPNRNPQAQD
LDISLTFIEI NEGALLLPHY NSKAIFVVLV DEGEGNYELV GIRDQQRQQD EQEVRRYSAR
LSEGDIFVIP AGHPISINAS SNLRLLGFGI NADENQRNFL AGSEDNVIRQ LDTEVKGLTF
PGSTEDVERL IKNQQQSYFA NAQPQQQQQR EREGRRGRRG HISSILSTLY
