CONB2_LUPAN
ID CONB2_LUPAN Reviewed; 603 AA.
AC F5B8W0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Conglutin beta 2 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Flags: Precursor;
GN Name=BETA2 {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; HQ670410; AEB33713.1; -; mRNA.
DR AlphaFoldDB; F5B8W0; -.
DR SMR; F5B8W0; -.
DR Allergome; 4015; Lup an 1.
DR PRIDE; F5B8W0; -.
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..603
FT /note="Conglutin beta 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003325732"
FT DOMAIN 177..335
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 394..554
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 36..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 603 AA; 70701 MW; 80EE7AAD2D253F6F CRC64;
MANMRVKFPT LVLLLGIVFL MAVSIGIAYG EKNAIKNHER PQEREQEERD PRQQPRPRHQ
EEQEREHGRE EERNREPSRG RSESEESREE EREQRREPSR GREQEQQPQH GRREEEEEWQ
PRRQRPQSRR EEREQEQGSS SSSGRQSGYE RREQREEREQ QQEQDSRSES RRQRNPYYFS
YERFQTLYKN RNGQIRVLER FDQRTNRLEN LQNYRIVEFQ SKPNTLILPK HSDADYILVV
LNGRATITIV NPDKRQAYNL EHGDALRLPA GTTSYILNPD DNQNLRVVKL AIPINNPGNF
YDFYPSSTKD QQSYFNGFSR NTLEATFNTR YEEIQRIILG NEDGQEDEEQ SRGQEQSHQD
QGVIVRVSKE QIQELRKHAQ SSSGKGKPSE SGPFNLRSDE PIYSNKFGNF YEITPDRNPQ
AQDLDISLTF IEINEGGLLL PHYNSKAIFV VVVDEGEGNY ELVGIRDQER QQDEQEQEEV
RRYNAKLSEG DIFVIPAGHP ISINASSNLR LLGFGINADE NQRNFLAGSE DNVIRQLDKE
VKQLTFPGSV EDVERLIKNQ QQSYFANAQP QQQQQREKEG RRGRRGLSFP FRSLFTKLLS
TIM
