CONB5_LUPAN
ID CONB5_LUPAN Reviewed; 637 AA.
AC F5B8W3;
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 5 {ECO:0000303|PubMed:21457583};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Flags: Precursor;
GN Name=BETA5 {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; HQ670413; AEB33716.1; -; mRNA.
DR RefSeq; XP_019459007.1; XM_019603462.1.
DR AlphaFoldDB; F5B8W3; -.
DR SMR; F5B8W3; -.
DR Allergome; 4015; Lup an 1.
DR GeneID; 109358950; -.
DR KEGG; lang:109358950; -.
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; 2.
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..637
FT /note="Conglutin beta 5"
FT /evidence="ECO:0000255"
FT /id="PRO_5003323051"
FT DOMAIN 217..375
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 434..594
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 33..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 637 AA; 75207 MW; 07E515BBB39D8E11 CRC64;
MAKMRVRFPM LVLLLGVVFL LAVSIGIAYG EKDVIKNPER PEERQEEERD PRQPPRSRQQ
EEQEREHRRE KERDREPSRG RSESKQSQEE ERERRKEHDR EREQEQQPQY GRRHEEEEKG
EEEEEGQARR QRPQRRREER EQEQGSSSES RRQSGDERRH RHEKREQREE REQEQGSSSG
RQSDYGRRQR HEGREQREER EQEQGSSSES HRLRNPYYFS SERFQTRYKN KNGQIRVLER
FDQRTNRLEN LQNYRIVEFQ SRPNTLILPK HSDADYILVV LNGRATITIV NPDKRQAYNL
EYGDALRLPA GTTSYILNPD DNQDLRVVKL AIPINNPGKF YDFYPSRTKD QQSYFSGFSK
NTLEATFNTH YEEIQRILLG YEDEQEDEEQ RREQEQSHQD EGVIVRVSKE QIQELRKHAQ
SSSRKGKPSE SGPFNLRSNE PIYSNKFGNF YEITPDRNPQ VQDLDISLIF TEISEGALLL
PHYNSKAIFV IVVDEGEGNY ELVGIRNQQR QQDEQEVEEV RSYNARLSEG DILVIPAGHP
LSINASSNLR LLGFGINADE NQRNFLAGSE DNVIRQLDRE VKELIFPGSA EDVERLIRNQ
QQSYFANAQP QQQQQQREKE GRRGRRGPIS SILSALY
