CONB2_LUPAL
ID CONB2_LUPAL Reviewed; 533 AA.
AC Q6EBC1; Q0R0N3;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Conglutin beta 2 {ECO:0000303|Ref.1};
DE AltName: Allergen=Lup an 1 {ECO:0000303|PubMed:18620408};
DE Contains:
DE RecName: Full=Blad {ECO:0000303|PubMed:9299789};
DE Flags: Precursor;
OS Lupinus albus (White lupine) (Lupinus termis).
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=3870 {ECO:0000312|EMBL:AAS97865.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Monteiro S.A., Freitas R.M., Teixeira A.N., Ferreira R.B.;
RT "The lectin-like breakdown product of beta-conglutin catabolism. Studies on
RT its origin.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-281, PROTEIN SEQUENCE OF 109-145 AND
RP 277-281, AND SUBUNIT.
RX PubMed=20066045; DOI=10.1371/journal.pone.0008542;
RA Monteiro S., Freitas R., Rajasekhar B.T., Teixeira A.R., Ferreira R.B.;
RT "The unique biosynthetic route from lupinus beta-conglutin gene to blad.";
RL PLoS ONE 5:E8542-E8542(2010).
RN [3]
RP PROTEIN SEQUENCE OF 113-131, FUNCTION (BLAD), AND DEVELOPMENTAL STAGE
RP (BLAD).
RX PubMed=9299789; DOI=10.1007/s00050161;
RA dos Ramos P.C., Ferreira R.M., Franco E., Teixeira A.R.;
RT "Accumulation of a lectin-like breakdown product of beta-conglutin
RT catabolism in cotyledons of germinating Lupinus albus L. seeds.";
RL Planta 203:26-34(1997).
RN [4]
RP ALLERGEN, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [5]
RP ALLERGEN.
RX PubMed=20461737; DOI=10.1002/mnfr.200900452;
RA Guillamon E., Rodriguez J., Burbano C., Muzquiz M., Pedrosa M.M.,
RA Cabanillas B., Crespo J.F., Sancho A.I., Mills E.N., Cuadrado C.;
RT "Characterization of lupin major allergens (Lupinus albus L.).";
RL Mol. Nutr. Food Res. 54:1668-1676(2010).
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.
CC -!- FUNCTION: [Blad]: Has a lectin-like activity.
CC {ECO:0000269|PubMed:9299789}.
CC -!- SUBUNIT: Multimers. Give rise to a complex array of processed forms,
CC due to a large number of processing sites and changes in glycosylation.
CC {ECO:0000269|PubMed:20066045}.
CC -!- DEVELOPMENTAL STAGE: [Blad]: Sudden accumulation in cotyledons of 4-
CC day-old plants, but rapidly disappears about 12-14 days after the onset
CC of germination. {ECO:0000269|PubMed:9299789}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Lup an 1 is the major
CC lupin allergen. {ECO:0000269|PubMed:18620408,
CC ECO:0000269|PubMed:20461737}.
CC -!- MISCELLANEOUS: Conglutin beta is characterized by a broad
CC microheterogeneity with almost a continuum of polypeptides ranging in
CC molecular mass from 15 to 72 KDa. Blad, the major 20 KDa polypeptide,
CC may be considered as a stable, intermediary product of conglutin beta
CC catabolism. {ECO:0000269|PubMed:20066045}.
CC -!- MISCELLANEOUS: The initial characterization of blad (PubMed:9299789)
CC was made on a seed storage protein extract containing both conglutin
CC beta 1 and 2. {ECO:0000305|PubMed:9299789}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; AY500372; AAS97865.1; -; mRNA.
DR EMBL; DQ142920; ABB13526.1; -; mRNA.
DR AlphaFoldDB; Q6EBC1; -.
DR SMR; Q6EBC1; -.
DR Allergome; 3818; Lup a 1.
DR PRIDE; Q6EBC1; -.
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; Direct protein sequencing; Glycoprotein; Seed storage protein;
KW Signal; Storage protein.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..533
FT /note="Conglutin beta 2"
FT /id="PRO_0000435271"
FT PROPEP 31..108
FT /evidence="ECO:0000269|PubMed:20066045,
FT ECO:0000269|PubMed:9299789"
FT /id="PRO_0000435272"
FT CHAIN 109..281
FT /note="Blad"
FT /evidence="ECO:0000269|PubMed:20066045"
FT /id="PRO_0000435273"
FT DOMAIN 115..273
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 332..494
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 37..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 533 AA; 62130 MW; F17E49A6F2C4E9EC CRC64;
MGKMRVRFPT LVLVLGIVFL MAVSIGIAYG EKDVLKSHER PEEREQEEWQ PRRQRPQSRR
EEREQEQEQG SPSYPRRQSG YERRQYHERS EQREEREQEQ QQGSPSYSRR QRNPYHFSSQ
RFQTLYKNRN GKIRVLERFD QRTNRLENLQ NYRIVEFQSK PNTLILPKHS DADYVLVVLN
GRATITIVNP DRRQAYNLEY GDALRIPAGS TSYILNPDDN QKLRVVKLAI PINNPGYFYD
FYPSSTKDQQ SYFSGFSRNT LEATFNTRYE EIQRIILGNE DEQEYEEQRR GQEQSDQDEG
VIVIVSKKQI QKLTKHAQSS SGKDKPSDSG PFNLRSNEPI YSNKYGNFYE ITPDRNPQVQ
DLNISLTYIK INEGALLLPH YNSKAIYVVV VDEGEGNYEL VGIRDQQRQQ DEQEEKEEEV
IRYSARLSEG DIFVIPAGYP ISINASSNLR LLGFGINADE NQRNFLAGSK DNVIRQLDRA
VNELTFPGSA EDIERLIKNQ QQSYFANGQP QQQQQQQSEK EGRRGRRGSS LPF
