CONB1_LUPAL
ID CONB1_LUPAL Reviewed; 531 AA.
AC Q53HY0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Conglutin beta 1 {ECO:0000303|PubMed:17320919};
DE AltName: Full=Protein Lup-1 {ECO:0000303|PubMed:20461737};
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:CAI84850.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17320919; DOI=10.1016/j.phytochem.2007.01.003;
RA Magni C., Scarafoni A., Herndl A., Sessa F., Prinsi B., Espen L.,
RA Duranti M.;
RT "Combined 2D electrophoretic approaches for the study of white lupin mature
RT seed storage proteome.";
RL Phytochemistry 68:997-1007(2007).
RN [2]
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 [3]
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 [4]
RP ALLERGEN, AND IDENTIFICATION BY MASS SPECTROMETRY.
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. {ECO:0000269|PubMed:17320919}.
CC -!- FUNCTION: [Blad]: Has a lectin-like activity.
CC {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: 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; AJ966470; CAI84850.2; -; mRNA.
DR AlphaFoldDB; Q53HY0; -.
DR SMR; Q53HY0; -.
DR Allergome; 3818; Lup a 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; Direct protein sequencing; Glycoprotein; Seed storage protein;
KW Signal; Storage protein.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..108
FT /evidence="ECO:0000269|PubMed:9299789"
FT /id="PRO_0000435268"
FT CHAIN 109..281
FT /note="Blad"
FT /evidence="ECO:0000250|UniProtKB:Q6EBC1"
FT /id="PRO_0000435269"
FT CHAIN 113..531
FT /note="Conglutin beta 1"
FT /id="PRO_0000435270"
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..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
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..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 531 AA; 62032 MW; 3DF0BE88026CCB5A CRC64;
MGKMRVRFPT LVLVLGIVFL MAVSIGIAYG EKDVLKSHER PEEREQEEWQ PRRQRPQSRR
EEREQEQEQG SPSYPRRQSG YERRQYHERS EQREEREQEQ QQGSPSYSRR QRNPYHFNSQ
RFQTLYKNRN GKIRVLERFD QRTNRLENLQ NYRIVEFQSK PNTLILPKHS DADYVLVVLN
GRATITIVNP DRRQAYNLEY GDALRIPAGS TSYILNPDDN QKLRVVKLAI PINNPGYFYD
FYPSSTKDQQ SYFSGFSRNT LEATFNTRYE EIQRILLGNE DEQEYEEQRR GQEQSHQDEG
VIVRVSREQI QELTKYAQSS SGKDKPSQSG PFNLRSNEPI YSNKYGNFYE ITPDRNPQVQ
DLDISLTFTE INEGALLLPH YNSKAIFIVV VGEGNGKYEL VGIRDQQRQQ DEQEEEPEEV
RRYSARLSEG DIFVIPAGYP ISVNASSNLR LLGFGINAYE NQRNFLAGSE DNVIRQLDRE
VKELTFPGSA EDIERLIKNQ QQSYFANALP QQQQQSEKEG RRGRRGPISS I
