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2SS1_BEREX
ID   2SS1_BEREX              Reviewed;         146 AA.
AC   P04403; P04402; Q9LRC2;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=2S sulfur-rich seed storage protein 1;
DE   AltName: Allergen=Ber e 1;
DE   Contains:
DE     RecName: Full=2S sulfur-rich seed storage protein small chain 1;
DE     AltName: Full=2S albumin 1 small subunit;
DE   Contains:
DE     RecName: Full=2S sulfur-rich seed storage protein large chain 1B;
DE     AltName: Full=2S albumin 1 large subunit;
DE   Flags: Precursor;
GN   Name=BE2S1;
OS   Bertholletia excelsa (Brazil nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Lecythidaceae; Bertholletia.
OX   NCBI_TaxID=3645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Altenbach S.B., Pearson K.W., Leung F.W., Sun S.S.M.;
RT   "Cloning and sequence analysis of a cDNA encoding a Brazil nut protein
RT   exceptionally rich in methionine.";
RL   Plant Mol. Biol. 8:239-250(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bassuener R.;
RL   Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840683; DOI=10.1007/bf00023994;
RA   Gander E.S., Holmstroem K.O., de Paiva G.R., de Castro L.A.B., Carneiro M.,
RA   Grossi de Sa M.F.;
RT   "Isolation, characterization and expression of a gene coding for a 2S
RT   albumin from Bertholletia excelsa (Brazil nut).";
RL   Plant Mol. Biol. 16:437-448(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yamauchi D.;
RT   "Brazil nut 2S albumin was synthesized in a transgenic French bean seed
RT   with a promoter of the gene for canavalin, 7S globulin from Canavalia
RT   gladiata.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 37-64 AND 70-142, AND PYROGLUTAMATE FORMATION AT
RP   GLN-37.
RX   PubMed=3758080; DOI=10.1111/j.1432-1033.1986.tb09926.x;
RA   Ampe C., van Damme J., de Castro L.A.B., Sampaio M.J.A.M., van Montagu M.,
RA   Vandekerckhove J.;
RT   "The amino-acid sequence of the 2S sulphur-rich proteins from seeds of
RT   Brazil nut (Bertholletia excelsa H.B.K.).";
RL   Eur. J. Biochem. 159:597-604(1986).
RN   [6]
RP   3D-STRUCTURE MODELING, GLYCOSYLATION, AND DISULFIDE BONDS.
RX   PubMed=12421566; DOI=10.1016/s0022-2836(02)01061-6;
RA   Alcocer M.J., Murtagh G.J., Bailey K., Dumoulin M., Meseguer A.S.,
RA   Parker M.J., Archer D.B.;
RT   "The disulphide mapping, folding and characterisation of recombinant Ber e
RT   1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins.";
RL   J. Mol. Biol. 324:165-175(2002).
CC   -!- FUNCTION: This is a 2S seed storage protein.
CC   -!- SUBUNIT: The mature protein consists of a small and a large chain
CC       linked by disulfide bonds.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   EMBL; M17146; AAA33010.1; -; mRNA.
DR   EMBL; X57027; CAA40343.1; -; Genomic_DNA.
DR   EMBL; X57028; CAA40344.1; -; Genomic_DNA.
DR   EMBL; X54490; CAA38362.1; -; Genomic_DNA.
DR   EMBL; AB044391; BAA96554.1; -; Genomic_DNA.
DR   PIR; A25802; A25802.
DR   PIR; S14946; S14946.
DR   PDB; 2LVF; NMR; -; A=37-146.
DR   PDBsum; 2LVF; -.
DR   AlphaFoldDB; P04403; -.
DR   SMR; P04403; -.
DR   Allergome; 3134; Ber e 1.0101.
DR   Allergome; 88; Ber e 1.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; PTHR35496; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW   Pyrrolidone carboxylic acid; Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..36
FT                   /evidence="ECO:0000269|PubMed:3758080"
FT                   /id="PRO_0000032105"
FT   CHAIN           37..64
FT                   /note="2S sulfur-rich seed storage protein small chain 1"
FT                   /id="PRO_0000032106"
FT   PROPEP          65..69
FT                   /evidence="ECO:0000269|PubMed:3758080"
FT                   /id="PRO_0000032107"
FT   CHAIN           70..142
FT                   /note="2S sulfur-rich seed storage protein large chain 1B"
FT                   /id="PRO_0000032108"
FT   PROPEP          143..146
FT                   /id="PRO_0000032109"
FT   MOD_RES         37
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3758080"
FT   DISULFID        40..92
FT                   /note="Interchain (between small and large chains)"
FT                   /evidence="ECO:0000269|PubMed:12421566"
FT   DISULFID        53..81
FT                   /note="Interchain (between small and large chains)"
FT                   /evidence="ECO:0000269|PubMed:12421566"
FT   DISULFID        82..130
FT                   /evidence="ECO:0000269|PubMed:12421566"
FT   DISULFID        94..137
FT                   /evidence="ECO:0000269|PubMed:12421566"
FT   VARIANT         91
FT                   /note="S -> E (in variant 1A)"
FT   CONFLICT        38..39
FT                   /note="EE -> QQ (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102..103
FT                   /note="MR -> RM (in Ref. 4; BAA96554)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="E -> K (in Ref. 4; BAA96554)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="L -> M (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="I -> L (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   HELIX           49..62
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   TURN            63..66
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   HELIX           76..87
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   HELIX           90..108
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   HELIX           114..130
FT                   /evidence="ECO:0007829|PDB:2LVF"
FT   TURN            138..141
FT                   /evidence="ECO:0007829|PDB:2LVF"
SQ   SEQUENCE   146 AA;  16911 MW;  A7DF778FD766410D CRC64;
     MAKISVAAAA LLVLMALGHA TAFRATVTTT VVEEENQEEC REQMQRQQML SHCRMYMRQQ
     MEESPYQTMP RRGMEPHMSE CCEQLEGMDE SCRCEGLRMM MMRMQQEEMQ PRGEQMRRMM
     RLAENIPSRC NLSPMRCPMG GSIAGF
 
 
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