BEV1A_BETPN
ID BEV1A_BETPN Reviewed; 160 AA.
AC P15494; Q96369;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Major pollen allergen Bet v 1-A;
DE AltName: Full=Allergen Bet v I-A;
DE AltName: Allergen=Bet v 1-A;
GN Name=BETVIA; Synonyms=BETVI;
OS Betula pendula (European white birch) (Betula verrucosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=3505;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-35.
RC TISSUE=Pollen;
RX PubMed=2571499; DOI=10.1002/j.1460-2075.1989.tb03597.x;
RA Breiteneder H., Pettenburger K., Bito A., Valenta R., Kraft D., Rumpold H.,
RA Scheiner O., Breitenbach M.;
RT "The gene coding for the major birch pollen allergen Betv1, is highly
RT homologous to a pea disease resistance response gene.";
RL EMBO J. 8:1935-1938(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pollen;
RA Larsen J.N.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-160.
RC TISSUE=Pollen;
RX PubMed=7852325; DOI=10.1074/jbc.270.6.2607;
RA Swoboda I., Jilek A., Ferreira F., Engel E., Hoffman-Sommergruber K.,
RA Scheiner O., Kraft D., Breiteneder H., Pittenauer E., Schmid E.,
RA Vicente O., Heberle-Bors E., Ahorn H., Breitenbach M.;
RT "Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid
RT chromatography, mass spectrometry, and cDNA cloning.";
RL J. Biol. Chem. 270:2607-2613(1995).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2101127; DOI=10.1159/000235269;
RA Elsayed S., Vik H.;
RT "Purification and N-terminal amino acid sequence of two birch pollen
RT isoallergens (Bet v I and Bet v II).";
RL Int. Arch. Allergy Appl. Immunol. 93:378-384(1990).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8702605; DOI=10.1074/jbc.271.32.19243;
RA Faber C., Lindemann A., Sticht H., Ejchart A., Kungl A., Susani M.,
RA Frank R.W., Kraft D., Breitenbach M., Roesch P.;
RT "Secondary structure and tertiary fold of the birch pollen allergen Bet v 1
RT in solution.";
RL J. Biol. Chem. 271:19243-19250(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND STRUCTURE BY NMR.
RX PubMed=8946858; DOI=10.1038/nsb1296-1040;
RA Gajhede M., Osmark P., Poulsen F.M., Ipsen H., Larsen J.N.,
RA van Neerven R.J.J., Schou C., Loewenstein H., Spangfort M.D.;
RT "X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy.";
RL Nat. Struct. Biol. 3:1040-1045(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH THE FAB FRAGMENT FROM
RP A MURINE MONOCLONAL IGG1 AB.
RX PubMed=10861069; DOI=10.4049/jimmunol.165.1.331;
RA Mirza O., Henriksen A., Ipsen H., Larsen J.N., Wissenbach M.,
RA Spangfort M.D., Gajhede M.;
RT "Dominant epitopes and allergic cross-reactivity: complex formation between
RT a Fab fragment of a monoclonal murine IgG antibody and the major allergen
RT from birch pollen Bet v 1.";
RL J. Immunol. 165:331-338(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH THE FAB FRAGMENT FROM
RP THE HUMAN MONOCLONAL BV16 IMMUNOGLOBULIN, AND MUTAGENESIS OF ASN-29;
RP LYS-33; GLU-46; ASN-48; GLU-61 AND PRO-109.
RX PubMed=12960334; DOI=10.4049/jimmunol.171.6.3084;
RA Spangfort M.D., Mirza O., Ipsen H., Van Neerven R.J., Gajhede M.,
RA Larsen J.N.;
RT "Dominating IgE-binding epitope of Bet v 1, the major allergen of birch
RT pollen, characterized by X-ray crystallography and site-directed
RT mutagenesis.";
RL J. Immunol. 171:3084-3090(2003).
CC -!- FUNCTION: May be a general steroid carrier protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALLERGEN: Causes an allergic reaction in human. Is a cause of type I
CC allergic reactions in Europe, North America and USSR.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; X15877; CAA33887.1; -; mRNA.
DR EMBL; Z80098; CAB02153.1; -; mRNA.
DR EMBL; Z80099; CAB02154.1; -; mRNA.
DR EMBL; Z80104; CAB02159.1; -; mRNA.
DR PIR; S05376; S05376.
DR PDB; 1B6F; NMR; -; A=2-160.
DR PDB; 1BTV; NMR; -; A=2-160.
DR PDB; 1BV1; X-ray; 2.00 A; A=2-160.
DR PDB; 1FSK; X-ray; 2.90 A; A/D/G/J=2-160.
DR PDB; 1LLT; X-ray; 3.10 A; A=2-160.
DR PDB; 1QMR; X-ray; 2.15 A; A=2-160.
DR PDB; 4A80; X-ray; 1.96 A; A=2-160.
DR PDB; 4A81; X-ray; 2.05 A; A=2-160.
DR PDB; 4A83; X-ray; 1.54 A; A=2-160.
DR PDB; 4A84; X-ray; 1.50 A; A=2-160.
DR PDB; 4A85; X-ray; 1.40 A; A=2-160.
DR PDB; 4A86; X-ray; 1.59 A; A=2-160.
DR PDB; 4A87; X-ray; 1.24 A; A=2-160.
DR PDB; 4A88; X-ray; 1.51 A; A=2-160.
DR PDB; 4A8G; X-ray; 2.10 A; A=2-160.
DR PDB; 4B9R; X-ray; 1.76 A; A=2-160.
DR PDB; 4BK6; X-ray; 1.63 A; A/B=2-160.
DR PDB; 4BK7; X-ray; 1.14 A; A=2-160.
DR PDB; 4BKC; X-ray; 1.73 A; A/B=2-160.
DR PDB; 4BKD; X-ray; 1.17 A; A=2-160.
DR PDB; 4BTZ; X-ray; 1.47 A; A=2-160.
DR PDB; 4MNS; X-ray; 1.20 A; A=2-160.
DR PDB; 4QIP; X-ray; 2.00 A; A=2-160.
DR PDB; 4Z3L; X-ray; 2.50 A; A/B/C/D/E/F=2-160.
DR PDB; 6R3C; NMR; -; A=2-160.
DR PDB; 7MXL; EM; 3.20 A; C=1-160.
DR PDB; 7N0U; X-ray; 3.00 A; C=2-160.
DR PDB; 7N0V; X-ray; 3.71 A; C=2-160.
DR PDBsum; 1B6F; -.
DR PDBsum; 1BTV; -.
DR PDBsum; 1BV1; -.
DR PDBsum; 1FSK; -.
DR PDBsum; 1LLT; -.
DR PDBsum; 1QMR; -.
DR PDBsum; 4A80; -.
DR PDBsum; 4A81; -.
DR PDBsum; 4A83; -.
DR PDBsum; 4A84; -.
DR PDBsum; 4A85; -.
DR PDBsum; 4A86; -.
DR PDBsum; 4A87; -.
DR PDBsum; 4A88; -.
DR PDBsum; 4A8G; -.
DR PDBsum; 4B9R; -.
DR PDBsum; 4BK6; -.
DR PDBsum; 4BK7; -.
DR PDBsum; 4BKC; -.
DR PDBsum; 4BKD; -.
DR PDBsum; 4BTZ; -.
DR PDBsum; 4MNS; -.
DR PDBsum; 4QIP; -.
DR PDBsum; 4Z3L; -.
DR PDBsum; 6R3C; -.
DR PDBsum; 7MXL; -.
DR PDBsum; 7N0U; -.
DR PDBsum; 7N0V; -.
DR AlphaFoldDB; P15494; -.
DR BMRB; P15494; -.
DR SMR; P15494; -.
DR BindingDB; P15494; -.
DR ChEMBL; CHEMBL3879834; -.
DR Allergome; 123; Bet v 1.0112.
DR Allergome; 89; Bet v 1.
DR Allergome; 90; Bet v 1.0101.
DR ABCD; P15494; 15 sequenced antibodies.
DR EvolutionaryTrace; P15494; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
DR SMART; SM01037; Bet_v_1; 1.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Cytoplasm; Direct protein sequencing;
KW Pathogenesis-related protein; Plant defense.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2571499,
FT ECO:0000269|PubMed:7852325"
FT CHAIN 2..160
FT /note="Major pollen allergen Bet v 1-A"
FT /id="PRO_0000154174"
FT BINDING 55
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:P43185"
FT BINDING 82
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:P43185"
FT BINDING 84
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:P43185"
FT BINDING 101
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000250|UniProtKB:P43185"
FT VARIANT 63
FT /note="F -> L"
FT MUTAGEN 29
FT /note="N->T: Slightly reduced interaction with BV16; when
FT associated with N-33."
FT /evidence="ECO:0000269|PubMed:12960334"
FT MUTAGEN 33
FT /note="K->N: Slightly reduced interaction with BV16; when
FT associated with T-29."
FT /evidence="ECO:0000269|PubMed:12960334"
FT MUTAGEN 46
FT /note="E->S: Strongly reduced interaction with BV16,
FT hypoallergenic."
FT /evidence="ECO:0000269|PubMed:12960334"
FT MUTAGEN 48
FT /note="N->S: Slightly reduced interaction with BV16."
FT /evidence="ECO:0000269|PubMed:12960334"
FT MUTAGEN 61
FT /note="E->S: Slightly reduced interaction with BV16."
FT /evidence="ECO:0000269|PubMed:12960334"
FT MUTAGEN 109
FT /note="P->G: Slightly reduced interaction with BV16."
FT /evidence="ECO:0000269|PubMed:12960334"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:4BK7"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:4BK7"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4BK7"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:4BK7"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1LLT"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:4BK7"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4BK7"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4QIP"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:4BK7"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1B6F"
FT STRAND 113..126
FT /evidence="ECO:0007829|PDB:4BK7"
FT HELIX 131..154
FT /evidence="ECO:0007829|PDB:4BK7"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:4BK7"
SQ SEQUENCE 160 AA; 17571 MW; 69B44110BBDA1AC6 CRC64;
MGVFNYETET TSVIPAARLF KAFILDGDNL FPKVAPQAIS SVENIEGNGG PGTIKKISFP
EGFPFKYVKD RVDEVDHTNF KYNYSVIEGG PIGDTLEKIS NEIKIVATPD GGSILKISNK
YHTKGDHEVK AEQVKASKEM GETLLRAVES YLLAHSDAYN
