BEV1J_BETPN
ID BEV1J_BETPN Reviewed; 160 AA.
AC P43183;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Major pollen allergen Bet v 1-J {ECO:0000303|PubMed:7852325};
DE AltName: Full=Allergen Bet v I-J {ECO:0000303|PubMed:7852325};
DE AltName: Allergen=Bet v 1-J {ECO:0000303|PubMed:7852325};
GN Name=BETV1J {ECO:0000303|PubMed:7852325};
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 PARTIAL PROTEIN SEQUENCE.
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 [2]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-160 IN COMPLEX WITH
RP 1-ANILINO-8-NAPHTHALENE SULFONATE.
RX PubMed=22634284; DOI=10.1016/j.jmb.2012.05.016;
RA Kofler S., Asam C., Eckhard U., Wallner M., Ferreira F., Brandstetter H.;
RT "Crystallographically mapped ligand binding differs in high and low IgE
RT binding isoforms of birch pollen allergen bet v 1.";
RL J. Mol. Biol. 422:109-123(2012).
CC -!- FUNCTION: May be a general steroid carrier protein.
CC {ECO:0000250|UniProtKB:P43185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80889}.
CC -!- TISSUE SPECIFICITY: Pollen. {ECO:0000305|PubMed:7852325}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Is a cause of type I
CC allergic reactions in Europe, North America and USSR.
CC {ECO:0000305|PubMed:7852325}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; X77271; CAA54487.1; -; mRNA.
DR PIR; G55699; G55699.
DR PDB; 4A8U; X-ray; 1.16 A; A=2-160.
DR PDB; 4A8V; X-ray; 1.23 A; A=2-160.
DR PDBsum; 4A8U; -.
DR PDBsum; 4A8V; -.
DR AlphaFoldDB; P43183; -.
DR SMR; P43183; -.
DR Allergome; 101; Bet v 1.0106.
DR Allergome; 89; Bet v 1.
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:0000255"
FT CHAIN 2..160
FT /note="Major pollen allergen Bet v 1-J"
FT /id="PRO_0000154181"
FT REGION 116..118
FT /note="Hydrophobic ligand pocket"
FT /evidence="ECO:0000269|PubMed:22634284,
FT ECO:0007744|PDB:4A8V"
FT REGION 133..141
FT /note="Hydrophobic ligand pocket"
FT /evidence="ECO:0000269|PubMed:22634284,
FT ECO:0007744|PDB:4A8V"
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 STRAND 3..14
FT /evidence="ECO:0007829|PDB:4A8U"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:4A8U"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4A8U"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:4A8U"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:4A8U"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:4A8U"
FT STRAND 113..126
FT /evidence="ECO:0007829|PDB:4A8U"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:4A8U"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:4A8U"
SQ SEQUENCE 160 AA; 17540 MW; 2DF9E6E0171193AD CRC64;
MGVFNYETEA TSVIPAARLF KAFILDGDNL FPKVAPQAIS SVENIEGNGG PGTIKKISFP
EGFPFKYVKD RVDEVDHTNF KYSYSVIEGG PVGDTLEKIS NEIKIVATPN GGSILKINNK
YHTKGDHEVK AEQIKASKEM GETLLRAVES YLLAHSDAYN
