PRU1_PRUAV
ID PRU1_PRUAV Reviewed; 160 AA.
AC O24248;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Major allergen Pru av 1;
DE AltName: Full=Allergen Pru a 1;
DE AltName: Allergen=Pru av 1;
GN Name=PRUA1;
OS Prunus avium (Cherry) (Cerasus avium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=42229;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9393965; DOI=10.1016/s0161-5890(97)00072-2;
RA Scheurer S., Metzner K., Haustein D., Vieths S.;
RT "Molecular cloning, expression and characterization of Pru a 1, the major
RT cherry allergen.";
RL Mol. Immunol. 34:619-629(1997).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=11287426; DOI=10.1074/jbc.m101657200;
RA Neudecker P., Schweimer K., Nerkamp J., Scheurer S., Vieths S., Sticht H.,
RA Rosch P.;
RT "Allergic cross-reactivity made visible. Solution structure of the major
RT cherry allergen Pru av 1.";
RL J. Biol. Chem. 276:22756-22763(2001).
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE and
CC induces a strong histamine release.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; U66076; AAC02632.1; -; mRNA.
DR PDB; 1E09; NMR; -; A=2-160.
DR PDB; 1H2O; NMR; -; A=2-160.
DR PDBsum; 1E09; -.
DR PDBsum; 1H2O; -.
DR AlphaFoldDB; O24248; -.
DR BMRB; O24248; -.
DR SMR; O24248; -.
DR Allergome; 1316; Pru av 1.0101.
DR Allergome; 597; Pru av 1.
DR EnsemblPlants; Pav_sc0000174.1_g1420.1.mk:mrna; Pav_sc0000174.1_g1420.1.mk:mrna; Pav_sc0000174.1_g1420.1.mk.
DR Gramene; Pav_sc0000174.1_g1420.1.mk:mrna; Pav_sc0000174.1_g1420.1.mk:mrna; Pav_sc0000174.1_g1420.1.mk.
DR EvolutionaryTrace; O24248; -.
DR Proteomes; UP000515124; Unplaced.
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 PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Pathogenesis-related protein; Plant defense;
KW Reference proteome.
FT CHAIN 1..160
FT /note="Major allergen Pru av 1"
FT /id="PRO_0000154202"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1E09"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:1E09"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1E09"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1E09"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1E09"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1E09"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1E09"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:1E09"
FT STRAND 111..123
FT /evidence="ECO:0007829|PDB:1E09"
FT HELIX 131..154
FT /evidence="ECO:0007829|PDB:1E09"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1H2O"
SQ SEQUENCE 160 AA; 17660 MW; 4CED0AF76310A893 CRC64;
MGVFTYESEF TSEIPPPRLF KAFVLDADNL VPKIAPQAIK HSEILEGDGG PGTIKKITFG
EGSQYGYVKH KIDSIDKENY SYSYTLIEGD ALGDTLEKIS YETKLVASPS GGSIIKSTSH
YHTKGNVEIK EEHVKAGKEK ASNLFKLIET YLKGHPDAYN