ID   P102F_LUPLU             Reviewed;         157 AA.
AC   Q7XZT8;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Class 10 plant pathogenesis-related protein 2F {ECO:0000303|Ref.1};
DE            Short=Llpr10.2f {ECO:0000303|Ref.1};
DE            Short=Ypr-10.2f {ECO:0000303|Ref.1};
DE            EC=3.1.27.- {ECO:0000250|UniProtKB:P52779};
DE   AltName: Allergen=Lup l 4 {ECO:0000305};
GN   Name=PR10.2F {ECO:0000303|Ref.1};
OS   Lupinus luteus (European yellow lupine).
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=3873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Handschuh L., Sikorski M.M.;
RT   "Yellow lupine pathogenesis-related protein of class 10.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Class II ribonuclease (RNase) (By similarity). Binds to
CC       cytokinins (By similarity). Interacts with melatonin (By similarity).
CC       {ECO:0000250|UniProtKB:P52779, ECO:0000250|UniProtKB:Q9LLQ2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9LLQ2}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY303549; AAP57943.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7XZT8; -.
DR   SMR; Q7XZT8; -.
DR   Allergome; 9727; Lup l 4.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0044373; F:cytokinin binding; ISS:UniProtKB.
DR   GO; GO:1904408; F:melatonin binding; ISS:UniProtKB.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR   GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
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   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISS:UniProtKB.
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.
PE   3: Inferred from homology;
KW   Allergen; Calcium; Cytoplasm; Hydrolase; Metal-binding; Nuclease;
KW   Pathogenesis-related protein; Plant defense.
FT   CHAIN           1..157
FT                   /note="Class 10 plant pathogenesis-related protein 2F"
FT                   /id="PRO_0000445934"
FT   BINDING         8
FT                   /ligand="trans-zeatin"
FT                   /ligand_id="ChEBI:CHEBI:16522"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         60
FT                   /ligand="trans-zeatin"
FT                   /ligand_id="ChEBI:CHEBI:16522"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         69
FT                   /ligand="trans-zeatin"
FT                   /ligand_id="ChEBI:CHEBI:16522"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         81
FT                   /ligand="trans-zeatin"
FT                   /ligand_id="ChEBI:CHEBI:16522"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
FT   BINDING         83
FT                   /ligand="trans-zeatin"
FT                   /ligand_id="ChEBI:CHEBI:16522"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LLQ2"
SQ   SEQUENCE   157 AA;  16821 MW;  CC3B17D96030EC6F CRC64;
     MGIFTFEDES TTTVAPARLY KALVKDADTI IPKAVEAIQS VEIVEGNGGP GTIKKLTLIE
     GGETKYVLHK IEAIDEANLG YNYSIVGGIG LPDTIEKISF ETKLFEGANG GSIGKVTIKI
     ETKGDAQPNE EEGKAAKARG DAFFKAIENY LIGHPEY