P102E_LUPLU
ID P102E_LUPLU Reviewed; 157 AA.
AC Q7Y1W5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Class 10 plant pathogenesis-related protein 2E {ECO:0000303|Ref.1};
DE Short=Llpr10.2e {ECO:0000303|Ref.1};
DE Short=Ypr-10.2e {ECO:0000303|Ref.1};
DE EC=3.1.27.- {ECO:0000250|UniProtKB:P52779};
DE AltName: Allergen=Lup l 4 {ECO:0000305};
GN Name=PR10.2E {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 [MRNA].
RA Podkowinski J., Kisiel A., Grabowska B., Legocki A.B.;
RT "Yellow lupine pathogenesis-related protein of subclass PR10.2.";
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}.
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DR EMBL; AY288355; AAP37978.1; -; mRNA.
DR AlphaFoldDB; Q7Y1W5; -.
DR SMR; Q7Y1W5; -.
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 2: Evidence at transcript level;
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 2E"
FT /id="PRO_0000445933"
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; 16869 MW; 215677D40590E4C5 CRC64;
MGIFTFEDES TTTVAPARLY KALVKDADTI IPKAVEAIQS VEIVEGNGGP GTIKKLTLIE
GGETKYVLHK IEAIDEANFG YNYSIVGGIG LPDTIEKISF ETKLFEGANG GSIGKVTIKI
ETKGDAQPNE EEGKAAKARG DAFFKAIENY LIAHPEY
