P102A_LUPLU
ID P102A_LUPLU Reviewed; 158 AA.
AC Q9LLQ3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Class 10 plant pathogenesis-related protein 2A {ECO:0000303|Ref.1};
DE Short=LlPR10.2a {ECO:0000303|Ref.1};
DE Short=Ypr-10.2a {ECO:0000303|Ref.2};
DE EC=3.1.27.- {ECO:0000250|UniProtKB:P52779};
DE AltName: Allergen=Lup l 4 {ECO:0000305};
GN Name=PR10.2A {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].
RC STRAIN=cv. Ventus; TISSUE=Root;
RX DOI=10.1007/0-306-47615-0_171;
RA Sikorski M.M., Handschuh L.A., Biesiadka J., Legocki A.B.;
RT "Two subclasses of yellow lupin PR10 proteins and their possible function
RT during the symbiosis development.";
RL Curr. Plant Sci. Biotechnol. Agric. 38:319-322(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Handschuh L., Sikorski M.M.;
RT "Yellow lupine pathogenesis-related protein of class 10.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP REVIEW.
RX PubMed=24311578; DOI=10.1107/s0907444913021975;
RA Ruszkowski M., Szpotkowski K., Sikorski M., Jaskolski M.;
RT "The landscape of cytokinin binding by a plant nodulin.";
RL Acta Crystallogr. D 69:2365-2380(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-158.
RX PubMed=15608381; DOI=10.1107/s0907444904028173;
RA Pasternak O., Biesiadka J., Dolot R., Handschuh L., Bujacz G.,
RA Sikorski M.M., Jaskolski M.;
RT "Structure of a yellow lupin pathogenesis-related PR-10 protein belonging
RT to a novel subclass.";
RL Acta Crystallogr. D 61:99-107(2005).
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; AF170091; AAF77633.1; -; mRNA.
DR EMBL; AY729802; AAU43882.1; -; Genomic_DNA.
DR PDB; 1XDF; X-ray; 1.90 A; A/B=2-158.
DR PDBsum; 1XDF; -.
DR AlphaFoldDB; Q9LLQ3; -.
DR SMR; Q9LLQ3; -.
DR Allergome; 9727; Lup l 4.
DR EvolutionaryTrace; Q9LLQ3; -.
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 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Cytoplasm; Hydrolase; Metal-binding;
KW Nuclease; Pathogenesis-related protein; Plant defense.
FT CHAIN 1..158
FT /note="Class 10 plant pathogenesis-related protein 2A"
FT /id="PRO_0000445929"
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"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:1XDF"
FT STRAND 110..126
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:1XDF"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:1XDF"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1XDF"
SQ SEQUENCE 158 AA; 16904 MW; C08DF886B68E4BDF CRC64;
MGVFTFEDES TSTIAPARLY KALVKDADAI IPKAVEAIQS IETVEGNGGP GTIKKLTLIE
GGETKYVLHK IEAVDEANLR YNYSIVGGVG LPDTIEKISF ETKLVEGANG GSIGKVTIKI
ETKGDAQPNE EEGKAAKARG DAFFKAIENY LSAHPEYN
