P102B_LUPLU
ID P102B_LUPLU Reviewed; 158 AA.
AC Q9LLQ2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Class 10 plant pathogenesis-related protein 2B {ECO:0000303|Ref.1};
DE Short=LlPR10.2b {ECO:0000303|Ref.1};
DE Short=Ypr-10.2b {ECO:0000303|Ref.2};
DE EC=3.1.27.- {ECO:0000250|UniProtKB:P52779};
DE AltName: Allergen=Lup l 4 {ECO:0000305};
GN Name=PR10.2B {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 (SEP-2003) 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] {ECO:0007744|PDB:2QIM}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP TRANS-ZEATIN, AND FUNCTION.
RX PubMed=18406424; DOI=10.1016/j.jmb.2008.03.027;
RA Fernandes H., Pasternak O., Bujacz G., Bujacz A., Sikorski M.M.,
RA Jaskolski M.;
RT "Lupinus luteus pathogenesis-related protein as a reservoir for
RT cytokinin.";
RL J. Mol. Biol. 378:1040-1051(2008).
RN [5] {ECO:0007744|PDB:3E85}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH 1,3-DIPHENYLUREA,
RP AND FUNCTION.
RX PubMed=19220853; DOI=10.1111/j.1742-4658.2009.06892.x;
RA Fernandes H., Bujacz A., Bujacz G., Jelen F., Jasinski M., Kachlicki P.,
RA Otlewski J., Sikorski M.M., Jaskolski M.;
RT "Cytokinin-induced structural adaptability of a Lupinus luteus PR-10
RT protein.";
RL FEBS J. 276:1596-1609(2009).
RN [6] {ECO:0007744|PDB:5MXB, ECO:0007744|PDB:5MXW}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 2-156 IN COMPLEXES WITH MELATONIN
RP AND TRANS-ZEATIN, AND FUNCTION.
RX PubMed=29630775; DOI=10.1111/febs.14455;
RA Sliwiak J., Sikorski M., Jaskolski M.;
RT "PR-10 proteins as potential mediators of melatonin-cytokinin cross-talk in
RT plants: crystallographic studies of LlPR-10.2B isoform from yellow
RT lupine.";
RL FEBS J. 285:1907-1922(2018).
CC -!- FUNCTION: Class II ribonuclease (RNase) (By similarity). Binds to
CC several cytokinins including natural adenine-type (e.g. trans-zeatin
CC and kinetin) and artificial urea-type (e.g. N,N'-diphenylurea and N-
CC phenyl-N'-(2-chloro-4-pyridyl)urea) hormones (PubMed:18406424,
CC PubMed:19220853, PubMed:29630775). Interacts with melatonin
CC (PubMed:29630775). {ECO:0000250|UniProtKB:P52779,
CC ECO:0000269|PubMed:18406424, ECO:0000269|PubMed:19220853,
CC ECO:0000269|PubMed:29630775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:18406424}.
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; AF170092; AAF77634.1; -; mRNA.
DR EMBL; AY377535; AAQ83586.1; -; Genomic_DNA.
DR PDB; 2QIM; X-ray; 1.35 A; A=1-158.
DR PDB; 3E85; X-ray; 1.95 A; A=1-158.
DR PDB; 5MXB; X-ray; 1.51 A; A=2-156.
DR PDB; 5MXW; X-ray; 1.57 A; A=2-157.
DR PDBsum; 2QIM; -.
DR PDBsum; 3E85; -.
DR PDBsum; 5MXB; -.
DR PDBsum; 5MXW; -.
DR AlphaFoldDB; Q9LLQ2; -.
DR SMR; Q9LLQ2; -.
DR Allergome; 9727; Lup l 4.
DR EvolutionaryTrace; Q9LLQ2; -.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0044373; F:cytokinin binding; IDA:UniProtKB.
DR GO; GO:1904408; F:melatonin binding; IDA: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 2B"
FT /id="PRO_0000445930"
FT BINDING 8
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 60
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0000269|PubMed:29630775, ECO:0007744|PDB:2QIM,
FT ECO:0007744|PDB:5MXW"
FT BINDING 69
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 81
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT BINDING 83
FT /ligand="melatonin"
FT /ligand_id="ChEBI:CHEBI:16796"
FT /evidence="ECO:0000269|PubMed:29630775,
FT ECO:0007744|PDB:5MXB, ECO:0007744|PDB:5MXW"
FT BINDING 83
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18406424,
FT ECO:0007744|PDB:2QIM"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2QIM"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:2QIM"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2QIM"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2QIM"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:2QIM"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2QIM"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:2QIM"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2QIM"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:2QIM"
FT STRAND 94..106
FT /evidence="ECO:0007829|PDB:2QIM"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5MXB"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:2QIM"
FT HELIX 130..153
FT /evidence="ECO:0007829|PDB:2QIM"
SQ SEQUENCE 158 AA; 16888 MW; 756A0144AAE9FECD CRC64;
MGVFTFQDEY TSTIAPAKLY KALVTDADII IPKAVETIQS VEIVEGNGGP GTIKKLTFIE
GGESKYVLHK IEAIDEANLG YNYSIVGGVG LPDTIEKISF ETKLVEGANG GSIGKVTIKI
ETKGDAQPNE EEGKAAKARG DAFFKAIESY LSAHPDYN
