L18B_LUPLU
ID L18B_LUPLU Reviewed; 156 AA.
AC P52779;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein LlR18B;
DE EC=3.1.27.- {ECO:0000269|PubMed:12079359};
DE AltName: Full=LlPR10.1B;
DE AltName: Allergen=Lup l 4 {ECO:0000305};
GN Name=LLR18B;
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;
RA Sikorski M.M., Szlagowska A.E., Legocki A.B.;
RT "cDNA sequences encoding for two homologues of Lupinus luteus (L.) IPR-like
RT proteins (LlR18A and LlR18B).";
RL (er) Plant Gene Register PGR95-114(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ventus; TISSUE=Root;
RA Sikorski M.M., Szlagowska A.E.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-156, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=12079359; DOI=10.1016/s0022-2836(02)00385-6;
RA Biesiadka J., Bujacz G., Sikorski M.M., Jaskolski M.;
RT "Crystal structures of two homologous pathogenesis-related proteins from
RT yellow lupine.";
RL J. Mol. Biol. 319:1223-1234(2002).
CC -!- FUNCTION: Class II ribonuclease (RNase), with low activity on single-
CC strand RNA (PubMed:12079359). Binds to cytokinins (By similarity).
CC Interacts with melatonin (By similarity).
CC {ECO:0000250|UniProtKB:Q9LLQ2, ECO:0000269|PubMed:12079359}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:12079359};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9LLQ2}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots.
CC {ECO:0000269|PubMed:12079359}.
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; X79975; CAA56299.1; -; mRNA.
DR EMBL; AF002278; AAC12791.1; -; Genomic_DNA.
DR PDB; 1IFV; X-ray; 2.25 A; A/B=2-156.
DR PDBsum; 1IFV; -.
DR AlphaFoldDB; P52779; -.
DR SMR; P52779; -.
DR Allergome; 9727; Lup l 4.
DR EvolutionaryTrace; P52779; -.
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; IDA: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; IDA: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.
DR PROSITE; PS00451; PATHOGENESIS_BETVI; 1.
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..156
FT /note="Protein LlR18B"
FT /id="PRO_0000154193"
FT BINDING 8
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P52778"
FT BINDING 28
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52778"
FT BINDING 32
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 54
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P52778"
FT BINDING 133
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P52778"
FT BINDING 136
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P52778"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1IFV"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1IFV"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 36..49
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1IFV"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 95..107
FT /evidence="ECO:0007829|PDB:1IFV"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1IFV"
FT STRAND 111..125
FT /evidence="ECO:0007829|PDB:1IFV"
FT HELIX 129..152
FT /evidence="ECO:0007829|PDB:1IFV"
SQ SEQUENCE 156 AA; 16655 MW; 9B9A2FD0E4310AC0 CRC64;
MGVFAFEDEH PSAVAQAKLF KALTKDSDDI IPKVIEQIQS VEIVEGNGGP GTVKKITASH
GGHTSYVLHK IDAIDEASFE YNYSIVGGTG LDESLEKITF ESKLLSGPDG GSIGKIKVKF
HTKGDVLSDA VREEAKARGT GLFKAVEGYV LANPNY
