RNLE_SOLLC
ID RNLE_SOLLC Reviewed; 230 AA.
AC P80022; P80801;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Extracellular ribonuclease LE;
DE Short=RNase LE;
DE EC=4.6.1.19;
DE Flags: Precursor;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-74 AND 221-230.
RC STRAIN=cv. Lukullus; TISSUE=Hypocotyl;
RX PubMed=7894013; DOI=10.1007/bf00019315;
RA Koeck M., Loeffler A., Abel S., Glund K.;
RT "cDNA structure and regulatory properties of a family of starvation-induced
RT ribonucleases from tomato.";
RL Plant Mol. Biol. 27:477-485(1995).
RN [2]
RP PROTEIN SEQUENCE OF 26-230.
RC STRAIN=cv. Lukullus;
RX PubMed=2040270; DOI=10.1111/j.1432-1033.1991.tb15978.x;
RA Jost W., Bak M., Glund K., Terpstra P., Beintema J.J.;
RT "Amino acid sequence of an extracellular, phosphate-starvation-induced
RT ribonuclease from cultured tomato (Lycopersicon esculentum) cells.";
RL Eur. J. Biochem. 198:1-6(1991).
RN [3]
RP PROTEIN SEQUENCE OF 26-48, AND SUBCELLULAR LOCATION.
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=10801354; DOI=10.1006/jmbi.2000.3707;
RA Tanaka N., Arai J., Inokuchi N., Koyama T., Ohgi K., Irie M.,
RA Nakamura K.T.;
RT "Crystal structure of a plant ribonuclease, RNase LE.";
RL J. Mol. Biol. 298:859-873(2000).
CC -!- FUNCTION: Probably involved in plant phosphate-starvation rescue
CC system.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:9188482}. Secreted, cell wall
CC {ECO:0000269|PubMed:9188482}.
CC -!- INDUCTION: By phosphate starvation.
CC -!- SIMILARITY: Belongs to the RNase T2 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; X79337; CAA55895.1; -; mRNA.
DR PIR; S53506; S53506.
DR RefSeq; NP_001234195.1; NM_001247266.2.
DR PDB; 1DIX; X-ray; 1.65 A; A=27-230.
DR PDBsum; 1DIX; -.
DR AlphaFoldDB; P80022; -.
DR SMR; P80022; -.
DR STRING; 4081.Solyc05g007950.2.1; -.
DR PaxDb; P80022; -.
DR PRIDE; P80022; -.
DR EnsemblPlants; Solyc05g007950.3.1; Solyc05g007950.3.1; Solyc05g007950.3.
DR GeneID; 544098; -.
DR Gramene; Solyc05g007950.3.1; Solyc05g007950.3.1; Solyc05g007950.3.
DR KEGG; sly:544098; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_069912_2_1_1; -.
DR InParanoid; P80022; -.
DR OMA; DMRRYWP; -.
DR OrthoDB; 994722at2759; -.
DR PhylomeDB; P80022; -.
DR BRENDA; 4.6.1.19; 3101.
DR EvolutionaryTrace; P80022; -.
DR Proteomes; UP000004994; Chromosome 5.
DR ExpressionAtlas; P80022; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Disulfide bond;
KW Endonuclease; Hydrolase; Lyase; Nuclease; Reference proteome; Secreted;
KW Signal; Stress response.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2040270,
FT ECO:0000269|PubMed:7894013, ECO:0000269|PubMed:9188482"
FT CHAIN 26..230
FT /note="Extracellular ribonuclease LE"
FT /id="PRO_0000030969"
FT ACT_SITE 64
FT ACT_SITE 118
FT ACT_SITE 122
FT DISULFID 43..49
FT DISULFID 50..106
FT DISULFID 79..125
FT DISULFID 186..221
FT DISULFID 202..213
FT CONFLICT 41
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="C -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="T -> TP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1DIX"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1DIX"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1DIX"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1DIX"
SQ SEQUENCE 230 AA; 25331 MW; A18CA6A2E720BEDF CRC64;
MASNSAFSLF LILLIITQCL SVLNAAKDFD FFYFVQQWPG SYCDTKQSCC YPTTGKPAAD
FGIHGLWPNN NDGTYPSNCD PNSPYDQSQI SDLISSMQQN WPTLACPSGS GSTFWSHEWE
KHGTCAESVL TNQHAYFKKA LDLKNQIDLL SILQGADIHP DGESYDLVNI RNAIKSAIGY
TPWIQCNVDQ SGNSQLYQVY ICVDGSGSSL IECPIFPGGK CGTSIEFPTF