位置:首页 > 蛋白库 > RNLE_SOLLC
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024