Detail Information for IndEnz0002007667
IED ID IndEnz0002007667
Enzyme Type ID protease007667
Protein Name Peptidyl-prolyl cis-trans isomerase CYP18-3
PPIase CYP18-3
EC 5.2.1.8
Cyclophilin of 18 kDa 3
Cyclosporin A-binding protein
Rotamase cyclophilin-1
Gene Name CYP18-3 ROC1 At4g38740 T9A14.20
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MAFPKVYFDMTIDGQPAGRIVMELYTDKTPRTAENFRALCTGEKGVGGTGKPLHFKGSKFHRVIPNFMCQGGDFTAGNGTGGESIYGSKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKVGSSSGKPTKPVVVADCGQLS
Enzyme Length 172
Uniprot Accession Number P34790
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
DNA Binding
EC Number 5.2.1.8
Enzyme Function FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in de-etiolation. Reduces the sensitivity to brassinosteroids by decreasing somehow the abundance of the partially dephosphorylated form of BES1. Triggers the activation of bacterial AvrRpt2 protease activity upon infection by P.syringae. Activated AvrRpt2 confers virulence in plant lacking the RPS2 resistance gene. In plants expressing RPS2, the AvrRpt2-mediated degradation of RIN4 activates RPS2, which induces hypersensitive response (HR) and plant resistance. {ECO:0000269|PubMed:15746386, ECO:0000269|PubMed:16968222, ECO:0000269|PubMed:20050698, ECO:0000269|PubMed:22463079}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Mutagenesis (3)
Keywords Chaperone;Cytoplasm;Hypersensitive response;Isomerase;Plant defense;Reference proteome;Rotamase
Interact With
Induction INDUCTION: Up-regulated by light, salt and wounding. Down-regulated by cytokinin treatment. {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:22463079, ECO:0000269|PubMed:9426607}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12225588; 14551330; 15047896; 15159628; 15632145; 15769804; 16242667; 16247729; 16284313; 16336779; 16502469; 16552445; 17028149; 17320239; 17339215; 17644812; 17705842; 18538804; 18650403; 18775970; 20405473; 20706207; 21798377; 23206262; 24064926; 24089553; 25299333; 28627464; 32388423;
Motif
Gene Encoded By
Mass 18,373
Kinetics
Metal Binding
Rhea ID RHEA:16237
Cross Reference Brenda 5.2.1.8;