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; |