| IED ID | IndEnz0002019029 |
| Enzyme Type ID | protease019029 |
| Protein Name |
Probable aspartic proteinase GIP2 EC 3.4.23.- Glucanase inhibitor protein 2 NbGIP2 |
| Gene Name | GIP2 Niben101Scf03191g04002 |
| Organism | Nicotiana benthamiana |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Nicotianoideae Nicotianeae Nicotiana Nicotiana benthamiana |
| Enzyme Sequence | MASSCCLHAILLCSLLFITSTTAQSETSFRPKGLILPITKDALTLQYLTQIQQRTPLVPVSLTLDLGGQFLWVDCDQGYVSSTYRPARCRSAQCSLAGAGSGCGQCFSPPKPGCNNNTCGLLPDNTITRTATSGELASDTVQVQSSNGKNPGRHVSDKDFLFVCGSTFLLEGLASGVKGMAGLGRTRISLPSQFSAEFSFPRKFAVCLSSSTNSKGVVLFGDGPYTFLPNREFANNDFSYTPLFINPVSTASAFSSREPSSEYFIGVKSIKINEKVVPINTTLLSIDNQGVGGTKISTVNPYTILETSIYNAVTNFFVKELVNITRVASVAPFRACFDSRNIASTRVGPAVPSIDLVLQNENVFWRIFGANSMVQVSENVLCLGFVDGGVSPRTSIVVGGYTIEDNLLQFDLARSRLGFTSSILFRQTTCANFNFTSIA |
| Enzyme Length | 439 |
| Uniprot Accession Number | P0DO21 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Involved in plant defense against Phytophtora parasitica (PubMed:28082413). Contributes positively to Nicotiana resistance against P.parasitica (PubMed:28082413). Binds the P.parasitica xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.parasitica virulence factor (PubMed:28082413). XEG1 acts as an important virulence factor during P.parasitica infection but also acts as a pathogen-associated molecular pattern (PAMP) in Nictotiana species, where it can trigger defense responses including cell death (PubMed:28082413). {ECO:0000269|PubMed:28082413}.; FUNCTION: (Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.parasitica XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.parasitica xyloglucanase XEG1 when hijacked by XLP1 binding. {ECO:0000269|PubMed:28082413}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Glycosylation (4); Signal peptide (1) |
| Keywords | Apoplast;Aspartyl protease;Glycoprotein;Hydrolase;Plant defense;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:28082413}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,214 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |