IED ID | IndEnz0002006412 |
Enzyme Type ID | protease006412 |
Protein Name |
Protease inhibitor HPI HbPI1 Protease inhibitor 1 |
Gene Name | PI1 |
Organism | Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Malpighiales Euphorbiaceae Crotonoideae Micrandreae Hevea Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis) |
Enzyme Sequence | MASQCPVKNSWPELVGTNGDIAAGIIQTENANVKAIVVKEGLPITQDLNFNRVRVFVDENRVVTQVPAIG |
Enzyme Length | 70 |
Uniprot Accession Number | Q6XNP7 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Inhibitor of serine proteases, strongly inhibits subtilisin A and weakly inhibits trypsin. Does not inhibit chymotrypsin, papain, pepsin, pronase E, protease type XIII and thermolysin. HPI-1 inhibits subtilisin A with an Ki of 0.21 nM. HPI-2a inhibits subtilisin A with an Ki of 0.08 nM. HPI-2b inhibits subtilisin A with an Ki of 0.1 nM. {ECO:0000269|PubMed:16438995}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Site (1) |
Keywords | Acetylation;Direct protein sequencing;Disulfide bond;Glutathionylation;Protease inhibitor;Serine protease inhibitor |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000269|PubMed:16438995; MOD_RES 5; /note=S-glutathionyl cysteine; alternate; /evidence=ECO:0000269|PubMed:16438995 |
Post Translational Modification | PTM: Occurs in 3 forms that differ in the modification of Cys-5, HPI-1 forms a homodimer through a disulfide bond, HPI-2a is modified by glutathionylation, and HPI-2b is covalently modified by addition of an unidentified adduct but not by a disulfide linkage. {ECO:0000269|PubMed:16438995}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 7,547 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |