Detail Information for IndEnz0002006412
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