| IED ID | IndEnz0002000428 |
| Enzyme Type ID | protease000428 |
| Protein Name |
Peptidase 1 EC 3.4.22.65 Allergen Der p I Major mite fecal allergen Der p 1 allergen Der p 1 |
| Gene Name | DERP1 |
| Organism | Dermatophagoides pteronyssinus (European house dust mite) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Arachnida Acari Acariformes Sarcoptiformes Astigmata Psoroptidia Analgoidea (feather mites) Pyroglyphidae (house-dust mites) Dermatophagoidinae Dermatophagoides Dermatophagoides pteronyssinus (European house dust mite) |
| Enzyme Sequence | MKIVLAIASLLALSAVYARPSSIKTFEEYKKAFNKSYATFEDEEAARKNFLESVKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVIL |
| Enzyme Length | 320 |
| Uniprot Accession Number | P08176 |
| Absorption | |
| Active Site | ACT_SITE 132; /evidence=ECO:0000250; ACT_SITE 268; /evidence=ECO:0000250; ACT_SITE 288; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.65; |
| DNA Binding | |
| EC Number | 3.4.22.65 |
| Enzyme Function | FUNCTION: Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (9); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (1); Helix (11); Mutagenesis (2); Natural variant (5); Propeptide (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Allergen;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites. {ECO:0000269|PubMed:16148130}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:16148130 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1XKG; 2AS8; 3RVW; 3RVX; 4PP1; 4PP2; 5VCN; 5VCO; 5VPH; |
| Mapped Pubmed ID | 16522455; 22210776; 26026055; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,104 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.65; |