| IED ID | IndEnz0002012280 |
| Enzyme Type ID | protease012280 |
| Protein Name |
Xaa-Pro aminopeptidase 2 EC 3.4.11.9 Aminoacylproline aminopeptidase Membrane-bound aminopeptidase P Membrane-bound APP Membrane-bound AmP mAmP X-Pro aminopeptidase 2 |
| Gene Name | XPNPEP2 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MAQACWGCYPWLVLICACAWGHPKSLNQREDVRNCSTSPPYLPVTAVNTTAQLTALREQMLTQNLSAYIIPDTDAHMSEYIGECDQRRAWITGFIGSAGIAVVTERKAALWTDSRYWTQAERQMDCNWELHKEVSTGHIVTWLLTEIPVGGRVGFDPFLFSIDSWESYDVALQDADRELVSITVNLVDLVWGSERPPLPNAPIYALQEAFAGSTWQEKVSNIRSQMQKHHERPTAVLLSALDETAWLFNLRSSDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLQYLNSSCNSSMCVQLEDYSQIRDSIQAYTSGDVKIWIGTRYTSYGLYEVIPKEKLVEDDYSPVMITKAVKNSREQALLKASHVRDAVAVIRYLAWLEKNVPTGTVDEFSGAKRVEEFRGEEEFFSGPSFETISASGLNAALAHYSPTKELHRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLVFPAATSGRVVEAFARKALWDVGLNYGHGTGHGIGNFLCVHEWPVGFQYGNIPMAEGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKYPGTYLTFEVVSLVPYDRKLIDVSLLSPEQLQYLNRYYQAIREKVGPELQRRGLLEELSWLQRHTEPLSARAAPTTSLGSLMTVSALAILGWSV |
| Enzyme Length | 673 |
| Uniprot Accession Number | Q95333 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by apstatin and the metal ion chelator EDTA (PubMed:8870669). Potently inhibited by the converting enzyme inhibitors cilazaprilat; enalaprilat; L155,212; ramiprilat and YS 980 (PubMed:1312513). Also inhibited to a lesser extent by indolaprilat; quinaprilat; spiraprilat; captopril and zofenoprilat (PubMed:1312513). {ECO:0000269|PubMed:1312513, ECO:0000269|PubMed:8870669}. |
| Binding Site | BINDING 115; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 429; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 523; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 532; /note=Substrate; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; BINDING 554; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O44750 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:1312513, ECO:0000269|PubMed:7744038, ECO:0000269|PubMed:8870669}; |
| DNA Binding | |
| EC Number | 3.4.11.9 |
| Enzyme Function | FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. {ECO:0000269|PubMed:1312513, ECO:0000269|PubMed:7744038, ECO:0000269|PubMed:8870669}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (5); Chain (1); Glycosylation (6); Lipidation (1); Metal binding (8); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Cell membrane;Direct protein sequencing;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:7744038, ECO:0000305|PubMed:8870669}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:7744038, ECO:0000269|PubMed:8870669}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:7744038}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 75,756 |
| Kinetics | |
| Metal Binding | METAL 449; /note=Manganese 2; /evidence=ECO:0000250; METAL 449; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 460; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 460; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750; METAL 523; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:O44750; METAL 554; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750; METAL 568; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:O44750; METAL 568; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:O44750 |
| Rhea ID | |
| Cross Reference Brenda |