| IED ID | IndEnz0002016714 |
| Enzyme Type ID | protease016714 |
| Protein Name |
Glutamyl aminopeptidase EAP EC 3.4.11.7 Aminopeptidase A AP-A Differentiation antigen gp160 CD antigen CD249 |
| Gene Name | ENPEP |
| Organism | Homo sapiens (Human) |
| 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 Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG |
| Enzyme Length | 957 |
| Uniprot Accession Number | Q07075 |
| Absorption | |
| Active Site | ACT_SITE 394; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXD" |
| Activity Regulation | ACTIVITY REGULATION: Substrate specificity is modulated by calcium which enhances the enzymatic activity for cleavage of acidic residues while reducing its activity with basic residues. Inhibited by aminopeptidase inhibitors amastatin and bestatin. {ECO:0000269|PubMed:10692253, ECO:0000269|PubMed:23888046}. |
| Binding Site | BINDING 223; /note="Substrate"; /evidence="ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB"; BINDING 887; /note="Substrate"; /evidence="ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.; EC=3.4.11.7; Evidence={ECO:0000269|PubMed:10692253, ECO:0000269|PubMed:23888046}; |
| DNA Binding | |
| EC Number | 3.4.11.7 |
| Enzyme Function | FUNCTION: Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. {ECO:0000305|PubMed:23888046}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (29); Binding site (2); Chain (1); Compositional bias (1); Glycosylation (14); Helix (43); Metal binding (3); Mutagenesis (2); Natural variant (5); Region (2); Site (2); Topological domain (2); Transmembrane (1); Turn (9) |
| Keywords | 3D-structure;Aminopeptidase;Calcium;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10692253}; Single-pass type II membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 4KX7; 4KX8; 4KX9; 4KXA; 4KXB; 4KXC; 4KXD; |
| Mapped Pubmed ID | 16790432; 17603472; 17850355; 17990103; 17999179; 18188697; 18206321; 18410507; 18550936; 18677709; 19187443; 19373777; 20332099; 20379614; 20711500; 21697726; 24098452; 24885240; 26311161; 28177885; 33421813; 8804068; 9062131; |
| Motif | |
| Gene Encoded By | |
| Mass | 109,244 |
| Kinetics | |
| Metal Binding | METAL 393; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"; METAL 397; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD"; METAL 416; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.7; |