| IED ID | IndEnz0002014185 |
| Enzyme Type ID | protease014185 |
| Protein Name |
Glutamyl aminopeptidase EAP EC 3.4.11.7 Aminopeptidase A AP-A CD antigen CD249 |
| Gene Name | ENPEP |
| Organism | Bos taurus (Bovine) |
| 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 Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MILEERSSWEGSKRYCIKTKHVAIICAVVVAVGLIVGLSVGLTRSCDSTEGMTQGTTQGTTQAPSHLPPVTSPPEDQGVCPASEDESGGWKDFRLPDFIKPVHYDLEVKPLMEQDTYTGSVDISINVSSSTRYLWLHLRETRITRLPVLRRPSGEQVQVRQCFEYKKQEYVVVEAEEELEPNTGEGPYHLILEFAGWLNGSLVGFYRTTYVEKGQTKSIAATDHEPTDARKSFPCFDEPNKKATYTISIVHSKEYKALSNMPVEKEESVDDIWSRTTFQKSVPMSTYLVCFAVHQFDSVTRISNRGIPLTIYVQPEQKHTAEYAANITKSVFDYFEDYFGMSYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPDESASSNKQRVAAVIAHELVHQWFGNIVTMEWWDDLWLNEGFASFFEYLGVAYAEKDWQMRDQMILDDVLPVQEDDSLMSSHPIVVTVATPDEITSVFDGISYSKGASILRMLENWITREKFQIGCQNYLKKHKFENAKTSDFWAALEEASNLPVKEVMDTWTNQMGYPVLNVDNMKNITQKRFLLDPRANASEPHSAFGYTWNIPIKWTEDDEQRITLYNRSETGGITLESTLSGNAFLKINPDHIGFYRVNYEVSTWEWIATNLSVNHTDFSSADRASFIDDAFALARAQLLNYKEALNLTKYLKEEKEYLPWHRVISAVTYIISMFEDDKELYPVIEKYFRDQVKPIADSLGWNDVGDHLTKLLRASVLGLACKMGDSDALNNASQLFQEWLTGTVSLPVNLRLLVYRYGMQNSGNETSWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDSNLIKTQDVFTVIQYISYNSYGKTMAWNWIQLNWEYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQIKSFFERYPEAGAGQKPREQVLETVKNNIEWLKQNRDTIRNWFLDLNG |
| Enzyme Length | 956 |
| Uniprot Accession Number | Q32LQ0 |
| Absorption | |
| Active Site | ACT_SITE 396; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| 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:0000250|UniProtKB:Q07075}. |
| Binding Site | BINDING 225; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q07075; BINDING 888; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q07075 |
| 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:0000250|UniProtKB:Q07075}; |
| 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:0000250|UniProtKB:Q07075}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Compositional bias (1); Glycosylation (13); Metal binding (3); Region (2); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Calcium;Cell membrane;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:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 109,801 |
| Kinetics | |
| Metal Binding | METAL 395; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 399; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 418; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |