| IED ID | IndEnz0002014188 |
| Enzyme Type ID | protease014188 |
| Protein Name |
Glutamyl aminopeptidase EAP EC 3.4.11.7 Aminopeptidase A AP-A CD antigen CD249 |
| Gene Name | Enpep |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MNFAEEEPSKKYCIKGKHVAIICATVVAVGLIVGLSVGLTRSCEPGTTPAPSNPPPHTSTALPPQDQNVCPDSDDESGEWKNFRLPDFIQPVHYDLEVKVLMEEDRYTGIVSISVNLSKDTRDLWLHIRETRITKLPELRRPSGEQVPIRRCFEYKKQEYVVIQAEEDLAATSGDSVYRLTIEFEGWLNGSLVGFYRTTYTEDGQTKSIAATDHEPTDARKSFPCFDEPNKKATYNISLIHPKEYSALSNMPVEKKETLDNDWKKTTFMKSVPMSTYLVCFAVHQFTSIQRTSRSGKPLTVYVQPNQKQTAEYAANITKAVFDFFEDYFAMEYSLPKLDKIAIPDFGTGAMENWGLVTYRETNLLYDPLLSASSNQQRVASVVAHELVHQWFGNIVTMDWWDDLWLNEGFASFFEFLGVNHAEADWQMLSQVLLEDVLPVQEDDSLMSSHPVVVTVSTPAEITSVFDGISYSKGASILRMLQDWITPEKFQKGCQIYLENFKFKNAKTSDFWDSLEKASNQPVKEVMDTWTSQMGYPVVTVSGKQNVTQKRFLLDYKADPSQPPSALGYTWNIPIKWTENGNSNITVYYRSNREGITLNANLSGDGFLKINPDHIGFYRVNYEAETWDWIAETLSSNHMNFSSADRSSFIDDAFALARAQLLDYEKALNLTRYLTSEKDFLPWERVISAVSYIISMFEDDRELYPLIETYFRSQVKPIADSLGWQDTGSHITKLLRASVLGFACKMGAGEALGNASQLFEAWLKGNESIPVNLRLLVYRYGMQNSGNEAAWNYTLEQYQKTSLAQEKEKLLYGLASVKDVTLLARYLEMLKDPNIIKTQDVFTVIRYISYNSYGKSMAWNWIQLNWDYLVNRFTINDRYLGRIVTIAEPFNTELQLWQMQSFFAKYPNAGAGAKPREQVLETVKNNIEWLKLNRKSISEWFTSMP |
| Enzyme Length | 945 |
| Uniprot Accession Number | P50123 |
| Absorption | |
| Active Site | ACT_SITE 386; /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 215; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q07075; BINDING 878; /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); Alternative sequence (2); Binding site (2); Chain (1); Glycosylation (12); Metal binding (3); Region (2); Sequence conflict (5); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;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:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12110004; 16537183; 17519555; 22206666; 25960007; 33161775; |
| Motif | |
| Gene Encoded By | |
| Mass | 107,995 |
| Kinetics | |
| Metal Binding | METAL 385; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 389; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 408; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.7; |