| IED ID | IndEnz0002016767 |
| Enzyme Type ID | protease016767 |
| Protein Name |
Aminopeptidase N AP-N EC 3.4.11.2 Apn2 Microsomal aminopeptidase |
| Gene Name | APN2 |
| Organism | Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Sphingidae (hawkmoths) Sphinginae (small-eyed sphinx moth) Sphingini Manduca Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) |
| Enzyme Sequence | MYSLIFLALIGAAFGVPLSTNEDSTRNQNLAALYVLPQTSYPTFYDVRLFIDPGYTEAFHGNVSIRIIPNINIDQITIHAMAMRIDSIRVVSDVNPNEDLFSDFTLATDDTHLLTIRLTRNITALQPHVIHIDYVAQYADDMFGVYVSTYEENGRTVNLVTSQLQPTFARRAFPCYDEPALKAVFRTTIYAPAAYATVRSNTPERRDSLKPNEPGYVKHEFEDTLVMSTYLIAYLVSNFNYIENSQNPIYPIPFRVYSRPGTQNTAEFALEFGQQNMIALEEYTEFPYAFPKIDKAAVPDFAAGAMENWGLVIYREVALLVREGVTTTSVKQNIGRIICHENTHMWFGNEVGPMSWTYTWLNEGFANFFENYATDFVRPQWRMMDQFVIAMQNVFQSDAVLSVNPMTHPVYTPSQIIGTFNAVAYQKSGSVIRMLQHFMTPEIFRRGLVIYIKANSRAAAAPSDLYVALQQALDESSHRIPKPISTIMTEWSTQGGFPVLTVRRTAPNADSVFVAQERYLTDRSLTSTDRWHVPVNWVISSNVNFSDTSPQAWILPTFPATAVDVPGLSNADWYIFNKQQTGYYRVNYDVENWVALARVLNNSHEIIHVLNRAQIVDDAFNLARNGRLHYKNAFEISRYLEMEKDYIPWAAANPAFNYLDIVLSGANSYNLYRYYLLNLTAPMFEDLGFDVKSGEEFVTPYHRNIILDINCRFGNQRCISRAQEILQAFKNNPNQRPNPDIQTLVYCSSLRAGNVENFNFLWNMYLGTSDSSEQSILLSALGCTSNAERRNFYLNQIIDDNSAVREQDRHSIAVSVINSSPEGMNVALDFVVENFHRIQPRVQALTGTTNILNTFARRLTTSAHNEKIDELVRRHESIFSAGERASIAAIRENIAASIAWSNSNAGIVENWLKENYGPPSGAKSLTAGLLVLISLFVAIFNH |
| Enzyme Length | 942 |
| Uniprot Accession Number | P91885 |
| Absorption | |
| Active Site | ACT_SITE 341; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (5); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Cell membrane;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 106,780 |
| Kinetics | |
| Metal Binding | METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 363; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.2; |