| IED ID | IndEnz0002002777 |
| Enzyme Type ID | protease002777 |
| Protein Name |
Aminopeptidase N AP-N EC 3.4.11.2 Apn1 Microsomal aminopeptidase |
| Gene Name | APN1 |
| Organism | Plutella xylostella (Diamondback moth) (Plutella maculipennis) |
| 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 Yponomeutoidea Plutellidae (diamondback moths) Plutella Plutella xylostella (Diamondback moth) (Plutella maculipennis) |
| Enzyme Sequence | MRLLICLTLLGLVCGNPVQLTDNSIALQNTYDNYVLPGESFPTFYDVQLFFDPEYEASFNGTVAIRVVPRIATQEIVLHAMEMEILSIRAYSDLPSDDNLNENLFSSYTLATDDTHLLKIQFTRVLDALQPITVEISYSAQYAPNMFGVYVSRYVENGATVSLVTSQLQPTFARRAFPCYDEPALKAVFRTTIYAPPAYNVVETNMPLRTDSLKSDRPGFTKHEFQDTLVMSSYLLAYLVSKFDYISNENNPTYDKSMKVFSRPGTQNTAEFALDFGQKNMVELEKYTEFPYAFPKIDKVAVPDFAAGAMENWGLVIYREIALLVQEGVTTTSTLQGIGRIISHENTHQWFGNEVGPDSWTYTWLNEGFANFFESFATDLVLPEWRMMDQFVINMQNVFQSDAVLSVNPITFEVRTPSQILGTFNSVAYQKSGSVIRMMQHFLTPEIFRKSLALYISRMSRKAAKPTDLFEAIQEVVDASDHSIRWRLSIIMNRWTQQGGFPVVTVRRSAPSAQSFVITQRRFLTDSTQESNTVWNVPLNWVLSTDVNFNDTRPMAWLPPQLAAEAVQVPGLQNAEWFIVNKQQTGYYRVNYDPENWRALAKVLNDTHEIIHLLNRAQLIDDSFNLARNGRLDYSLAFDLSRYLVQERDYIPWAAANAAFNYLNSVLSGSSVHPLFQEYLLFLTAPLYQRLGFNAATGEEHVTPFHRNIILNINCLHGNEDCVSTAETLLQNFRDNPTQTLNPDIQTTVFCSGLRGGDVDNFNFLWARYTATQDSSEQSILLNALGCTSNADRRDFLFSQVIASDSQVREQDRHSVLVSAINSGPDNMNAALDFVLENFANIQPNVQGLTGTTNILNAFARTLTTQEHANKIDEFSNKYANVFTAGEMASVAAIKENIAASITWNSQNAATVEAWLRKNFGTDGASTVSASITIIISAMVAIYNIL |
| Enzyme Length | 946 |
| Uniprot Accession Number | P91887 |
| Absorption | |
| Active Site | ACT_SITE 345; /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 (3); Metal binding (3); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Aminopeptidase;Cell membrane;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 | 106,578 |
| Kinetics | |
| Metal Binding | METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 367; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.2; |