| IED ID | IndEnz0002015834 |
| Enzyme Type ID | protease015834 |
| Protein Name |
Neprilysin-2 EC 3.4.24.11 Cleaved into: Neprilysin-2, soluble form |
| Gene Name | Nep2 CG9761 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW |
| Enzyme Length | 774 |
| Uniprot Accession Number | A0A0B4K692 |
| Absorption | |
| Active Site | ACT_SITE 610; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 675; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}; |
| DNA Binding | |
| EC Number | 3.4.24.11 |
| Enzyme Function | FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues (PubMed:15554877, PubMed:17157960). Functions in female fertility, embryogenesis and memory formation (PubMed:24395329, PubMed:27629706). Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates (PubMed:24395329). Also required for normal patterns of hatching due to its important role in early embryonic development (PubMed:24395329). Required in the dorsal paired medial neurons for the proper formation of middle-term memory (PubMed:27629706). Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation (PubMed:27629706). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000269|PubMed:24395329, ECO:0000269|PubMed:27629706}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5 at 35 degrees Celsius. {ECO:0000269|PubMed:17157960}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (2); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (8); Metal binding (3); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is probably produced by proteolytic cleavage (Probable). In embryos, adult Malpighian tubules and testes, detected in the soluble fraction but is not detected in the membrane fraction (PubMed:15554877, PubMed:17157960). {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960, ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:17157960}.; PTM: The soluble form is probably produced by proteolytic cleavage. {ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10961941; 11223883; 15234342; 15525709; 18215274; 18245849; 18463098; 19038301; 19317464; 20220848; 20371351; 20813047; 21684629; 23071443; 23087838; 23827522; 25294944; 25312911; 25838129; 27717375; 28008309; 28090760; 28213160; 28610887; 28633019; 31247332; 31722958; 32045897; 33049996; 34189422; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,125 |
| Kinetics | |
| Metal Binding | METAL 609; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 613; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 671; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B14; |