Detail Information for IndEnz0002007270
IED ID IndEnz0002007270
Enzyme Type ID protease007270
Protein Name Neprilysin
EC 3.4.24.11
Atriopeptidase
Enkephalinase
Neutral endopeptidase 24.11
NEP
Neutral endopeptidase
Skin fibroblast elastase
SFE
CD antigen CD10
Gene Name MME
Organism Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGEPLLKLLPDVYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYKKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
Enzyme Length 750
Uniprot Accession Number Q5RE69
Absorption
Active Site ACT_SITE 585; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 651; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
Activity Regulation
Binding Site BINDING 103; /note=Substrate carboxyl; /evidence=ECO:0000250
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:0000250|UniProtKB:P08473};
DNA Binding
EC Number 3.4.24.11
Enzyme Function FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. {ECO:0000250|UniProtKB:P08473}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (1); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (6); Initiator methionine (1); Lipidation (1); Metal binding (3); Modified residue (2); Motif (1); Region (1); Sequence conflict (5); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Myristate;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Modified Residue MOD_RES 4; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P08473; MOD_RES 6; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P08473
Post Translational Modification PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000250}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 16..23; /note=Stop-transfer sequence; /evidence=ECO:0000255
Gene Encoded By
Mass 85,514
Kinetics
Metal Binding METAL 584; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 588; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 647; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
Rhea ID
Cross Reference Brenda