Sequence Detail

ID/Version

Q9JLI3 Q9QZV7 Q9ERK3 Q9ERK2 Q3U495 Q9QZV6 (UniProt | EBI)

Last sequence update: 2000-10-01
Last annotation update: 2025-02-05

Sequence description from provider

RecName: Full=Membrane metallo-endopeptidase-like 1; EC=3.4.24.11;AltName: Full=NEP2(m);AltName: Full=Neprilysin II; Short=NEPII;AltName: Full=Neprilysin-2; Short=NEP2; Short=NL2;AltName: Full=Neprilysin-like 1; Sho

Provider

SWISS-PROT

Sequence

Polypeptide 765 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Mmel1	membrane metallo-endopeptidase-like 1	27	96	3	9

Sequence references in MGI

J:58258 Ikeda K, et al., Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides. J Biol Chem. 1999 Nov 5;274(45):32469-77
J:61898 Ghaddar G, et al., Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family. Biochem J. 2000 Apr 15;347(Pt 2):419-29
J:70325 Shirotani K, et al., Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J Biol Chem. 2001 Jun 15;276(24):21895-901
J:89881 Carpentier M, et al., Reduced fertility in male mice deficient in the zinc metallopeptidase NL1. Mol Cell Biol. 2004 May;24(10):4428-37
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563