nep-2 Neprilysin-2 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: nep-2
Official Full Name: Neprilysin-2
Primary source: WormBase:WBGene00020230
Locus tag: CELE_T05A8.4
See related: AllianceGenome:WB:WBGene00020230
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Caenorhabditis elegans (strain: Bristol N2)
Lineage: Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
Summary: Predicted to enable metalloendopeptidase activity. Involved in olfactory learning and regulation of chemotaxis. Located in cell surface. Is expressed in GLR; body wall musculature; muscle cell; and neurons. Human ortholog(s) of this gene implicated in Charcot-Marie-Tooth disease axonal type 2T; X-linked dominant hypophosphatemic rickets; cerebral amyloid angiopathy; membranous glomerulonephritis; and neurodegenerative disease (multiple). Orthologous to several human genes including MME (membrane metalloendopeptidase) and MMEL1 (membrane metalloendopeptidase like 1). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See nep-2 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 18

Sequence:: Chromosome: II; NC_003280.10 (2716555..2725752, complement)

Chromosome II - NC_003280.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003280.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

findings show a peptide, suppressor of NEP-2 (SNET-1), negatively regulates olfactory plasticity; its expression is down-regulated by the pheromone; NEP-2, a homolog of neprilysin, antagonizes SNET-1; this function is essential for olfactory plasticity
Title: Olfactory plasticity is regulated by pheromonal signaling in Caenorhabditis elegans.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

T05A8.4 (e-PCR)
- UniSTS:314888

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metallopeptidase activity	TAS Traceable Author Statement more info	PubMed
enables zinc ion binding	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in olfactory learning	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in regulation of chemotaxis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cell surface	IMP Inferred from Mutant Phenotype more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Neprilysin-2

NP_494343.2

Confirmed by transcript evidence

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_003280.10 Reference assembly

Range

2716555..2725752 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_061942.3 → NP_494343.2 Neprilysin-2 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_494343.2

Status: REVIEWED

UniProtKB/Swiss-Prot

O44857

Conserved Domains (2) summary

cd08662
Location:73 → 734

M13; Peptidase family M13 includes neprilysin, endothelin-converting enzyme I

COG3590
Location:61 → 736

PepO; Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones]