nrf-5 Nose resistant to fluoxetine protein 5 [Caenorhabditis elegans] - Gene

Summary

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Official Symbol: nrf-5
Official Full Name: Nose resistant to fluoxetine protein 5
Primary source: WormBase:WBGene00003812
Locus tag: CELE_F55B12.5
See related: AllianceGenome:WB:WBGene00003812
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: Enables phosphatidylserine binding activity. Involved in lipid transport and positive regulation of engulfment of apoptotic cell. Located in extracellular region. Is expressed in apoptotic cell; body wall musculature; intestine; and pharyngeal cell. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See nrf-5 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 9

Sequence:: Chromosome: V; NC_003283.11 (13828267..13830907)

Chromosome V - NC_003283.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_003283.11

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The results reveal the existence of a WLDS/Nmnat-independent axonal degeneration pathway in C. elegans, conservation of the axonal clearance machinery, and a function for CED-7 and NRF-5 in this process.
Title: The Apoptotic Engulfment Machinery Regulates Axonal Degeneration in C. elegans Neurons.
The data suggest that NRF-5 may act with CED-7 and TTR-52 to mediate phosphatidylserine transfer from apoptotic cells to engulfing cells and thus promotes engulfment by phagocytes.
Title: C. elegans secreted lipid-binding protein NRF-5 mediates PS appearance on phagocytes for cell corpse engulfment.
Nrf-5 is expressed in the intestine and is likely secreted into the pseudocoelomic fluid, where it could function to transport fluoxetine.
Title: Fluoxetine-resistance genes in Caenorhabditis elegans function in the intestine and may act in drug transport.

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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

F55B12.5 (e-PCR)
- UniSTS:311820

Homology

Orthologs from OrthoDB

Gene Ontology Provided by WormBase

Function	Evidence Code	Pubs
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables phosphatidylserine binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in lipid transport	IDA Inferred from Direct Assay more info	PubMed
involved_in lipid transport	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of engulfment of apoptotic cell	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular region	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: Nose resistant to fluoxetine protein 5

NP_506424.2

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_003283.11 Reference assembly

Range

13828267..13830907

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_074023.9 → NP_506424.2 Nose resistant to fluoxetine protein 5 [Caenorhabditis elegans]

See identical proteins and their annotated locations for NP_506424.2

Status: REVIEWED

UniProtKB/Swiss-Prot

Q6RV00, Q6RV01, Q93796

Conserved Domains (2) summary

smart00328
Location:36 → 278

BPI1; BPI/LBP/CETP N-terminal domain

cl00188
Location:322 → 518

BPI; BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative ...