Ngly1 N-glycanase 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ngly1provided by MGI
Official Full Name: N-glycanase 1provided by MGI
Primary source: MGI:MGI:1913276
See related: Ensembl:ENSMUSG00000021785 AllianceGenome:MGI:1913276
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Png1; PNGase; 1110002C09Rik
Summary: Predicted to enable peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity. Involved in glycoprotein catabolic process. Located in cytoplasm. Is expressed in axial musculature; nervous system; thymus primordium; and vibrissa. Human ortholog(s) of this gene implicated in congenital disorder of deglycosylation 1. Orthologous to human NGLY1 (N-glycanase 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in testis adult (RPKM 30.1), adrenal adult (RPKM 10.0) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 14 A1; 14 7.08 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	14	NC_000080.7 (6157837..6220449, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	14	NC_000080.6 (16249314..16311926)

Chromosome 14 - NC_000080.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Comparative proteomics reveals elevated CCN2 in NGLY1-deficient cells.
Title: Comparative proteomics reveals elevated CCN2 in NGLY1-deficient cells.
Loss of peptide:N-glycanase causes proteasome dysfunction mediated by a sugar-recognizing ubiquitin ligase.
Title: Loss of peptide:N-glycanase causes proteasome dysfunction mediated by a sugar-recognizing ubiquitin ligase.
N-Glycanase 1 Transcriptionally Regulates Aquaporins Independent of Its Enzymatic Activity.
Title: N-Glycanase 1 Transcriptionally Regulates Aquaporins Independent of Its Enzymatic Activity.
findings reveal novel functions of the NGLY1-NRF1 (Nfe2l1) pathway in mitochondrial homeostasis and inflammation and uncover an unexpected therapeutic strategy using pharmacological activators of NRF2 for treating mitochondrial and immune dysregulation.
Title: N-glycanase NGLY1 regulates mitochondrial homeostasis and inflammation through NRF1.
These observations strongly suggest that the Ngly1- or Ngly1/Engase-deficient mice could serve as a valuable animal model for studies related to the pathogenesis of the NGLY1-deficiency, and that cytoplasmic ENGase represents one of the potential therapeutic targets for this genetic disorder.
Title: Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene.
study underscores the functional importance of Ngly1 in the ERAD process and provides a potential mechanism underlying the phenotypic consequences of a newly emerging genetic disorder caused by mutation of the human NGLY1 gene
Title: Endo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells.
cytoplasmic protein mouse p97(mp97) participates in the formation of a ternary complex containing mouse autocrine motility factor receptor (mAMFR), mp97, and peptide N-glycanase
Title: The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor.
enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins
Title: Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module.
The crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B is described; the results suggest a co-evolution of ER-associated degradation and DNA repair pathways.
Title: Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.
results suggested two possible pathways for the interaction between mPNGase and the proteasome; in one, mHR23B mediates the interaction between mPNGase and the proteasome; in an alternative pathway, mPNGase directly binds to the proteasome subunit, mS4
Title: Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (6) 1 citation
Targeted (6) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Ngly1 (e-PCR), detects polymorphism
- UniSTS:259333

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity	ISO Inferred from Sequence Orthology more info
enables peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in glycoprotein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycoprotein catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in glycoprotein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of BMP signaling pathway	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
located_in collagen-containing extracellular matrix	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info	PubMed

General protein information

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Preferred Names: peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Names: peptide N-glycanase homolog

NP_001349361.1

EC 3.5.1.52

NP_001349362.1

EC 3.5.1.52

NP_067479.2

EC 3.5.1.52

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001362432.1 → NP_001349361.1 peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase isoform 2

Status: VALIDATED

Source sequence(s)

AC173482, AK148931, BC028961

Conserved Domains (4) summary

pfam03835
Location:316 → 400

Rad4; Rad4 transglutaminase-like domain

pfam01841
Location:253 → 332

Transglut_core; Transglutaminase-like superfamily

pfam04721
Location:435 → 629

PAW; PNGase C-terminal domain, mannose-binding module PAW

cl15262
Location:26 → 90

PUB; PNGase/UBA or UBX (PUB) domain of p97 adaptor proteins
NM_001362433.1 → NP_001349362.1 peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase isoform 3

Status: VALIDATED

Source sequence(s)

AC173482, AK028248, AK169205, BC028961

Consensus CDS

CCDS88581.1

UniProtKB/TrEMBL

A0A286YCI0

Related

ENSMUSP00000152998.2, ENSMUST00000224656.2

Conserved Domains (4) summary

cd10459
Location:19 → 109

PUB_PNGase; PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase)

pfam03835
Location:335 → 420

Rad4; Rad4 transglutaminase-like domain

pfam01841
Location:272 → 351

Transglut_core; Transglutaminase-like superfamily

pfam04721
Location:413 → 593

PAW; PNGase C-terminal domain, mannose-binding module PAW
NM_021504.3 → NP_067479.2 peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase isoform 1

See identical proteins and their annotated locations for NP_067479.2

Status: VALIDATED

Source sequence(s)

AK028248

Consensus CDS

CCDS26832.1

UniProtKB/Swiss-Prot

Q8K113, Q9CTK3, Q9JI78

Related

ENSMUSP00000022310.7, ENSMUST00000022310.7

Conserved Domains (5) summary

cd10459
Location:19 → 109

PUB_PNGase; PNGase/UBA or UBX (PUB) domain of the P97 adaptor protein Peptide:N-glycanase (PNGase)

COG1305
Location:290 → 351

YebA; Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones]

pfam01841
Location:272 → 351

Transglut_core; Transglutaminase-like superfamily

pfam03835
Location:335 → 419

Rad4; Rad4 transglutaminase-like domain

pfam04721
Location:454 → 648

PAW; PNGase C-terminal domain, mannose-binding module PAW