PNG1/YPL096W Summary Help

Standard Name PNG1 1
Systematic Name YPL096W
Feature Type ORF, Verified
Description Conserved peptide N-glycanase; required for deglycosylation of misfolded glycoproteins during proteasome-dependent degradation; localizes to the cytoplasm and nucleus; activity is enhanced by interaction with Rad23p (1, 2, 3 and see Summary Paragraph)
Name Description Peptide N-Glycanase 1
Chromosomal Location
ChrXVI:366927 to 368018 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All PNG1 GO evidence and references
  View Computational GO annotations for PNG1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 2 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
Resources
34 total interaction(s) for 19 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 5
  • Co-crystal Structure: 1
  • Co-purification: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 4
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 7
  • Positive Genetic: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 363
Molecular Weight (Da) 42,485
Isoelectric Point (pI) 6.6
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:366927 to 368018 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1092 366927..368018 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006017
SUMMARY PARAGRAPH for PNG1

PNG1 encodes a soluble peptide:N-glycanase (PNGase), which catalyzes the deglycosylation of N-glycosylated proteins (1, 4). Misfolded secretory proteins and ER membrane proteins are exported from the ER to the cytosol, where they are deglycosylated by PNGase and then degraded by the proteasome, a process known as the ER quality control system (reviewed in references 5, 6, 7, and 8). Defects in ER quality control are associated with several human diseases, including cystic fibrosis, neurodegenerative diseases, and some viral infections (5).

Cells lacking Png1p are viable, and have no apparent growth defect, but have no detectable PNGase activity (1). In png1 null mutant cells, an abnormal form of carboxypeptidase Y (Prc1p) is degraded more slowly than in wild type cells (1). Png1p is found in both the cytosol and the nucleus (1). PNGase activity increases during stationary phase (4).

Proteins similar to Png1p are found in many eukaryotes, including S. pombe, C. elegans, D. melanogaster, mouse, and human (1).

Last updated: 2000-06-08 Contact SGD

References cited on this page View Complete Literature Guide for PNG1
1) Suzuki T, et al.  (2000) PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. J Cell Biol 149(5):1039-52
2) Biswas S, et al.  (2004) The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23. Biochem Biophys Res Commun 323(1):149-55
3) Wang S, et al.  (2009) N-terminal deletion of Peptide:N-glycanase results in enhanced deglycosylation activity. PLoS One 4(12):e8335
4) Suzuki T, et al.  (1998) Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J Biol Chem 273(34):21526-30
5) Plemper RK and Wolf DH  (1999) Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem Sci 24(7):266-70
6) Plemper RK and Wolf DH  (1999) Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome. Mol Biol Rep 26(1-2):125-30
7) Romisch K  (1999) Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci 112 ( Pt 23)():4185-91
8) Suzuki T, et al.  (1998) Complex, two-way traffic of molecules across the membrane of the endoplasmic reticulum. J Biol Chem 273(17):10083-6