OGA
Function
Isoform 1
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839, PubMed:37962578). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (PubMed:28939839, PubMed:37962578). Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).
Isoform 3
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.
Post-translational modifications
Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.
Sequence Similarities
Belongs to the glycosyl hydrolase 84 family.
Tissue Specificity
Ubiquitous. Shows highest expression in the brain, placenta and pancreas.
Cellular localization
- Isoform 3
- Nucleus
- Isoform 1
- Cytoplasm
Alternative names
HEXC, KIAA0679, MEA5, MGEA5, OGA, Protein O-GlcNAcase, Beta-N-acetylglucosaminidase, Beta-N-acetylhexosaminidase, Beta-hexosaminidase, Meningioma-expressed antigen 5, N-acetyl-beta-D-glucosaminidase, N-acetyl-beta-glucosaminidase, Nuclear cytoplasmic O-GlcNAcase and acetyltransferase, NCOAT