Protein O-GlcNAcase

OGA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2YDQ
Identifiers
Aliases	OGA, MEA5, NCOAT, meningioma expressed antigen 5 (hyaluronidase), MGEA5, O-GlcNAcase
External IDs	OMIM: 604039; MGI: 1932139; HomoloGene: 8154; GeneCards: OGA; OMA:OGA - orthologs
Gene location (Human)
Chr.	Chromosome 10 (human)
End	101,818,465 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	45,772,276 bp
RNA expression pattern
	Top expressed in
	sperm; ; skin of abdomen; ; skin of leg; ; cerebellar hemisphere; ; tibial nerve; ; right uterine tube; ; gastric mucosa; ; right hemisphere of cerebellum; ; left ovary; ; ventricular zone;
	Top expressed in
	saccule; ; otic placode; ; otic vesicle; ; fossa; ; vestibular membrane of cochlear duct; ; conjunctival fornix; ; epithelium of lens; ; motor neuron; ; ciliary body; ; vestibular sensory epithelium;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	hyalurononglucosaminidase activity; beta-N-acetylglucosaminidase activity; hydrolase activity; hydrolase activity, acting on glycosyl bonds; [protein-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity]; [protein-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity]; [protein-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity];
Cellular component	cytoplasm; cytosol; membrane; nucleus;
Biological process	metabolism; protein deglycosylation; N-acetylglucosamine metabolic process; glycoprotein catabolic process; protein O-linked glycosylation; glycoprotein metabolic process; viral process;
	Sources:Amigo / QuickGO
Orthologs
	10724
	76055
	ENSG00000198408
	ENSMUSG00000025220
	O60502
	Q9EQQ9
	NM_001142434; NM_012215
	NM_023799
	NP_001135906; NP_036347
	NP_076288
	Wikidata
View/Edit Human	View/Edit Mouse

Protein O-GlcNAcase (EC 3.2.1.169, OGA, glycoside hydrolase O-GlcNAcase, O-GlcNAcase, BtGH84, O-GlcNAc hydrolase) is an enzyme with systematic name (protein)-3-O-(N-acetyl-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase.^[5]^[6]^[7]^[8]^[9] OGA is encoded by the OGA gene. This enzyme catalyses the removal of the O-GlcNAc post-translational modification in the following chemical reaction:

[protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H₂O ⇌ [protein]-L-serine + N-acetyl-D-glucosamine
[protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine + H₂O ⇌ [protein]-L-threonine + N-acetyl-D-glucosamine

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000198408 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025220 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Wells L, Gao Y, Mahoney JA, Vosseller K, Chen C, Rosen A, Hart GW (January 2002). "Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase". The Journal of Biological Chemistry. 277 (3): 1755–61. doi:10.1074/jbc.M109656200. PMID 11788610.
^ Cetinbaş N, Macauley MS, Stubbs KA, Drapala R, Vocadlo DJ (March 2006). "Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants". Biochemistry. 45 (11): 3835–44. doi:10.1021/bi052370b. PMID 16533067.
^ Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, et al. (April 2006). "Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity". Nature Structural & Molecular Biology. 13 (4): 365–71. doi:10.1038/nsmb1079. PMID 16565725. S2CID 9239755.
^ Kim EJ, Kang DO, Love DC, Hanover JA (June 2006). "Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate". Carbohydrate Research. 341 (8): 971–82. doi:10.1016/j.carres.2006.03.004. PMC 10561171. PMID 16584714.
^ Dong DL, Hart GW (July 1994). "Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol". The Journal of Biological Chemistry. 269 (30): 19321–30. doi:10.1016/S0021-9258(17)32170-1. PMID 8034696.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000198408 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025220 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Wells L, Gao Y, Mahoney JA, Vosseller K, Chen C, Rosen A, Hart GW (January 2002). "Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase". The Journal of Biological Chemistry. 277 (3): 1755–61. doi:10.1074/jbc.M109656200. PMID 11788610.

[6] Cetinbaş N, Macauley MS, Stubbs KA, Drapala R, Vocadlo DJ (March 2006). "Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants". Biochemistry. 45 (11): 3835–44. doi:10.1021/bi052370b. PMID 16533067.

[7] Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, et al. (April 2006). "Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity". Nature Structural & Molecular Biology. 13 (4): 365–71. doi:10.1038/nsmb1079. PMID 16565725. S2CID 9239755.

[8] Kim EJ, Kang DO, Love DC, Hanover JA (June 2006). "Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate". Carbohydrate Research. 341 (8): 971–82. doi:10.1016/j.carres.2006.03.004. PMC 10561171. PMID 16584714.

[9] Dong DL, Hart GW (July 1994). "Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol". The Journal of Biological Chemistry. 269 (30): 19321–30. doi:10.1016/S0021-9258(17)32170-1. PMID 8034696.

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