Q9EQQ9 · OGA_MOUSE
- ProteinProtein O-GlcNAcase
- GeneOga
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids916 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:16517082).
Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (By similarity).
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:16517082).
Does not bind acetyl-CoA and does not have histone acetyltransferase activity (By similarity).
Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (By similarity).
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:16517082).
Does not bind acetyl-CoA and does not have histone acetyltransferase activity (By similarity).
Catalytic activity
- 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.49 mM | pNP-GlcNAc |
pH Dependence
Optimum pH is 6.5-7.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 67 | a protein (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 98 | a protein (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 174 | a protein (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 175 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 219 | a protein (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 278-280 | a protein (UniProtKB | ChEBI) | ||||
Sequence: WDN | ||||||
Binding site | 285 | a protein (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 313 | a protein (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 413-414 | Cleavage; by caspase-3 | ||||
Sequence: DG |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein O-GlcNAcase
- EC number
- Short namesOGA
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9EQQ9
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 166 | No change in substrate affinity but 60% reduction in O-GlcNAcase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 174 | 2-fold increase in substrate affinity and 77% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. No recovery of activity in the presence of sodium azide. | ||||
Sequence: D → N | ||||||
Mutagenesis | 175 | 3-fold increase in substrate affinity and 90% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 70% recovery of activity in the presence of sodium azide. | ||||
Sequence: D → A | ||||||
Mutagenesis | 177 | 2-fold decrease in substrate affinity and 96% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 40% recovery of activity in the presence of sodium azide. | ||||
Sequence: D → N | ||||||
Mutagenesis | 878 | No effect on O-GlcNAcase activity. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000252119 | 1-916 | Protein O-GlcNAcase | |||
Sequence: MVQKESQAALEERESERNANPAAASGASLEQSVAPAPGEDNPSGAGAAAVVGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKTSVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPSVLTKEEEKKQPDEEPMDMVVEKQEEAEHKNDNQILTEIVEAKMAEELRPMDTDKESMAESKSPEMSMQEDCIPDVAPMQTDEQTQKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCALVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGFPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL | ||||||
Modified residue | 364 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Expression in the liver oscillates in a circadian manner with peak levels at CT8-CT12.
Developmental stage
Expressed throughout development from blastocyst stage to embryonic day 16.5.
Gene expression databases
Interaction
Subunit
Monomer (By similarity).
Interacts with CLOCK (PubMed:23395175).
Interacts with CLOCK (PubMed:23395175).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9EQQ9 | H4c1 P62806 | 2 | EBI-8321615, EBI-299632 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-46 | Disordered | ||||
Sequence: MVQKESQAALEERESERNANPAAASGASLEQSVAPAPGEDNPSGAG | ||||||
Domain | 60-336 | GH84 | ||||
Sequence: FLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNM | ||||||
Region | 443-465 | Disordered | ||||
Sequence: ALSGEPSVLTKEEEKKQPDEEPM | ||||||
Compositional bias | 450-465 | Basic and acidic residues | ||||
Sequence: VLTKEEEKKQPDEEPM |
Sequence similarities
Belongs to the glycosyl hydrolase 84 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9EQQ9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length916
- Mass (Da)103,162
- Last updated2001-10-01 v2
- ChecksumB2FAC6F10E03C5CA
Q9EQQ9-2
- Name2
Q9EQQ9-3
- Name3
- Differences from canonical
- 1-1: M → MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494B913 | A0A494B913_MOUSE | Oga | 182 | ||
A0A494BAA3 | A0A494BAA3_MOUSE | Oga | 84 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020871 | 1 | in isoform 3 | |||
Sequence: M → MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM | ||||||
Alternative sequence | VSP_020870 | 1-698 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 6 | in Ref. 3; BAE26311 | ||||
Sequence: S → T | ||||||
Sequence conflict | 52-53 | in Ref. 3; BAE26311 | ||||
Sequence: GA → RT | ||||||
Compositional bias | 450-465 | Basic and acidic residues | ||||
Sequence: VLTKEEEKKQPDEEPM | ||||||
Alternative sequence | VSP_020872 | 699-725 | in isoform 2 | |||
Sequence: NDLFFQPPPLTPTSKVYTIRPYFPKDE → MYTTHSCLYSFFLTFFLVCCLTRLYFQ | ||||||
Sequence conflict | 742 | in Ref. 2; BAC97998 | ||||
Sequence: F → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF132214 EMBL· GenBank· DDBJ | AAG43273.2 EMBL· GenBank· DDBJ | mRNA | ||
AK129188 EMBL· GenBank· DDBJ | BAC97998.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC041109 EMBL· GenBank· DDBJ | AAH41109.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC054821 EMBL· GenBank· DDBJ | AAH54821.1 EMBL· GenBank· DDBJ | mRNA | ||
AK012695 EMBL· GenBank· DDBJ | BAB28416.1 EMBL· GenBank· DDBJ | mRNA | ||
AK014781 EMBL· GenBank· DDBJ | BAB29550.1 EMBL· GenBank· DDBJ | mRNA | ||
AK077613 EMBL· GenBank· DDBJ | BAC36900.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088774 EMBL· GenBank· DDBJ | BAC40564.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145227 EMBL· GenBank· DDBJ | BAE26311.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |