Q5NDL3 · EOGT_CHICK
- ProteinEGF domain-specific O-linked N-acetylglucosamine transferase
- GeneEOGT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids535 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains.
Catalytic activity
- L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H+ + UDP
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | protein O-acetylglucosaminyltransferase activity | |
Biological Process | protein O-GlcNAcylation via threonine | |
Biological Process | protein O-linked glycosylation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEGF domain-specific O-linked N-acetylglucosamine transferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionQ5NDL3
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MFILLMFVLLLQEILA | ||||||
Chain | PRO_0000301975 | 17-535 | EGF domain-specific O-linked N-acetylglucosamine transferase | |||
Sequence: NSRDENLTELNSVLEEPTYSYRAINLPAEHIPYFLHNNRHIAGICKQDSRCPYKVGFYFVLHKYLKKLKSCWGYEKSCKSDYRFSYPVCDYVESGWANDIETAQQIFWKQADFGYIRERLNEMKTHCKPTVTGDSSLTCSQFLQHCRATNLYIDLRTAKRNHERFKEDFFQKGEIGGHCTLDVKAFLAEGQRKSPLQSWFAELQTFTSLNFRPLDDGKCDIVIEKPTYFMKLDAGVNMYHHFCDFVNLYITQHINNSFSTDVNIVMWDTSSYGYGDLFSETWKAFTDYDIIYLKTFDSKRVCFKEAVFSLLPRMRYGLFYNTPLISGCHGTGLFRAFSQHVLHRLNITQEGPKDGKIRVTILARSTDYRKILNQNELVNALKTVSTLEVKVVDYKYKELEFSEQLRITHNSDIFIGMHGAGLTHLLFLPDWAVVFELYNCEDERCYLDLARLRGIHYITWRKRNKVFPQDQGHHPTLGEHPKFTNYSFDVEEFMYLVLLAANHVSQHSKWPFRVKHDEF | ||||||
Glycosylation | 22 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 271 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 303-305 | Required for optimal activity | ||||
Sequence: DYD |
Sequence similarities
Belongs to the glycosyltransferase 61 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length535
- Mass (Da)62,868
- Last updated2007-09-11 v2
- Checksum2F0EC0F588B4BB3B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BU415425 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AJ868233 EMBL· GenBank· DDBJ | CAI30568.1 EMBL· GenBank· DDBJ | mRNA |