Q9VUT6 · GALT8_DROME
- ProteinPolypeptide N-acetylgalactosaminyltransferase 8
- GenePgant8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids590 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels fro Muc5AC-3/13.
Catalytic activity
- L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H+ + UDP
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 168 | substrate | ||||
Sequence: D | ||||||
Binding site | 220 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 221 | substrate | ||||
Sequence: S | ||||||
Binding site | 222 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 322 | substrate | ||||
Sequence: W | ||||||
Binding site | 350 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 353 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | Golgi stack | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Molecular Function | polypeptide N-acetylgalactosaminyltransferase activity | |
Biological Process | oligosaccharide biosynthetic process | |
Biological Process | protein O-linked glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePolypeptide N-acetylgalactosaminyltransferase 8
- EC number
- Short namespp-GaNTase 8
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VUT6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MCLDIWRHKKK | ||||||
Transmembrane | 12-31 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VLPLLLLMAIGSIIYYLYTL | ||||||
Topological domain | 32-590 | Lumenal | ||||
Sequence: KLEGERDESATSTTSRLERDIRDLQAVFESEVIPDLGALGRPARGNWTEEQLEAIAKSQRETGYNAWLSKRISPERSLYDMRHRSCKKLKYPMEKLPSVSVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKIKFLNMVQHRRITTQVGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLLKEEAVAMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGNFQIRYTNKDKNSEKKLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLATDFLNLYPILDPAEYASGVLQSISSPKLCLDRKDPSHGQPKLAPCSSDHVFPSPEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKTHQVISGQQQNFRHCLEAQPELNAVTSSVCDPKNHKQQWKFGYLNSQRLQHFWDNVKTQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059162 | 1-590 | Polypeptide N-acetylgalactosaminyltransferase 8 | |||
Sequence: MCLDIWRHKKKVLPLLLLMAIGSIIYYLYTLKLEGERDESATSTTSRLERDIRDLQAVFESEVIPDLGALGRPARGNWTEEQLEAIAKSQRETGYNAWLSKRISPERSLYDMRHRSCKKLKYPMEKLPSVSVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKIKFLNMVQHRRITTQVGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLLKEEAVAMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGNFQIRYTNKDKNSEKKLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLATDFLNLYPILDPAEYASGVLQSISSPKLCLDRKDPSHGQPKLAPCSSDHVFPSPEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKTHQVISGQQQNFRHCLEAQPELNAVTSSVCDPKNHKQQWKFGYLNSQRLQHFWDNVKTQ | ||||||
Glycosylation | 77 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 117↔345 | |||||
Sequence: CKKLKYPMEKLPSVSVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKIKFLNMVQHRRITTQVGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLLKEEAVAMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPC | ||||||
Glycosylation | 241 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 336↔419 | |||||
Sequence: CGGQILEVPCSRVGHLFRDGNFQIRYTNKDKNSEKKLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHC | ||||||
Disulfide bond | 459↔475 | |||||
Sequence: CLDRKDPSHGQPKLAPC | ||||||
Disulfide bond | 502↔517 | |||||
Sequence: CLEVRNHGVNVHIYQC | ||||||
Disulfide bond | 546↔561 | |||||
Sequence: CLEAQPELNAVTSSVC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. No expression detected during embryonic stages 16-17 or in third instar larvae imaginal disks.
Developmental stage
Expressed both maternally and zygotically. Weakly expressed during early embryonic stages but increases during 12-24 hours of embryogenesis through larval development and continues to be expressed throughout adulthood, albeit at slightly lower levels in males than females.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 127-236 | Catalytic subdomain A | ||||
Sequence: LPSVSVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKIKFLNMVQHRRITTQVGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAP | ||||||
Region | 291-353 | Catalytic subdomain B | ||||
Sequence: PHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFR | ||||||
Domain | 446-573 | Ricin B-type lectin | ||||
Sequence: ASGVLQSISSPKLCLDRKDPSHGQPKLAPCSSDHVFPSPEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKTHQVISGQQQNFRHCLEAQPELNAVTSSVCDPKNHKQQWKFG |
Domain
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length590
- Mass (Da)68,100
- Last updated2000-05-01 v1
- ChecksumB18B759A9FC2B021
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014296 EMBL· GenBank· DDBJ | AAF49587.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY070966 EMBL· GenBank· DDBJ | AAL48588.1 EMBL· GenBank· DDBJ | mRNA |