Q7TT15 · GLT17_MOUSE
- ProteinPolypeptide N-acetylgalactosaminyltransferase 17
- GeneGalnt17
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids598 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May catalyze 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.
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 | 192 | substrate | ||||
Sequence: D | ||||||
Binding site | 223 | substrate | ||||
Sequence: R | ||||||
Binding site | 246 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 378 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 381 | substrate | ||||
Sequence: R | ||||||
Binding site | 386 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Molecular Function | polypeptide N-acetylgalactosaminyltransferase activity | |
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 17
- EC number
- 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 accessionQ7TT15
- Secondary accessions
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 | 1-6 | Cytoplasmic | ||||
Sequence: MASLRR | ||||||
Transmembrane | 7-27 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VKVLLVLNLIAVAGFVIFLAK | ||||||
Topological domain | 28-598 | Lumenal | ||||
Sequence: CRPIAVRSGDAFHEIRPRAEVANLSAHSASPIQDAVLKRLSLLEDIVYRQLNGLSKSLGLIEGYGGRGKGGLPATLSPSEEEKAKGPHEKYGYNSYLSEKISLDRSIPDYRPTKCKELKYSKELPQISIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKAPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKAATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELWCMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLPLENPGIDIGDVSERKALRKSLKCKNFQWYLDHVYPEMRRYNNTIAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLDCDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWAIKNPIK |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059140 | 1-598 | Polypeptide N-acetylgalactosaminyltransferase 17 | |||
Sequence: MASLRRVKVLLVLNLIAVAGFVIFLAKCRPIAVRSGDAFHEIRPRAEVANLSAHSASPIQDAVLKRLSLLEDIVYRQLNGLSKSLGLIEGYGGRGKGGLPATLSPSEEEKAKGPHEKYGYNSYLSEKISLDRSIPDYRPTKCKELKYSKELPQISIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKAPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKAATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELWCMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLPLENPGIDIGDVSERKALRKSLKCKNFQWYLDHVYPEMRRYNNTIAYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLDCDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWAIKNPIK | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 142↔373 | |||||
Sequence: CKELKYSKELPQISIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKAPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKAATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELWCMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPC | ||||||
Disulfide bond | 364↔443 | |||||
Sequence: CGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLPLENPGIDIGDVSERKALRKSLKC | ||||||
Glycosylation | 461 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 478↔494 | |||||
Sequence: CLDQGPLENHTAILYPC | ||||||
Glycosylation | 486 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 526↔541 | |||||
Sequence: CLVDNSKSRLPQLLDC | ||||||
Disulfide bond | 568↔586 | |||||
Sequence: CLEVENRGLAGIDLILRSC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 151-262 | Catalytic subdomain A | ||||
Sequence: LPQISIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKAPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKAATGQVTGFFDAHVEFTAGWAEPVLSR | ||||||
Region | 319-381 | Catalytic subdomain B | ||||
Sequence: PIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIKVWLCGGSMEVLPCSRVAHIER | ||||||
Domain | 465-594 | Ricin B-type lectin | ||||
Sequence: AYGELRNNKAKDVCLDQGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLDCDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWAIK |
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 & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q7TT15-1
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
- Length598
- Mass (Da)67,691
- Last updated2003-10-01 v1
- Checksum66F91B355EF571F5
Q7TT15-2
- Name2
- Differences from canonical
- 194-196: SDE → R
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9Q714 | E9Q714_MOUSE | Galnt17 | 371 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 74 | in Ref. 3; BAC33446 | ||||
Sequence: V → D | ||||||
Alternative sequence | VSP_011232 | 194-196 | in isoform 2 | |||
Sequence: SDE → R | ||||||
Sequence conflict | 224 | in Ref. 3; BAC33446 | ||||
Sequence: E → D | ||||||
Sequence conflict | 264 | in Ref. 3; BAC33446 | ||||
Sequence: Q → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF467979 EMBL· GenBank· DDBJ | AAM62404.1 EMBL· GenBank· DDBJ | mRNA | ||
AK035817 EMBL· GenBank· DDBJ | BAC29197.1 EMBL· GenBank· DDBJ | mRNA | ||
AK048758 EMBL· GenBank· DDBJ | BAC33446.2 EMBL· GenBank· DDBJ | mRNA | ||
AK051281 EMBL· GenBank· DDBJ | BAC34591.2 EMBL· GenBank· DDBJ | mRNA | ||
BC052469 EMBL· GenBank· DDBJ | AAH52469.1 EMBL· GenBank· DDBJ | mRNA |