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polypeptide N-acetylgalactosaminyltransferase 17; protein-UDP acetylgalactosaminyltransferase 17; UDP-galNAc:polypeptide N-acetylgalactosaminyltransferase 17; polypeptide galNAc transferase 17; galNAc-T17; pp-GaNTase 17 (GALNT17, GALNTL6)
Function:
- catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a Ser or Thr on the protein receptor (putative)
- protein modification; protein glycosylation
UDP-N-acetyl-D-galactosamine + polypeptide UDP + N-acetyl-D-galactosaminyl-polypeptide
Cofactor: Mn+2 (putative), Ca+2 (putative)
Structure:
- 2 conserved domains in the glycosyltransferase region:
a) N-terminal domain (domain A, GT1 motif), probably involved in Mn+2 coordination & substrate binding
b) C-terminal domain (domain B, gal/galNAc-T motif), probably involved in catalytic reaction & UDP-gal binding
- the ricin B-type lectin domain binds to galNAc & contributes to the glycopeptide specificity (putative)
- belongs to the glycosyltransferase 2 family, galNAc-T subfamily
- contains 1 ricin B-type lectin domain
Compartment:
- Golgi apparatus membrane
Alternative splicing: named isoforms=2
General
galactosyltransferase
glycoprotein
membrane protein
Properties
SIZE: entity length = 601 aa
MW = 70 kD
COMPARTMENT: golgi
MOTIF: transmembrane domain {8-28}
cysteine residue {C130}
MODIFICATION: cysteine residue {C360}
active site
SITE: 139-248
MOTIF: N-glycosylation site {N141}
manganese [Mn]-binding site
SITE: 232-232
manganese [Mn]-binding site
SITE: 234-234
active site
SITE: 306-368
MOTIF: cysteine residue {C351}
MODIFICATION: cysteine residue {C427}
cysteine residue {C360}
MODIFICATION: cysteine residue {C130}
manganese [Mn]-binding site
SITE: 365-365
cysteine residue {C427}
MODIFICATION: cysteine residue {C351}
Ricin B-type lectin {453-585}
MOTIF: cysteine residue {C466}
MODIFICATION: cysteine residue {C483}
cysteine residue {C483}
MODIFICATION: cysteine residue {C466}
cysteine residue {C518}
MODIFICATION: cysteine residue {C533}
cysteine residue {C533}
MODIFICATION: cysteine residue {C518}
cysteine residue {C558}
MODIFICATION: cysteine residue {C573}
cysteine residue {C573}
MODIFICATION: cysteine residue {C558}
N-glycosylation site {N588}
Database Correlations
UniProt Q49A17
PFAM correlations
Kegg hsa:4421
References
UniProt :accession Q49A17