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Probable polypeptide N-acetylgalactosaminyltransferase 8

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.

Function

Probably 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.

Pathway

Protein modification; protein glycosylation.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Tissue specificity

Widely expressed. Expressed in heart, skeletal muscle, kidney, liver, small intestine and placenta. Weakly expressed in colon, thymus, spleen, lung and leukocyte.

Cellular localization

  • Golgi apparatus membrane
  • Single-pass type II membrane protein

Alternative names

Probable polypeptide N-acetylgalactosaminyltransferase 8, Polypeptide GalNAc transferase 8, Protein-UDP acetylgalactosaminyltransferase 8, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8, GalNAc-T8, pp-GaNTase 8, GALNT8

Target type

Proteins

Primary research area

Oncology

Molecular weight

72851Da

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Primary Antibodies

Target

Application

Reactive species

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