Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12

FEBS Lett. 2002 Jul 31;524(1-3):211-8. doi: 10.1016/s0014-5793(02)03007-7.


We cloned in silico a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T), pp-GalNAc-T12. The deduced amino acid sequence of pp-GalNAc-T12 contains all conserved motifs in pp-GalNAc-T family proteins. Quantitative real time polymerase chain reaction analysis revealed that the pp-GalNAc-T12 transcript was expressed mainly in digestive organs such as stomach, small intestine and colon. The recombinant pp-GalNAc-T12 transferred GalNAc to the mucin-derived peptides such as the Muc1a, Muc5AC, EA2 peptides and the GalNAc-Muc5AC glycopeptide. Since mucins are glycoproteins mainly produced in the digestive organs, our results suggest that pp-GalNAc-T12 plays an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • Molecular Sequence Data
  • Mucins / genetics*
  • N-Acetylgalactosaminyltransferases / chemistry
  • N-Acetylgalactosaminyltransferases / genetics*
  • N-Acetylgalactosaminyltransferases / metabolism
  • Sequence Homology, Amino Acid
  • Tandem Repeat Sequences


  • DNA, Complementary
  • Mucins
  • GALNT12 protein, human
  • N-Acetylgalactosaminyltransferases

Associated data

  • GENBANK/AB078146
  • GENBANK/AF024865
  • GENBANK/AI800923
  • GENBANK/AL136084
  • GENBANK/BE677813
  • GENBANK/Y08564