Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3.
A novel isoform of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated ppGaNTase-T3, has been cloned from a mouse testis cDNA library and expressed in COS7 cells. ppGaNTase-T3 displayed 64 and 59% amino acid identity with ppGaNTase-T1 and ppGaNTase-T2, respectively, and 96% amino acid identity with the recently reported human form of ppGaNTase-T3. The ppGaNTase-T3 transcript is abundant in the major salivary glands, gastrointestinal tract and both the male and female reproductive systems. ppGaNTase-T3 and ppGaNTase-T1 display overlapping substrate preferences in vitro, although mapping studies of O-glycosylated peptides suggests that certain hydroxyamino acids are preferentially glycosylated by each isoform. This suggests that more than one isoform of ppGaNTase may be required to complete the O-glycosylation of endogenous substrates.
Department of Dental Research, School of Medicine and Dentistry, University of Rochester, New York 14642, USA.
J
J
Zara
F K
FK
Hagen
K G
KG
Ten Hagen
B C
BC
Van Wuyckhuyse
L A
LA
Tabak
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D019556:COS Cells; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D005260:Female; D015870:Gene Expression; D015723:Gene Library; D006031:Glycosylation; D006801:Humans; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009077:Mucins / Q000378:metabolism; D017350:N-Acetylgalactosaminyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D013379:Substrate Specificity; D013737:Testis / Q000378:metabolism; D014162:Transfection; D014599:Uterus / Q000378:metabolism; D000097763:Polypeptide N-acetylgalactosaminyltransferase
D018076:DNA, Complementary; D009077:Mucins; D017350:N-Acetylgalactosaminyltransferases; D012333:RNA, Messenger; D000097763:Polypeptide N-acetylgalactosaminyltransferase