Polypeptide N-acetylgalactosaminyltransferase 1 is an
enzyme that in
humans is encoded by the GALNT1gene.[5][6][7]
This gene encodes a member of the UDP-N-acetyl-alpha-D-
galactosamine:
polypeptide N-
acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate
mucin-type O-linked
glycosylation in the
Golgi apparatus by
catalyzing the transfer of GalNAc to
serine and
threonine residues on target
proteins. They are characterized by an
N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc
transferase motif, and a C-terminal
ricin/
lectin-like domain. GalNAc-Ts have different, but overlapping,
substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature.[7]
Meurer JA, Naylor JM, Baker CA, et al. (1996). "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase". J. Biochem. 118 (3): 568–74.
doi:
10.1093/oxfordjournals.jbchem.a124947.
PMID8690719.
Takai S, Hinoda Y, Adachi T, et al. (1997). "A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1". Hum. Genet. 99 (3): 293–4.
doi:
10.1007/s004390050359.
PMID9050910.
S2CID22965327.
Röttger S, White J, Wandall HH, et al. (1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". J. Cell Sci. 111 (1): 45–60.
doi:
10.1242/jcs.111.1.45.
PMID9394011.
Brokx RD, Revers L, Zhang Q, et al. (2004). "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat". Biochemistry. 42 (47): 13817–25.
CiteSeerX10.1.1.879.1929.
doi:
10.1021/bi0353070.
PMID14636048.