Biology:GALNT1

Generic protein structure example

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.

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.

Further reading

• "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation.". J. Biol. Chem. 264 (30): 17615–8. 1989. doi:10.1016/S0021-9258(19)84610-0. PMID 2681181. 
• "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.". J. Biol. Chem. 271 (29): 17006–12. 1996. doi:10.1074/jbc.271.29.17006. PMID 8663203. 
• "cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase.". J. Biochem. 118 (3): 568–74. 1996. doi:10.1093/oxfordjournals.jbchem.a124947. PMID 8690719. 
• "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene.". Glycobiology 6 (2): 231–41. 1996. doi:10.1093/glycob/6.2.231. PMID 8727794. 
• "A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase type 1 gene is located at the chromosomal region 18q12.1.". Hum. Genet. 99 (3): 293–4. 1997. doi:10.1007/s004390050359. PMID 9050910. 
• "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3.". J. Biol. Chem. 272 (38): 23503–14. 1997. doi:10.1074/jbc.272.38.23503. PMID 9295285. 
• "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo.". J. Biol. Chem. 272 (40): 24780–93. 1997. doi:10.1074/jbc.272.40.24780. PMID 9312074. 
• "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. 1998. doi:10.1242/jcs.111.1.45. PMID 9394011. 
• "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.". Glycobiology 8 (6): 547–55. 1998. doi:10.1093/glycob/8.6.547. PMID 9592121. 
• Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074. 
• "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites.". J. Biol. Chem. 277 (49): 47088–96. 2003. doi:10.1074/jbc.M207369200. PMID 12364335. 
• "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core.". Glycobiology 13 (12): 929–39. 2004. doi:10.1093/glycob/cwg109. PMID 12925576. 
• "Nuclear magnetic resonance-based dissection of a glycosyltransferase specificity for the mucin MUC1 tandem repeat.". Biochemistry 42 (47): 13817–25. 2004. doi:10.1021/bi0353070. PMID 14636048. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.