GALNT1

From Wikipedia, the free encyclopedia

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)

PDB rendering based on 1xhb.

Available structures: 1xhb

Identifiers

Symbol(s)

GALNT1; GALNAC-T1

External IDs

OMIM: 602273 MGI: 894693 HomoloGene: 8469

Gene ontology
Molecular Function:	• polypeptide N-acetylgalactosaminyltransferase activity • calcium ion binding • sugar binding • transferase activity, transferring glycosyl groups • manganese ion binding
Cellular Component:	• membrane • integral to membrane
Biological Process:	• protein amino acid O-linked glycosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_020474 (mRNA)
NP_065207 (protein)

NM_013814 (mRNA)
NP_038842 (protein)

Location

Chr 18: 31.49 - 31.55 Mb

Chr 18: 24.35 - 24.43 Mb

Pubmed search

[1]

[2]

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1), also known as GALNT1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: GALNT1 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1).

[edit] Further reading

Paulson JC, Colley KJ (1989). "Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation.". J. Biol. Chem. 264 (30): 17615–8. PMID 2681181.
White T, Bennett EP, Takio K, et al. (1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase.". J. Biol. Chem. 270 (41): 24156–65. PMID 7592619.
Bennett EP, Hassan H, Clausen H (1996). "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. PMID 8663203.
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. PMID 8690719.
Meurer JA, Drong RF, Homa FL, et al. (1996). "Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene.". Glycobiology 6 (2): 231–41. PMID 8727794.
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. PMID 9050910.
Wandall HH, Hassan H, Mirgorodskaya E, et al. (1997). "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. PMID 9295285.
Müller S, Goletz S, Packer N, et al. (1997). "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. PMID 9312074.
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 ( Pt 1): 45–60. PMID 9394011.
Bennett EP, Weghuis DO, Merkx G, et al. (1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family.". Glycobiology 8 (6): 547–55. PMID 9592121.
"Toward a complete human genome sequence." (1999). Genome Res. 8 (11): 1097–108. PMID 9847074.
Tenno M, Toba S, Kézdy FJ, et al. (2002). "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1).". Eur. J. Biochem. 269 (17): 4308–16. PMID 12199709.
Tenno M, Saeki A, Kézdy FJ, et al. (2003). "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. doi:10.1074/jbc.M207369200. PMID 12364335.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932.
Kinarsky L, Suryanarayanan G, Prakash O, et al. (2004). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core.". Glycobiology 13 (12): 929–39. doi:10.1093/glycob/cwg109. PMID 12925576.
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. doi:10.1021/bi0353070. PMID 14636048.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.