GALNT6

From Wikipedia, the free encyclopedia

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)

Identifiers

GALNT6; GALNAC-T6; GalNAcT6

External IDs

OMIM: 605148 MGI: 1891640 HomoloGene: 5218

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_007210 (mRNA)
NP_009141 (protein)

XM_001000202 (mRNA)
XP_001000202 (protein)

Location

Chr 12: 50.03 - 50.07 Mb

Chr 15: 100.52 - 100.56 Mb

Pubmed search

[1]

[2]

UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6), also known as GALNT6, 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. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.^[1]

[edit] References

^ ^a ^b Entrez Gene: GALNT6 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6).

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Bennett EP, Hassan H, Mandel U, et al. (1999). "Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy.". J. Biol. Chem. 274 (36): 25362-70. PMID 10464263.
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.
Argüeso P, Tisdale A, Mandel U, et al. (2003). "The cell-layer- and cell-type-specific distribution of GalNAc-transferases in the ocular surface epithelia is altered during keratinization.". Invest. Ophthalmol. Vis. Sci. 44 (1): 86-92. PMID 12506059.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
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.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117-26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.