GALNT3

Polypeptide N-acetylgalactosaminyltransferase 3
Identifiers
Symbols	GALNT3 ; GalNAc-T3; HFTC; HHS
External IDs	OMIM: 601756 MGI: 894695 HomoloGene: 55827 GeneCards: GALNT3 Gene
EC number	2.4.1.41
Gene ontology Molecular function • polypeptide N-acetylgalactosaminyltransferase activity • calcium ion binding • protein binding • manganese ion binding • carbohydrate binding Cellular component • Golgi membrane • Golgi apparatus • membrane • integral component of membrane • Golgi cisterna membrane • perinuclear region of cytoplasm • extracellular exosome Biological process • carbohydrate metabolic process • protein O-linked glycosylation • O-glycan processing • protein O-linked glycosylation via serine • protein O-linked glycosylation via threonine • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2591	14425
Ensembl	ENSG00000115339	ENSMUSG00000026994
UniProt	Q14435	P70419
RefSeq (mRNA)	NM_004482	NM_015736
RefSeq (protein)	NP_004473	NP_056551
Location (UCSC)	Chr 2: 165.75 – 165.79 Mb	Chr 2: 66.08 – 66.12 Mb
PubMed search

Polypeptide N-acetylgalactosaminyltransferase 3 is an enzyme that in humans is encoded by the GALNT3 gene.^[1][2][3]

This gene encodes UDP-GalNAc transferase 3, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. Individual GalNAc-transferases have distinct activities and initiation of O-glycosylation is regulated by a repertoire of GalNAc-transferases. The protein encoded by this gene is highly homologous to other family members, however the enzymes have different substrate specificities.^[3]

References

1. Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology 8 (6): 547–55. doi:10.1093/glycob/8.6.547. PMID 9592121.
2. Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E (May 2004). "Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis". Nat Genet 36 (6): 579–81. doi:10.1038/ng1358. PMID 15133511.
3. "Entrez Gene: GALNT3 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)".

Further reading

• 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. doi:10.1074/jbc.271.29.17006. PMID 8663203.
• 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. doi:10.1074/jbc.272.38.23503. PMID 9295285.
• 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. PMID 9394011.
• Mandel U, Hassan H, Therkildsen MH, et al. (1999). "Expression of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcinomas: immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family". Glycobiology 9 (1): 43–52. doi:10.1093/glycob/9.1.43. PMID 9884405.
• Dosaka-Akita H, Kinoshita I, Yamazaki K, et al. (2002). "N-acetylgalactosaminyl transferase-3 is a potential new marker for non-small cell lung cancers". Br. J. Cancer 87 (7): 751–5. doi:10.1038/sj.bjc.6600536. PMC 2364253. PMID 12232759.
• 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. PMC 139241. 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. doi:10.1167/iovs.02-0181. PMID 12506059.
• Onitsuka K, Shibao K, Nakayama Y, et al. (2003). "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma". Cancer Sci. 94 (1): 32–6. doi:10.1111/j.1349-7006.2003.tb01348.x. PMID 12708471.
• Yamamoto S, Nakamori S, Tsujie M, et al. (2004). "Expression of uridine diphosphate N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase 3 in adenocarcinoma of the pancreas". Pathobiology 71 (1): 12–8. doi:10.1159/000072957. PMID 14555840.
• Gu C, Oyama T, Osaki T, et al. (2004). "Low expression of polypeptide GalNAc N-acetylgalactosaminyl transferase-3 in lung adenocarcinoma: impact on poor prognosis and early recurrence". Br. J. Cancer 90 (2): 436–42. doi:10.1038/sj.bjc.6601531. PMC 2409559. PMID 14735190.
• Miyahara N, Shoda J, Kawamoto T, et al. (2004). "Expression of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetylgalactosaminyltransferase isozyme 3 in the subserosal layer correlates with postsurgical survival of pathological tumor stage 2 carcinoma of the gallbladder". Clin. Cancer Res. 10 (6): 2090–9. doi:10.1158/1078-0432.CCR-1024-03. PMID 15041730.
• 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. PMC 528928. PMID 15489334.
• Ishikawa M, Kitayama J, Kohno K, Nagawa H (2005). "The expression pattern of UDP-N-acetyl-alpha-D-galactosamine-polypeptide N-acetyl-galactosaminyl transferase-3 in squamous cell carcinoma of the esophagus". Pathobiology 72 (3): 139–45. doi:10.1159/000084117. PMID 15860931.
• 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. PMC 1356129. PMID 16344560.
• Kato K, Jeanneau C, Tarp MA, et al. (2006). "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation". J. Biol. Chem. 281 (27): 18370–7. doi:10.1074/jbc.M602469200. PMID 16638743.
• Ichikawa S, Imel EA, Sorenson AH, et al. (2007). "Tumoral calcinosis presenting with eyelid calcifications due to novel missense mutations in the glycosyl transferase domain of the GALNT3 gene". J. Clin. Endocrinol. Metab. 91 (11): 4472–5. doi:10.1210/jc.2006-1247. PMID 16940445.
• Barbieri AM, Filopanti M, Bua G, Beck-Peccoz P (2007). "Two novel nonsense mutations in GALNT3 gene are responsible for familial tumoral calcinosis". J. Hum. Genet. 52 (5): 464–8. doi:10.1007/s10038-007-0126-5. PMID 17351710.
• Inoue T, Eguchi T, Oda Y, et al. (2007). "Expression of GalNAc-T3 and its relationships with clinicopathological factors in 61 extrahepatic bile duct carcinomas analyzed using stepwise sections - special reference to its association with lymph node metastases-". Mod. Pathol. 20 (2): 267–76. doi:10.1038/modpathol.3800700. PMID 17361208.