GAL3ST3

From Wikipedia, the free encyclopedia

Galactose-3-O-sulfotransferase 3

Identifiers

GAL3ST3; GAL3ST2; GAL3ST-3; MGC142112; MGC142114

External IDs

OMIM: 608234 MGI: 3617843 HomoloGene: 57198

Gene ontology
Molecular Function:	• magnesium ion binding • galactosylceramide sulfotransferase activity • transferase activity • carbohydrate binding • 3'-phosphoadenosine 5'-phosphosulfate binding • proteoglycan sulfotransferase activity
Cellular Component:	• Golgi apparatus • membrane • integral to membrane
Biological Process:	• monosaccharide metabolic process • sulfur metabolic process • biosynthetic process • oligosaccharide metabolic process • proteoglycan biosynthetic process • poly-N-acetyllactosamine metabolic process

Orthologs

Human

Mouse

Refseq

NM_033036 (mRNA)
NP_149025 (protein)

XM_975776 (mRNA)
XP_980870 (protein)

Location

Chr 11: 65.57 - 65.57 Mb

Chr 19: 5.3 - 5.31 Mb

Pubmed search

[1]

[2]

Galactose-3-O-sulfotransferase 3, also known as GAL3ST3, is a human gene.^[1]

This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate group to the 3' position of galactose in N-acetyllactosamine in both type 2 (Gal-beta-1-4GlcNAc-R) oligosaccharides and core-2-branched O-glycans, but not on type 1 or core-1-branched structures. This gene, which has also been referred to as GAL3ST2, is different from the GAL3ST2 gene located on chromosome 2 that encodes a related enzyme with distinct tissue distribution and substrate specificities, compared to galactose-3-O-sulfotransferase 3.^[1]

[edit] References

^ ^a ^b Entrez Gene: GAL3ST3 galactose-3-O-sulfotransferase 3.

[edit] Further reading

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.
Chandrasekaran EV, Lakhaman SS, Chawda R, et al. (2004). "Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide.". J. Biol. Chem. 279 (11): 10032-41. doi:10.1074/jbc.M311989200. PMID 14701868.
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.
El-Fasakhany FM, Uchimura K, Kannagi R, Muramatsu T (2001). "A novel human Gal-3-O-sulfotransferase: molecular cloning, characterization, and its implications in biosynthesis of (SO(4)-3)Galbeta1-4(Fucalpha1-3)GlcNAc.". J. Biol. Chem. 276 (29): 26988-94. doi:10.1074/jbc.M100348200. PMID 11356829.
Seko A, Hara-Kuge S, Yamashita K (2001). "Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans.". J. Biol. Chem. 276 (28): 25697-704. doi:10.1074/jbc.M101558200. PMID 11333265.
Suzuki A, Hiraoka N, Suzuki M, et al. (2001). "Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.". J. Biol. Chem. 276 (26): 24388-95. doi:10.1074/jbc.M103135200. PMID 11323440.
Chandrasekaran EV, Jain RK, Rhodes JM, et al. (2000). "Characterization of distinct Gal:3-O-sulfotransferase activities in human tumor epithelial cell lines and of calf lymph node GlcNAc : 6-O-sulfotransferase activity.". Glycoconj. J. 16 (9): 523-36. PMID 10815989.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548.