GAL3ST3

GAL3ST3
Identifiers
Aliases	GAL3ST3 , GAL3ST-3, GAL3ST2, galactose-3-O-sulfotransferase 3
External IDs	OMIM: 608234 MGI: 3617843 HomoloGene: 57198 GeneCards: GAL3ST3
Gene location (Human)
Chr.	Chromosome 11 (human)
End	66,049,161 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	5,358,766 bp
RNA expression pattern
	Top expressed in
	left lobe of thyroid gland; ; right lobe of thyroid gland; ; caudate nucleus; ; putamen; ; nucleus accumbens; ; prefrontal cortex; ; Brodmann area 9; ; ganglionic eminence; ; amygdala; ; hypothalamus;
	Top expressed in
	hippocampus proper; ; superior frontal gyrus; ; cerebellum; ; cerebellar cortex; ; neural tube; ; mesencephalon; ; olfactory bulb; ; ganglionic eminence; ; heart; ; hypothalamus;
	More reference expression data
	n/a
Gene ontology
Molecular function	galactose 3-O-sulfotransferase activity ; transferase activity ; galactosylceramide sulfotransferase activity ; proteoglycan sulfotransferase activity ; 3'-phosphoadenosine 5'-phosphosulfate binding ; carbohydrate binding ;
Cellular component	integral component of membrane ; Golgi cisterna membrane ; Golgi apparatus ; membrane ;
Biological process	glycolipid biosynthetic process ; sulfur compound metabolic process ; poly-N-acetyllactosamine metabolic process ; oligosaccharide metabolic process ; proteoglycan biosynthetic process ; monosaccharide metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	89792
	545276
	ENSG00000175229
	ENSMUSG00000047658
	Q96A11
	P61315
	NM_033036
	NM_001024717
	NP_149025
	NP_001019888
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Galactose-3-O-sulfotransferase 3 is an enzyme that in humans is encoded by the GAL3ST3 gene.^[5]^[6]^[7]

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.^[7]

Related Research Articles

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

In enzymology, a N-acetyllactosaminide 3-alpha-galactosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

Carbohydrate sulfotransferase 6 is an enzyme that in humans is encoded by the CHST6 gene.

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the GCNT1 gene.

Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.

Carbohydrate sulfotransferase 4 is an enzyme that in humans is encoded by the CHST4 gene.

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase is an enzyme that in humans is encoded by the ST3GAL4 gene.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 is an enzyme that in humans is encoded by the B3GNT2 gene.

Carbohydrate sulfotransferase 1 is an enzyme that in humans is encoded by the CHST1 gene.

Galactose-3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the GAL3ST2 gene.

ST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, also known as sialyltransferase 3C (SIAT3-C) or sialyltransferase 7D (SIAT7-D) is a sialyltransferase enzyme that in humans is encoded by the ST6GALNAC4 gene.

Beta-1,4-galactosyltransferase 2 is an enzyme that in humans is encoded by the B4GALT2 gene.

Beta-1,3-galactosyltransferase 5 is an enzyme that in humans is encoded by the B3GALT5 gene.

Galactose-3-O-sulfotransferase 4 is an enzyme that in humans is encoded by the GAL3ST4 gene.

Beta-1,4-galactosyltransferase 3 is an enzyme that in humans is encoded by the B4GALT3 gene.

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 is an enzyme that in humans is encoded by the NDST3 gene. It catalyses the reaction:

3'-phosphoadenylyl sulfate + α-D-glucosaminyl-[heparan sulfate]_(n) = adenosine 3',5'-bisphosphate + 2 H⁺ + N-sulfo-α-D-glucosaminyl-[heparan sulfate]_(n)

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span>

Carbohydrate sulfotransferases are sulfotransferase enzymes that transfer sulfate to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.

Galactose-3-O-sulfotransferases is a family of several mammalian galactose-3-O-sulfotransferase proteins. Gal-3-O-sulfotransferase is thought to play a critical role in 3'-sulfation of N-acetyllactosamine in both O- and N-glycans.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000175229 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047658 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Suzuki A, Hiraoka N, Suzuki M, Angata K, Misra AK, McAuliffe J, Hindsgaul O, Fukuda M (Jun 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.
↑ El-Fasakhany FM, Uchimura K, Kannagi R, Muramatsu T (Jul 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.
1 2 "Entrez Gene: GAL3ST3 galactose-3-O-sulfotransferase 3".

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.
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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
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.
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. doi:10.1023/A:1007074005371. PMID 10815989. S2CID 19966059.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID 8889548.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000175229 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000047658 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11323440-5] Suzuki A, Hiraoka N, Suzuki M, Angata K, Misra AK, McAuliffe J, Hindsgaul O, Fukuda M (Jun 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.

[pmid11356829-6] El-Fasakhany FM, Uchimura K, Kannagi R, Muramatsu T (Jul 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.

[entrez-7] 1 2 "Entrez Gene: GAL3ST3 galactose-3-O-sulfotransferase 3".

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GAL3ST3

Related Research Articles

References

Further reading