HS3ST1

HS3ST1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1ZRH
Identifiers
Aliases	HS3ST1 , 3OST, 3OST1, heparan sulfate-glucosamine 3-sulfotransferase 1
External IDs	OMIM: 603244 MGI: 1201606 HomoloGene: 3751 GeneCards: HS3ST1
Gene location (Human)
Chr.	Chromosome 4 (human)
End	11,429,564 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	39,912,818 bp
RNA expression pattern
	Top expressed in
	bronchial epithelial cell; ; caput epididymis; ; cavity of mouth; ; palpebral conjunctiva; ; mucosa of urinary bladder; ; pancreatic epithelial cell; ; gallbladder; ; trachea; ; cerebellar vermis; ; pancreatic ductal cell;
	Top expressed in
	cerebellar cortex; ; cumulus cell; ; olfactory bulb; ; cerebellar vermis; ; barrel cortex; ; superior frontal gyrus; ; medial geniculate nucleus; ; iris; ; respiratory epithelium; ; olfactory epithelium;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity ; sulfotransferase activity ; [heparan sulfate-glucosamine 3-sulfotransferase 1 activity]; heparan sulfate sulfotransferase activity ;
Cellular component	Golgi lumen ; integral component of membrane ; Golgi apparatus ;
Biological process	glycosaminoglycan biosynthetic process ; heparan sulfate proteoglycan biosynthetic process ;
	Sources:Amigo / QuickGO
Orthologs
	9957
	15476
	ENSG00000002587
	ENSMUSG00000051022
	O14792
	O35310
	NM_005114
	NM_010474
	NP_005105
	NP_034604
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 04, 2023

Heparan sulfate glucosamine 3-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS3ST1 gene.^[5]^[6]

Function

Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein.^[6]

Clinical significance

Polymorphisms in HS3ST1 appear to be a risk factor for developing Alzheimer's disease.^[7]

Related Research Articles

Glycosaminoglycans (GAGs) or mucopolysaccharides are long, linear polysaccharides consisting of repeating disaccharide units. The repeating two-sugar unit consists of a uronic sugar and an amino sugar, except in the case of the sulfated glycosaminoglycan keratan, where, in place of the uronic sugar there is a galactose unit. GAGs are found in vertebrates, invertebrates and bacteria. Because GAGs are highly polar molecules and attract water; the body uses them as lubricants or shock absorbers.

Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins. In this form, HS binds to a variety of protein ligands, including Wnt, and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB, and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus. One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.

In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 1 is an enzyme that catalyzes the chemical reaction

In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 2 is an enzyme that catalyzes the chemical reaction

In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 3 is an enzyme that catalyzes the chemical reaction

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 is an enzyme. In humans, it is encoded by the NDST1 gene.

Carbohydrate sulfotransferase 5 is an enzyme that in humans is encoded by the CHST5 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene.

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 is an enzyme that in humans is encoded by the NDST2 gene.

Heparan sulfate 2-O-sulfotransferase 1 is an enzyme that in humans is encoded by the HS2ST1 gene.

Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 is an enzyme that in humans is encoded by the HS3ST3B1 gene. Heparan sulfate biosynthetic enzymes are key components in generating myriad distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity ( HS3ST3A1). The Sulfotransferase domain of this enzyme is highly similar to the same domain of heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1 and these two enzymes sulfate an identical disaccharide. This gene is widely expressed, with the most abundant expression in liver and placenta.

Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 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)

Heparan sulfate glucosamine 3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the HS3ST2 gene.

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span> Class of enzymes which transfer an –SO3 group to glycoproteins and lipids

In biochemistry, carbohydrate sulfotransferases are enzymes within the class of sulfotransferases which catalyze the transfer of the sulfate functional group 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.

Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan 4IV-alpha-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase. This enzyme catalyses the following chemical reaction

Glucosaminyl 3-O-sulfotransferase may refer to:

Heparanase is an enzyme with systematic name heparan sulfate N-sulfo-D-glucosamine endoglucanase. This enzyme catalyses the following chemical reaction

Jian Liu is a John & Deborah S. McNeill, Jr. Distinguished Professor at the UNC Eshelman School of Pharmacy, at the University of North Carolina at Chapel Hill. He is also a founder and the chief scientific officer at Glycan Therapeutics.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000002587 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000051022 - 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.
↑ Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (February 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". The Journal of Biological Chemistry. 274 (8): 5170–84. doi: 10.1074/jbc.274.8.5170 . PMID 9988767.
1 2 "Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1".
↑ Witoelar A, Rongve A, Almdahl IS, et al. (2018-12-27). "Meta-analysis of Alzheimer's disease on 9,751 samples from Norway and IGAP study identifies four risk loci". Scientific Reports. 8 (1): 18088. Bibcode:2018NatSR...818088W. doi:10.1038/s41598-018-36429-6. PMC 6308232 . PMID 30591712.

External links

Overview of all the structural information available in the PDB for UniProt : O14792 (Human Heparan sulfate glucosamine 3-O-sulfotransferase 1) at the PDBe-KB .
Overview of all the structural information available in the PDB for UniProt : O35310 (Mouse Heparan sulfate glucosamine 3-O-sulfotransferase 1) at the PDBe-KB .

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000002587 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000051022 - 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.

[pmid9988767-5] Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD (February 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". The Journal of Biological Chemistry. 274 (8): 5170–84. doi: 10.1074/jbc.274.8.5170 . PMID 9988767.

[entrez-6] 1 2 "Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1".

[7] Witoelar A, Rongve A, Almdahl IS, et al. (2018-12-27). "Meta-analysis of Alzheimer's disease on 9,751 samples from Norway and IGAP study identifies four risk loci". Scientific Reports. 8 (1): 18088. Bibcode:2018NatSR...818088W. doi:10.1038/s41598-018-36429-6. PMC 6308232 . PMID 30591712.

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