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Protein-coding gene in the species Homo sapiens
Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 is an enzyme that in humans is encoded by the HS3ST3A1 gene .[5] [6]
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. 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 the liver and placenta .[6]
References [ edit ]
^ a b c GRCh38: Ensembl release 89: ENSG00000153976 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000047759 – 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 (Mar 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci" . J Biol Chem . 274 (8): 5170–84. doi :10.1074/jbc.274.8.5170 PMID 9988767 . ^ a b "Entrez Gene: HS3ST3A1 heparan sulfate (glucosamine) 3-O-sulfotransferase 3A1" .
Further reading [ edit ]
Razi N, Lindahl U (1995). "Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides" . J. Biol. Chem . 270 (19): 11267–75. doi :10.1074/jbc.270.19.11267 PMID 7744762 . Liu J, Shworak NW, Sinaÿ P, et al. (1999). "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities" . J. Biol. Chem . 274 (8): 5185–92. doi :10.1074/jbc.274.8.5185 PMID 9988768 . Shukla D, Liu J, Blaiklock P, et al. (1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry" . Cell . 99 (1): 13–22. doi :10.1016/S0092-8674(00)80058-6 PMID 10520990 . S2CID 14139940 . Liu J, Shriver Z, Blaiklock P, et al. (2000). "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-unsubstituted glucosamine residues" . J. Biol. Chem . 274 (53): 38155–62. doi :10.1074/jbc.274.53.38155 PMID 10608887 . Salehi LB, Mangino M, De Serio S, et al. (2002). "Assignment of a locus for autosomal dominant idiopathic scoliosis (IS) to human chromosome 17p11". Hum. Genet . 111 (4–5): 401–4. doi :10.1007/s00439-002-0785-4 . PMID 12384783 . S2CID 29912776 . 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 . Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment" . Genome Res . 13 (10): 2265–70. doi :10.1101/gr.1293003 . PMC 403697 PMID 12975309 . Moon AF, Edavettal SC, Krahn JM, et al. (2004). "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1" . J. Biol. Chem . 279 (43): 45185–93. doi :10.1074/jbc.M405013200 PMC 4114238 PMID 15304505 . 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 .
