The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Multiple transcript variants encoding several different isoforms have been found for this gene.[6]
Mutations in the ST3GAL3 gene was recently shown to be the cause of autosomal recessive mental retardation 12. Since the mutations disrupt a glycosylation pathway, this disorder may be considered a congenital disorder of glycosylation.
^"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.
^Kitagawa H, Paulson JC (Jul 1993). "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase". Biochemical and Biophysical Research Communications. 194 (1): 375–82. doi:10.1006/bbrc.1993.1830. PMID8333853.
Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes. 2 (2): 163–9. PMID2649653.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Research and Human Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID2829950.
Kitagawa H, Paulson JC (Jul 1993). "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase". Biochemical and Biophysical Research Communications. 194 (1): 375–82. doi:10.1006/bbrc.1993.1830. PMID8333853.
Taniguchi A, Morishima T, Tsujita Y, Matsumoto Y, Matsumoto K (Jan 2003). "Genomic structure, expression, and transcriptional regulation of human Gal beta 1,3 GalNAc alpha 2,3-sialyltransferase gene". Biochemical and Biophysical Research Communications. 300 (2): 570–6. doi:10.1016/S0006-291X(02)02899-1. PMID12504121.
Taniguchi A, Saito K, Kubota T, Matsumoto K (Apr 2003). "Characterization of the promoter region of the human Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase III (hST3Gal III) gene". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1626 (1–3): 92–6. doi:10.1016/s0167-4781(03)00021-6. PMID12697334.
Grahn A, Barkhordar GS, Larson G (Mar 2002). "Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues". Glycoconjugate Journal. 19 (3): 197–210. doi:10.1023/A:1024253808424. PMID12815231. S2CID23897339.
Gretschel S, Haensch W, Schlag PM, Kemmner W (2003). "Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer". Oncology. 65 (2): 139–45. doi:10.1159/000072339. PMID12931020. S2CID6438454.
Grahn A, Barkhordar GS, Larson G (2005). "Identification of seven new alpha2,3-sialyltransferase III, ST3Gal III, transcripts from human foetal brain". Glycoconjugate Journal. 20 (7–8): 493–500. doi:10.1023/B:GLYC.0000038295.87747.0b. PMID15316282. S2CID1544031.