ST3GAL3

ST3 beta-galactoside alpha-2,3-sialyltransferase 3
Identifiers
Symbols	ST3GAL3 ; EIEE15; MRT12; SIAT6; ST3GALII; ST3GalIII; ST3N
External IDs	OMIM: 606494 MGI: 1316659 HomoloGene: 7539 GeneCards: ST3GAL3 Gene
EC number	2.4.99.6
Gene ontology Molecular function • beta-galactoside (CMP) alpha-2,3-sialyltransferase activity • N-acetyllactosaminide alpha-2,3-sialyltransferase activity Cellular component • Golgi membrane • extracellular region • integral component of Golgi membrane • Golgi cisterna membrane Biological process • carbohydrate metabolic process • dolichol-linked oligosaccharide biosynthetic process • protein O-linked glycosylation • O-glycan processing • keratan sulfate biosynthetic process • protein N-linked glycosylation via asparagine • glycosaminoglycan metabolic process • keratan sulfate metabolic process • post-translational protein modification • cellular protein metabolic process • small molecule metabolic process • sialylation Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6487	20441
Ensembl	ENSG00000126091	ENSMUSG00000028538
UniProt	Q11203	P97325
RefSeq (mRNA)	NM_001270459	NM_001161774
RefSeq (protein)	NP_001257388	NP_001155246
Location (UCSC)	Chr 1: 43.71 – 43.93 Mb	Chr 4: 117.93 – 118.13 Mb
PubMed search

ST3 beta-galactoside alpha-2,3-sialyltransferase 3, also known as ST3GAL3, is a protein which in humans is encoded by the ST3GAL3 gene.^[1][2]

Function

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.^[2]

Interestingly, 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 considererd a congenital disorder of glycosylation.

See also

• Sialyltransferase

References

1. 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. PMID 8333853.
2. "Entrez Gene: ST3GAL3 ST3 beta-galactoside alpha-2,3-sialyltransferase 3".

Further reading

• Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (Mar 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
• Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America 86 (9): 3384–8. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
• Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (Jun 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology 63 (6): 2452–6. PMC 250699. PMID 2542563.
• 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. PMID 2649653.
• 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. PMID 2829950.
• Kitagawa H, Paulson JC (Jul 1994). "Differential expression of five sialyltransferase genes in human tissues". The Journal of Biological Chemistry 269 (27): 17872–8. PMID 8027041.
• 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. PMID 8333853.
• Burger PC, Lötscher M, Streiff M, Kleene R, Kaissling B, Berger EG (Mar 1998). "Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization". Glycobiology 8 (3): 245–57. doi:10.1093/glycob/8.3.245. PMID 9451034.
• 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. PMID 12504121.
• 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 1626 (1-3): 92–6. doi:10.1016/s0167-4781(03)00021-6. PMID 12697334.
• Saito S, Aoki H, Ito A, Ueno S, Wada T, Mitsuzuka K, Satoh M, Arai Y, Miyagi T (Jul 2003). "Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic antigen-4 synthase". The Journal of Biological Chemistry 278 (29): 26474–9. doi:10.1074/jbc.M213223200. PMID 12716912.
• 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. PMID 12815231.
• 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. PMID 12931020.
• Jeanneau C, Chazalet V, Augé C, Soumpasis DM, Harduin-Lepers A, Delannoy P, Imberty A, Breton C (Apr 2004). "Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif". The Journal of Biological Chemistry 279 (14): 13461–8. doi:10.1074/jbc.M311764200. PMID 14722111.
• 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. PMID 15316282.
• Van Dyken SJ, Green RS, Marth JD (Feb 2007). "Structural and mechanistic features of protein O glycosylation linked to CD8+ T-cell apoptosis". Molecular and Cellular Biology 27 (3): 1096–111. doi:10.1128/MCB.01750-06. PMC 1800694. PMID 17101770.
• Hu H, Eggers K, Chen W, Garshasbi M, Motazacker MM, Wrogemann K, Kahrizi K, Tzschach A, Hosseini M, Bahman I, Hucho T, Mühlenhoff M, Gerardy-Schahn R, Najmabadi H, Ropers HH, Kuss AW (Sep 2011). "ST3GAL3 mutations impair the development of higher cognitive functions". American Journal of Human Genetics. 3 89 (3): 407–14. doi:10.1016/j.ajhg.2011.08.008. PMID 21907012.