ST3GAL3

ST3GAL3
Identifiers
Aliases	ST3GAL3, EIEE15, MRT12, SIAT6, ST3GALII, ST3GalIII, ST3N, ST3 beta-galactoside alpha-2,3-sialyltransferase 3, ST3Gal III, DEE15
External IDs	OMIM: 606494 MGI: 1316659 HomoloGene: 7539 GeneCards: ST3GAL3
Gene location (Human) Chr. Chromosome 1 (human) Band 1p34.1 Start 43,705,824 bp End 43,931,165 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 D1- D2.1 Start 117,789,351 bp End 117,992,111 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle ganglionic eminence sperm prefrontal cortex Brodmann area 9 nucleus accumbens hypothalamus popliteal artery right coronary artery putamen Top expressed in motor neuron right ventricle masseter muscle ankle internal carotid artery intercostal muscle left lobe of liver digastric muscle temporal muscle triceps brachii muscle More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity glycosyltransferase activity sialyltransferase activity beta-galactoside (CMP) alpha-2,3-sialyltransferase activity N-acetyllactosaminide alpha-2,3-sialyltransferase activity Cellular component integral component of membrane Golgi apparatus membrane extracellular region Golgi cisterna membrane Golgi membrane Biological process sialylation protein glycosylation O-glycan processing keratan sulfate biosynthetic process oligosaccharide metabolic process protein N-linked glycosylation via asparagine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6487 20441 Ensembl ENSG00000126091 ENSMUSG00000028538 UniProt Q11203 P97325 RefSeq (mRNA) NM_001270459 NM_001270460 NM_001270461 NM_001270462 NM_001270463 NM_001270464 NM_001270465 NM_001270466 NM_006279 NM_174963 NM_174964 NM_174965 NM_174966 NM_174967 NM_174968 NM_174969 NM_174970 NM_174971 NM_174972 NM_001350619 NM_001350620 NM_001350621 NM_001363573 NM_001161774 NM_001285520 NM_001285521 NM_009176 RefSeq (protein) NP_001257388 NP_001257389 NP_001257390 NP_001257391 NP_001257392 NP_001257393 NP_001257394 NP_001257395 NP_006270 NP_777623 NP_777624 NP_777625 NP_777626 NP_777627 NP_777628 NP_777629 NP_777630 NP_777631 NP_001337548 NP_001337549 NP_001337550 NP_001350502 NP_001155246 NP_001272449 NP_001272450 NP_033202 Location (UCSC) Chr 1: 43.71 – 43.93 Mb Chr 4: 117.79 – 117.99 Mb PubMed search
Wikidata
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ST3 beta-galactoside alpha-2,3-sialyltransferase 3, also known as ST3GAL3, is a protein which in humans is encoded by the ST3GAL3 gene.

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.

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.

See also

• Sialyltransferase

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. Bibcode:1989PNAS...86.3384P. 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. doi:10.1128/JVI.63.6.2452-2456.1989. 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. doi:10.1016/S0021-9258(17)32390-6. 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 (BBA) - Gene Structure and Expression. 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. S2CID 23897339.
• 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. S2CID 6438454.
• 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. S2CID 1544031.
• 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. 89 (3): 407–14. doi:10.1016/j.ajhg.2011.08.008. PMC 3169827. PMID 21907012.
• Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.