GBA2

GBA2
Identifiers
Aliases	GBA2, SPG46, AD035, NLGase, glucosylceramidase beta 2
External IDs	OMIM: 609471; MGI: 2654325; HomoloGene: 10859; GeneCards: GBA2; OMA:GBA2 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9p13.3 Start 35,736,866 bp End 35,749,228 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 A5 Start 43,566,928 bp End 43,578,873 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum transverse colon mucosa of transverse colon muscle layer of sigmoid colon right lobe of thyroid gland rectum apex of heart left lobe of thyroid gland anterior pituitary body of stomach Top expressed in medial dorsal nucleus medial geniculate nucleus ascending aorta superior frontal gyrus granulocyte dorsal tegmental nucleus seminiferous tubule nucleus accumbens subiculum lateral geniculate nucleus More reference expression data BioGPS n/a
Gene ontology Molecular function hydrolase activity, acting on glycosyl bonds catalytic activity beta-glucosidase activity hydrolase activity hydrolase activity, hydrolyzing O-glycosyl compounds glucosylceramidase activity glucosyltransferase activity steryl-beta-glucosidase activity transferase activity glycosyltransferase activity Cellular component Golgi apparatus endoplasmic reticulum membrane membrane Golgi membrane plasma membrane smooth endoplasmic reticulum endoplasmic reticulum integral component of membrane cytosol extrinsic component of membrane extrinsic component of endoplasmic reticulum membrane extrinsic component of Golgi membrane Biological process glycosphingolipid metabolic process lipid metabolism bile acid metabolic process glycoside catabolic process glucosylceramide catabolic process central nervous system neuron development metabolism sphingolipid metabolic process central nervous system development cholesterol metabolic process lipid glycosylation regulation of actin filament polymerization regulation of microtubule polymerization regulation of membrane lipid distribution steroid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 57704 230101 Ensembl ENSG00000070610 ENSMUSG00000028467 UniProt Q9HCG7 Q69ZF3 RefSeq (mRNA) NM_020944 NM_001330660 NM_172692 RefSeq (protein) NP_001317589 NP_065995 NP_766280 Location (UCSC) Chr 9: 35.74 – 35.75 Mb Chr 4: 43.57 – 43.58 Mb PubMed search
Wikidata
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GBA2 is the gene that encodes the enzyme non-lysosomal glucosylceramidase in humans. It has glucosylceramidase (EC 3.2.1.45) activity.

Function

This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.

See also

• Closely related enzymes
  • GBA: acid β-glucosidase (lysosomal), EC 3.2.1.45
  • GBA3: acid β-glucosidase (cytosolic), EC 3.2.1.21

Further reading

• Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl:1874/5091. PMID 11530211. S2CID 13576808.
• Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID 2136376.
• Boot RG, Verhoek M, Donker-Koopman W, et al. (2007). "Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2". J. Biol. Chem. 282 (2): 1305–12. doi:10.1074/jbc.M610544200. hdl:1887/49963. PMID 17105727. S2CID 24657729.
• Wolk T, Schreiber M (2007). "N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization". Med. Microbiol. Immunol. 195 (3): 165–72. doi:10.1007/s00430-006-0016-z. PMID 16547752. S2CID 31347157.
• 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.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. S2CID 21903526.
• Pantophlet R, Wilson IA, Burton DR (2003). "Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design". J. Virol. 77 (10): 5889–901. doi:10.1128/JVI.77.10.5889-5901.2003. PMC 154011. PMID 12719582.
• Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin". J. Gen. Virol. 84 (Pt 2): 353–60. doi:10.1099/vir.0.18734-0. PMID 12560567.
• 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.
• Nagase T, Kikuno R, Nakayama M, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (4): 273–81. doi:10.1093/dnares/7.4.271. PMID 10997877.
• Matern H, Heinemann H, Legler G, Matern S (1997). "Purification and characterization of a microsomal bile acid beta-glucosidase from human liver". J. Biol. Chem. 272 (17): 11261–7. doi:10.1074/jbc.272.17.11261. PMID 9111029. S2CID 33058533.
• Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416. S2CID 17660.
• Bolmstedt A, Sjölander S, Hansen JE, et al. (1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
• Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
• Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. doi:10.1128/jvi.67.1.150-160.1993. PMC 237347. PMID 8093218.
• Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. Bibcode:1988PNAS...85.9248M. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.
• Blough HA, Pauwels R, De Clercq E, et al. (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.