GBA2

GBA2
Identifiers
Aliases	GBA2 , SPG46, AD035, NLGase, glucosylceramidase beta 2
External IDs	OMIM: 609471 MGI: 2654325 HomoloGene: 10859 GeneCards: GBA2
Gene location (Human)
Chr.	Chromosome 9 (human)
End	35,749,228 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	43,578,873 bp
RNA expression pattern
	Top expressed in
	transverse colon; ; right lobe of thyroid gland; ; rectum; ; left lobe of thyroid gland; ; anterior pituitary; ; body of stomach; ; gastric mucosa; ; right lung; ; right coronary artery; ; body of pancreas;
	Top expressed in
	medial dorsal nucleus; ; medial geniculate nucleus; ; ascending aorta; ; superior frontal gyrus; ; dorsal tegmental nucleus; ; seminiferous tubule; ; nucleus accumbens; ; subiculum; ; lateral geniculate nucleus; ; aortic valve;
	More reference expression data
	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
	57704
	230101
	ENSG00000070610
	ENSMUSG00000028467
	Q9HCG7
	Q69ZF3
	NM_020944 ; NM_001330660
	NM_172692
	NP_001317589 ; NP_065995
	NP_766280
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 05, 2024

GBA2 is the gene that encodes the enzyme non-lysosomal glucosylceramidase in humans.^[5]^[6] 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.^[6]

Related Research Articles

<span class="mw-page-title-main">Envelope glycoprotein GP120</span> Glycoprotein exposed on the surface of the HIV virus

Envelope glycoprotein GP120 is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1984. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and a specific interaction with the CD4 receptor, particularly on helper T-cells. Binding to CD4 induces the start of a cascade of conformational changes in gp120 and gp41 that lead to the fusion of the viral membrane with the host cell membrane. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

Acid alpha-glucosidase, also called acid maltase, is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme, but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol. In humans, it is encoded by the GAA gene. Errors in this gene cause glycogen storage disease type II.

C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene. CLEC4M has also been designated as CD299.

Alpha-(1,6)-fucosyltransferase is an enzyme that in humans is encoded by the FUT8 gene.

Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.

Neutral alpha-glucosidase AB is an enzyme that in humans is encoded by the GANAB gene.

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase is an enzyme that in humans is encoded by the MAN1B1 gene.

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT2 gene.

Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B is an enzyme that in humans is encoded by the MGAT4B gene.

Glycoprotein endo-alpha-1,2-mannosidase is an enzyme that in humans is encoded by the MANEA gene.

Epididymis-specific alpha-mannosidase is an enzyme that in humans is encoded by the MAN2B2 gene.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA is an enzyme that in humans is encoded by the MAN1A1 gene.

Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene.

Beta-1,4-galactosyltransferase 4 is an enzyme that in humans is encoded by the B4GALT4 gene.

β-Mannosidase is an enzyme with systematic name β-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene. This enzyme catalyses the following chemical reaction

Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B is an enzyme that in humans is encoded by the MGAT5B gene.

Beta-1,4-galactosyltransferase 3 is an enzyme that in humans is encoded by the B4GALT3 gene.

Beta-1,3-galactosyltransferase 4 is an enzyme that in humans is encoded by the B3GALT4 gene.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB is an enzyme that in humans is encoded by the MAN1A2 gene.

Cytosolic beta-glucosidase, also known as cytosolic beta-glucosidase-like protein 1, is a beta-glucosidase enzyme that in humans is encoded by the GBA3 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000070610 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028467 - 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.
↑ Matern H, Boermans H, Lottspeich F, Matern S (Oct 2001). "Molecular cloning and expression of human bile acid beta-glucosidase". J Biol Chem. 276 (41): 37929–33. doi: 10.1074/jbc.M104290200 . PMID 11489889.
1 2 "Entrez Gene: GBA2 glucosidase, beta (bile acid) 2".

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000070610 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028467 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11489889-5] Matern H, Boermans H, Lottspeich F, Matern S (Oct 2001). "Molecular cloning and expression of human bile acid beta-glucosidase". J Biol Chem. 276 (41): 37929–33. doi: 10.1074/jbc.M104290200 . PMID 11489889.

[entrez-6] 1 2 "Entrez Gene: GBA2 glucosidase, beta (bile acid) 2".

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[5]

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

GBA2

Contents

Function

See also

Related Research Articles

References

Further reading