Glucocerebrosidase

GBA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1OGS, 1Y7V, 2F61, 2J25, 2NSX, 2NT0, 2NT1, 2V3D, 2V3E, 2V3F, 2VT0, 2WCG, 2WKL, 2XWD, 2XWE, 3GXD, 3GXF, 3GXI, 3GXM, 3KE0, 3KEH, 3RIK, 3RIL
Identifiers
Aliases	GBA, GBA1, GCB, GLUC, glucosylceramidase beta, Glucocerebrosidase
External IDs	OMIM: 606463; MGI: 95665; HomoloGene: 68040; GeneCards: GBA; OMA:GBA - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q22 Start 155,234,452 bp[1] End 155,244,699 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 F1|3 39.01 cM Start 89,110,235 bp[2] End 89,116,273 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium islet of Langerhans placenta blood pituitary gland anterior pituitary bone marrow cells right adrenal gland right adrenal cortex left adrenal gland Top expressed in esophagus internal carotid artery external carotid artery lip stroma of bone marrow superior surface of tongue decidua fossa endothelial cell of lymphatic vessel motor neuron More reference expression data BioGPS More reference expression data
Gene ontology Molecular function hydrolase activity, acting on glycosyl bonds protein binding hydrolase activity signaling receptor binding glucosylceramidase activity Cellular component membrane lysosome extracellular exosome lysosomal lumen lysosomal membrane extracellular space Biological process termination of signal transduction skin morphogenesis glycosphingolipid metabolic process positive regulation of protein dephosphorylation lipid metabolism response to testosterone cellular response to starvation negative regulation of interleukin-6 production response to thyroid hormone ceramide biosynthetic process cellular response to tumor necrosis factor sphingosine biosynthetic process positive regulation of proteolysis involved in cellular protein catabolic process regulation of water loss via skin response to estrogen glucosylceramide catabolic process negative regulation of MAP kinase activity response to pH metabolism negative regulation of inflammatory response regulation of macroautophagy sphingolipid metabolic process mitochondrion organization neuron projection development regulation of cellular protein metabolic process positive regulation of proteasomal ubiquitin-dependent protein catabolic process negative regulation of protein homooligomerization cell death in response to oxidative stress positive regulation of protein-containing complex disassembly regulation of protein metabolic process negative regulation of neuron death positive regulation of protein lipidation positive regulation of neuronal action potential positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization autophagosome organization regulation of lysosomal protein catabolic process beta-glucoside catabolic process response to dexamethasone Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2629 14466 Ensembl ENSG00000262446 ENSG00000177628 ENSMUSG00000028048 UniProt P04062 P17439 RefSeq (mRNA) NM_000157 NM_001005741 NM_001005742 NM_001005749 NM_001005750 NM_001171811 NM_001171812 NM_001077411 NM_008094 RefSeq (protein) NP_000148 NP_001005741 NP_001005742 NP_001165282 NP_001165283 NP_001070879 NP_032120 Location (UCSC) Chr 1: 155.23 – 155.24 Mb Chr 3: 89.11 – 89.12 Mb PubMed search [3] [4]
Wikidata
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β-Glucocerebrosidase (also called acid β-glucosidase, D-glucosyl-N-acylsphingosine glucohydrolase, or GCase) is an enzyme with glucosylceramidase activity (EC 3.2.1.45) that cleaves by hydrolysis the β-glycosidic linkage of the chemical glucocerebroside, an intermediate in glycolipid metabolism that is abundant in cell membranes (particularly skin cells).^[5] It is localized in the lysosome, where it remains associated with the lysosomal membrane.^[6] β-Glucocerebrosidase is 497 amino acids in length and has a molecular mass of 59,700 Da.^{[citation needed]}