GBA2
entrez
57704
canonical
uniprot
Q9HCG7
canonical
ensembl
ENSG00000070610
resolver
ensp
ENSP00000367334
resolver
ensp
ENSP00000367343
resolver
ensp
ENSP00000550951
resolver
ensp
ENSP00000601132
resolver
genesymbol
GBA2
resolver
genesymbol_syn
KIAA1605
resolver
genesymbol_syn
SPG46
resolver
hgnc
HGNC:18986
resolver
uniprot
D3DRP2
resolver
uniprot
Q5TCV6
resolver
uniprot
Q96A51
resolver
uniprot
Q96LY1
resolver
uniprot
Q96SJ2
resolver
uniprot
Q9H2L8
resolver
uniprot_entry
GBA2_HUMAN
resolver
uniprot_sec
D3DRP2
resolver
uniprot_sec
Q5TCV6
resolver
uniprot_sec
Q96A51
resolver
uniprot_sec
Q96LY1
resolver
uniprot_sec
Q96SJ2
resolver
uniprot_sec
Q9H2L8
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by AMP-DMN/N -((5-adamantane-1-yl-methoxy)pentyl)-deoxynojirimycin (PubMed:11489889, PubMed:30308956). Activated by Mn(2+), Co(2+) and Mg(2+) and inhibited by Zn(2+) (PubMed:11489889). Enzymatic activity is dependent on membrane association and requires the presence of lipids (PubMed:11489889). The membrane-associated enzyme is not inhibited by condutiriol B epoxide and bromocondutiriol B epoxide (PubMed:11489889). {ECO:0000269|PubMed:11489889, ECO:0000269|PubMed:30308956}.
uniprot
proteins
amino_acid_sequence
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCCNPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLRYLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMYQHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQLPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDDAPGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQQVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFGAKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSALFNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVHFYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDDEPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDKDHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILSRGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVRALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWEGFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASWPKVKQGTGLRTGPMFGPKEAMANLSPE
uniprot
proteins
disease_involvement
DISEASE: Spastic paraplegia 46, autosomal recessive (SPG46) [MIM:614409]: A neurodegenerative disorder characterized by onset in childhood of slowly progressive spastic paraplegia and cerebellar signs. Some patients have cognitive impairment, cataracts, and cerebral, cerebellar, and corpus callosum atrophy on brain imaging. {ECO:0000269|PubMed:23332916, ECO:0000269|PubMed:23332917, ECO:0000269|PubMed:24252062, ECO:0000269|PubMed:26220345, ECO:0000269|PubMed:30308956}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.1.-
uniprot
proteins
ec_number
3.2.1.-
uniprot
proteins
ec_number
3.2.1.45
uniprot
proteins
ec_number
3.2.1.46
uniprot
proteins
function
FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as N-acylsphing-4-enine) (PubMed:17105727, PubMed:30308956, PubMed:32144204). GlcCers are membrane glycosphingolipids that have a wide intracellular distribution (By similarity). They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties (By similarity). Involved in the transglucosylation of cholesterol, transfers glucose from GlcCer to cholesterol, thereby modifying its water solubility and biological properties (PubMed:32144204). Under specific conditions, may catalyze the reverse reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to ceramide (such as N-acylsphing-4-enine) (Probable). May play a role in the metabolism of bile acids (PubMed:11489889, PubMed:17080196, PubMed:9111029). Able to hydrolyze bile acid 3-O-glucosides as well as to produce bile acid-glucose conjugates thanks to a bile acid glucosyl transferase activity (PubMed:11489889, PubMed:17080196, PubMed:9111029). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers (PubMed:32144204). {ECO:0000250|UniProtKB:Q69ZF3, ECO:0000269|PubMed:11489889, ECO:0000269|PubMed:17080196, ECO:0000269|PubMed:17105727, ECO:0000269|PubMed:30308956, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:9111029, ECO:0000305|PubMed:32144204}.
uniprot
proteins
mass_dalton
104649
uniprot
proteins
mutagenesis
MUTAGEN 419; /note="F->V: Loss of glucosylceramide catabolic process."; /evidence="ECO:0000305|PubMed:26220345
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:17080196, ECO:0000269|PubMed:30308956, ECO:0000305|PubMed:32144204}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000305|PubMed:32144204}.
uniprot
proteins
protein_family
Non-lysosomal glucosylceramidase family
uniprot
proteins
pubmed
10997877
uniprot
proteins
pubmed
11489889
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17080196
uniprot
proteins
pubmed
17105727
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
23332916
uniprot
proteins
pubmed
23332917
uniprot
proteins
pubmed
24252062
uniprot
proteins
pubmed
26220345
uniprot
proteins
pubmed
30308956
uniprot
proteins
pubmed
32144204
uniprot
proteins
pubmed
9111029
uniprot
proteins
sequence_length
927
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q69ZF3}; Peripheral membrane protein {ECO:0000269|PubMed:11489889}; Cytoplasmic side {ECO:0000250|UniProtKB:Q69ZF3}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q69ZF3}; Peripheral membrane protein {ECO:0000269|PubMed:11489889}; Cytoplasmic side {ECO:0000250|UniProtKB:Q69ZF3}. Note=Localization to the plasma membrane and alternative topologies have also been reported. {ECO:0000269|PubMed:11489889, ECO:0000269|PubMed:17105727}.
uniprot
proteins