Gba2
entrez
230101
canonical
uniprot
Q69ZF3
canonical
ensembl
ENSMUSG00000028467
resolver
ensp
ENSMUSP00000030189
resolver
enst
ENSMUST00000030189
resolver
genesymbol
Gba2
resolver
genesymbol_syn
Kiaa1605
resolver
uniprot
Q6PGM3
resolver
uniprot
Q8BTN9
resolver
uniprot_entry
GBA2_MOUSE
resolver
uniprot_sec
Q6PGM3
resolver
uniprot_sec
Q8BTN9
resolver
activity_regulation
ACTIVITY REGULATION: Enzymatic activity is dependent on membrane association and requires the presence of lipids (PubMed:23250757). Inhibited by N-(adamantanemethyloxypentyl)-deoxynojirimycin/AMP-DNM (PubMed:26724485). Inhibited by its product sphingosine/N-acylsphing-4-enine in a feedback loop (PubMed:28258214). Also inhibited by other non-acetylated sphingoid bases and their derivatives but not by sphingosine-1-phosphate and complex sphingolipids (PubMed:28258214). {ECO:0000269|PubMed:23250757, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:28258214}.
uniprot
proteins
amino_acid_sequence
MVTCVPASEQVGCAERDSQVYCEDTGGTEAVRVTDCGSPEDSGPQDEPSYCNSEDSGQLMASYEGKARGYQVPPFGWRICLAHEFAEKRRPFQANNISLSNLVKHLGMGLRYLKWWYRKTHVEKKTPFIDMLNSLPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMYQHQTVIADQFIVCLRRDGRTVYQQVLSLELPNVLRSWNWGLCGYFAFYHALYPRAWTVYQLPGQNVTLTCRQVTPILPHDYQDSSLPVGVFVWDVENEGDETLDVSITFSMRNGLGGEDDAAGSLWNEPFRLEQGGTTVQGLLLHHPTPPNPYTMAVAARCTADTTVTHTTAFDPNGTGQQVWQDLLQDGQLDSPAGQSTPTQKGEGIAGAVCVSSKLLPRSRCCLEFSLAWDMPKIMFGAKSQVHYRRYTRFFGSDGDVAPALSHYALCHYADWEDRISAWQNPVLDDRTLPAWYKSALFNELYFLADGGTVWLEVPADSLPEGLGGSMRQLRSTLQDYGRFGYLEGQEYRMYNTYDVHFYASFALVMLWPKLELSLQYDMALATLKEDLTRRRYLMSGVVAPVKRRNVIPHDIGDPDDEPWLRVNAYLIHDTADWKDLNLKFVLQIYRDYYLTGDQGFLEDMWPVCLAVMESEMKFDKDQDGLIENGGYADQTYDAWVTTGPSAYCGGLWLAAVAVMVQMAVLCGAQDVQERFASILCRGREAYERLLWNGRYYNYDSSSHPQSRSIMSDQCAGQWFLRACGLGEGDTEVFPTLHVVRALQTIFELNVQAFAGGAMGAVNGMHPHGVPDRSSVQSDEVWVGVVYGLAATMIQEGLTWEGFRTAEGCYRTVWERLGLAFQTPEAYCQQQVFRSLAYMRPLSIWAMQLALQQQQHKKSRRPSVTQGTGLSTQPECGPKRSLANLNSE
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:17080196, PubMed:23250757). GlcCers are membrane glycosphingolipids that have a wide intracellular distribution (PubMed:23250757). They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties (PubMed:25803043). Also involved in the transglucosylation of cholesterol, transferring glucose from GlcCer, thereby modifying its water solubility and biological properties (PubMed:26724485, 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) (PubMed:26724485, PubMed:32144204). May play a role in the metabolism of bile acids (PubMed:17080196). 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:17080196). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers (PubMed:32144204). {ECO:0000269|PubMed:17080196, ECO:0000269|PubMed:23250757, ECO:0000269|PubMed:25803043, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:32144204, ECO:0000303|PubMed:23250757}.
uniprot
proteins
mass_dalton
103294
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:17080196, ECO:0000269|PubMed:23250757, ECO:0000269|PubMed:26724485, ECO:0000305|PubMed:32144204}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:26724485, ECO:0000305|PubMed:32144204}.
uniprot
proteins
protein_family
Non-lysosomal glucosylceramidase family
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17080196
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23250757
uniprot
proteins
pubmed
25803043
uniprot
proteins
pubmed
26724485
uniprot
proteins
pubmed
28258214
uniprot
proteins
pubmed
32144204
uniprot
proteins
sequence_length
918
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23250757}; Peripheral membrane protein {ECO:0000269|PubMed:23250757}; Cytoplasmic side {ECO:0000269|PubMed:23250757}. Golgi apparatus membrane {ECO:0000269|PubMed:23250757}; Peripheral membrane protein {ECO:0000269|PubMed:23250757}; Cytoplasmic side {ECO:0000269|PubMed:23250757}. Note=Localization to the plasma membrane and alternative topologies have also been reported. {ECO:0000250|UniProtKB:Q9HCG7}.
uniprot
proteins