GBA3
entrez
57733
canonical
uniprot
Q9H227
canonical
ensembl
ENSG00000249948
resolver
ensembl
ENSG00000291927
resolver
genesymbol
GBA3
resolver
genesymbol_syn
CBG
resolver
genesymbol_syn
CBGL1
resolver
hgnc
HGNC:19069
resolver
uniprot
A8K9N1
resolver
uniprot
B7Z536
resolver
uniprot
Q32LY7
resolver
uniprot
Q3MIH4
resolver
uniprot
Q53GG8
resolver
uniprot
Q6NSF4
resolver
uniprot
Q8NHT8
resolver
uniprot
Q9H3T4
resolver
uniprot
Q9H4C6
resolver
uniprot_entry
A8K9N1_HUMAN
resolver
uniprot_entry
B7Z536_HUMAN
resolver
uniprot_entry
GBA3_HUMAN
resolver
uniprot_sec
Q32LY7
resolver
uniprot_sec
Q3MIH4
resolver
uniprot_sec
Q53GG8
resolver
uniprot_sec
Q6NSF4
resolver
uniprot_sec
Q8NHT8
resolver
uniprot_sec
Q9H3T4
resolver
uniprot_sec
Q9H4C6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside (PubMed:11784319). Inhibited by sodium taurocholate (PubMed:11389701). Inhibited by alpha-1-C-nonyl-DIX/AnDIX (PubMed:20728381). The glucosylceramidase activity is slightly inhibited by conduritol B epoxide/CBE while the galactosylceramidase activity is not (PubMed:17595169). {ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319, ECO:0000269|PubMed:17595169, ECO:0000269|PubMed:20728381}.
uniprot
proteins
amino_acid_sequence
MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYYNKIIDDLLKNGVTPIVTLYHFDLPQTLEDQGGWLSEAIIESFDKYAQFCFSTFGDRVKQWITINEANVLSVMSYDLGMFPPGIPHFGTGGYQAAHNLIKAHARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQEAAKRAITFHLDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGTADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVPWGVCKLLKYIKDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQELFKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL
uniprot
proteins
ec_number
3.2.1.21
uniprot
proteins
ec_number
3.2.1.45
uniprot
proteins
ec_number
3.2.1.46
uniprot
proteins
function
FUNCTION: Neutral cytosolic beta-glycosidase with a broad substrate specificity that could play a role in the catabolism of glycosylceramides (PubMed:11389701, PubMed:11784319, PubMed:17595169, PubMed:20728381, PubMed:26724485, PubMed:33361282). Has a significant glucosylceramidase activity in vitro (PubMed:17595169, PubMed:26724485). However, that activity is relatively low and its significance in vivo is not clear (PubMed:17595169, PubMed:20728381, PubMed:26724485). Hydrolyzes galactosylceramides/GalCers, glucosylsphingosines/GlcSphs and galactosylsphingosines/GalSphs (PubMed:17595169). However, the in vivo relevance of these activities is unclear (PubMed:17595169). It can also hydrolyze a broad variety of dietary glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro and could therefore play a role in the metabolism of xenobiotics (PubMed:11784319). Possesses transxylosylase activity in vitro using xylosylated ceramides/XylCers (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) as xylosyl donors and cholesterol as acceptor (PubMed:33361282). Could also play a role in the catabolism of cytosolic sialyl free N-glycans (PubMed:26193330). {ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319, ECO:0000269|PubMed:17595169, ECO:0000269|PubMed:20728381, ECO:0000269|PubMed:26193330, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:33361282}.
uniprot
proteins
mass_dalton
53696
uniprot
proteins
mutagenesis
MUTAGEN 165; /note="E->D: 2-fold decreased glucosylceramidase activity."; /evidence="ECO:0000269|PubMed:17595169, ECO:0000269|PubMed:18662675"; MUTAGEN 165; /note="E->Q: Loss of glucosylceramidase activity."; /evidence="ECO:0000269|PubMed:17595169, ECO:0000269|PubMed:18662675"; MUTAGEN 168; /note="V->Y: No change in temperature or pH dependence. Decreased glucosidase activity."; /evidence="ECO:0000269|PubMed:12667141"; MUTAGEN 225; /note="F->S: Decreased glucosidase activity."; /evidence="ECO:0000269|PubMed:12667141"; MUTAGEN 308; /note="Y->F,A: Decreased glucosidase activity."; /evidence="ECO:0000269|PubMed:12667141"; MUTAGEN 373; /note="E->D: 2-fold decreased glucosylceramidase activity."; /evidence="ECO:0000269|PubMed:17595169"; MUTAGEN 373; /note="E->Q: Loss of glucosylceramidase activity."; /evidence="ECO:0000269|PubMed:17595169
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:11784319}.
uniprot
proteins
protein_family
Glycosyl hydrolase 1 family
uniprot
proteins
protein_family
Klotho subfamily
uniprot
proteins
pubmed
11043382
uniprot
proteins
pubmed
11389701
uniprot
proteins
pubmed
11784319
uniprot
proteins
pubmed
12594539
uniprot
proteins
pubmed
12667141
uniprot
proteins
pubmed
15322500
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17555766
uniprot
proteins
pubmed
17595169
uniprot
proteins
pubmed
18662675
uniprot
proteins
pubmed
20728381
uniprot
proteins
pubmed
26193330
uniprot
proteins
pubmed
26724485
uniprot
proteins
pubmed
33361282
uniprot
proteins
sequence_length
469
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12594539, ECO:0000269|PubMed:17595169}.
uniprot
proteins