Gba1
entrez
14466
canonical
uniprot
P17439
canonical
ensembl
ENSMUSG00000028048
resolver
ensp
ENSMUSP00000076589
resolver
ensp
ENSMUSP00000130660
resolver
ensp
ENSMUSP00000297800
resolver
ensp
ENSMUSP00000336533
resolver
ensp
ENSMUSP00000357193
resolver
enst
ENSMUST00000077367
resolver
enst
ENSMUST00000167998
resolver
genesymbol
Gba1
resolver
genesymbol_syn
Gba
resolver
uniprot
Q78NR7
resolver
uniprot_entry
GBA1_MOUSE
resolver
uniprot_sec
Q78NR7
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by conduritol B epoxide/CBE. {ECO:0000269|PubMed:24211208}.
uniprot
proteins
amino_acid_sequence
MAARLIGFFLFQAVSWAYGAQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRMELSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPTQKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLPEEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLGFTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEAAKYVHGIAVHWYMDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVTGWTDWNLALNPEGGPNWVRNFVDSPIIVDIPKDAFYKQPMFYHLGHFSKFIPEGSQRVALVASESTDLETVALLRPDGSAVVVVLNRSSEDVPLTISDPDLGFLETVSPGYSIHTYLWRRQ
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: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:24211208). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (By similarity). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (By similarity). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (By similarity). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (By similarity). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (By similarity). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (By similarity). {ECO:0000250|UniProtKB:P04062, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:27378698}.
uniprot
proteins
mass_dalton
57622
uniprot
proteins
pathway_participation
PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208}.; PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:24211208}.
uniprot
proteins
protein_family
Glycosyl hydrolase 30 family
uniprot
proteins
pubmed
1317175
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1594045
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16170054
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22665763
uniprot
proteins
pubmed
24211208
uniprot
proteins
pubmed
27378698
uniprot
proteins
pubmed
2740343
uniprot
proteins
pubmed
27789271
uniprot
proteins
sequence_length
515
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P04062}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04062}; Lumenal side {ECO:0000250|UniProtKB:P04062}. Note=Interaction with saposin-C promotes membrane [?]association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. {ECO:0000250|UniProtKB:P04062}.
uniprot
proteins