GBA3_CAVPO
ID GBA3_CAVPO Reviewed; 469 AA.
AC P97265;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytosolic beta-glucosidase {ECO:0000305};
DE EC=3.2.1.21 {ECO:0000305|PubMed:9657108};
DE AltName: Full=Cytosolic galactosylceramidase {ECO:0000250|UniProtKB:Q9H227};
DE EC=3.2.1.46 {ECO:0000250|UniProtKB:Q9H227};
DE AltName: Full=Cytosolic glucosylceramidase {ECO:0000250|UniProtKB:Q9H227};
DE EC=3.2.1.45 {ECO:0000250|UniProtKB:Q9H227};
DE AltName: Full=Cytosolic glycosylceramidase {ECO:0000250|UniProtKB:Q9H227};
DE Short=Cytosolic GCase {ECO:0000250|UniProtKB:Q9H227};
GN Name=Gba3 {ECO:0000250|UniProtKB:Q9H227};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-41; 46-59; 76-82;
RP 96-102; 204-212; 218-232; 246-260; 270-274; 299-310; 321-335; 390-394 AND
RP 448-454, AND BLOCKAGE OF N-TERMINUS.
RC STRAIN=Dunkin-Hartley; TISSUE=Liver;
RX PubMed=8920987; DOI=10.1042/bj3190829;
RA Hays W.S., Jenison S.A., Yamada T., Pastuszyn A., Glew R.H.;
RT "Primary structure of the cytosolic beta-glucosidase of guinea pig liver.";
RL Biochem. J. 319:829-837(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP ACTIVITY REGULATION.
RX PubMed=9657108; DOI=10.1002/hep.510280121;
RA Hays W.S., Wheeler D.E., Eghtesad B., Glew R.H., Johnston D.E.;
RT "Expression of cytosolic beta-glucosidase in guinea pig liver cells.";
RL Hepatology 28:156-163(1998).
CC -!- FUNCTION: Neutral cytosolic beta-glycosidase with a broad substrate
CC specificity that could play a role in the catabolism of
CC glycosylceramides (Probable). Has a significant glucosylceramidase
CC activity in vitro. However, that activity is relatively low and its
CC significance in vivo is not clear (By similarity). Hydrolyzes
CC galactosylceramide/GalCer, glucosylsphingosine/GlcSph and
CC galactosylsphingosine/GalSph. However, the in vivo relevance of these
CC activities is unclear (By similarity). It can also hydrolyze a broad
CC variety of dietary glycosides including phytoestrogens, flavonols,
CC flavones, flavanones and cyanogens in vitro and could therefore play a
CC role in the metabolism of xenobiotics (Probable). Possesses
CC transxylosylase activity in vitro using xylosylated ceramides/XylCers
CC (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) as xylosyl
CC donors and cholesterol as acceptor (By similarity). Could also play a
CC role in the catabolism of cytosolic sialyl free N-glycans (By
CC similarity). {ECO:0000250|UniProtKB:Q9H227,
CC ECO:0000305|PubMed:9657108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000305|PubMed:9657108};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-
CC acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639; EC=3.2.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an
CC N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390,
CC ChEBI:CHEBI:52639; EC=3.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1)-sphing-4-enine + H2O = D-glucose +
CC sphing-4-enine; Xref=Rhea:RHEA:59288, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:83992;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59289;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1)-N-octadecanoylsphing-4-enine + H2O =
CC D-glucose + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:59284,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:72961,
CC ChEBI:CHEBI:84719; Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59285;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1)-sphing-4-enine + H2O = D-galactose +
CC sphing-4-enine; Xref=Rhea:RHEA:43908, ChEBI:CHEBI:4139,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:57934;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43909;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1')-N-octadecanoylsphing-4-enine + H2O
CC = D-galactose + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:59292,
CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:72961,
CC ChEBI:CHEBI:84720; Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59293;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine + cholesterol =
CC an N-acylsphing-4-enine + cholesteryl 3-beta-D-xyloside;
CC Xref=Rhea:RHEA:70239, ChEBI:CHEBI:16113, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:189067, ChEBI:CHEBI:189068;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70240;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70241;
CC Evidence={ECO:0000250|UniProtKB:Q9H227};
CC -!- ACTIVITY REGULATION: Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-
CC beta-D-glucopyranoside. {ECO:0000269|PubMed:9657108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:9657108}.
CC -!- TISSUE SPECIFICITY: Present in hepatocytes (at protein level).
CC {ECO:0000305|PubMed:9657108}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8920987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
CC subfamily. {ECO:0000305}.
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DR EMBL; U50545; AAB41058.1; -; mRNA.
DR RefSeq; NP_001166590.1; NM_001173119.1.
DR AlphaFoldDB; P97265; -.
DR SMR; P97265; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 100379247; -.
DR KEGG; cpoc:100379247; -.
DR CTD; 57733; -.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; P97265; -.
DR OrthoDB; 408001at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0004348; F:glucosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0017042; F:glycosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901805; P:beta-glucoside catabolic process; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006683; P:galactosylceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0006680; P:glucosylceramide catabolic process; ISS:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1..469
FT /note="Cytosolic beta-glucosidase"
FT /id="PRO_0000063907"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 424..425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 53745 MW; 9ED6B5BA89C22EE6 CRC64;
MAFPADLVGG LPTAAYQVEG GWDADGRGPC VWDTFTHQGG ERVFKNQTGD VACGSYTLWE
EDLKCIKQLG LTHYRFSISW SRLLPDGTTG FINQKGVDYY NKIIDDLLTN GVTPVVTLYH
FDLPQALEDQ GGWLSEAIIE VFDKYAQFCF STFGNRVRQW ITINEPNVLC AMGYDLGFFA
PGVSQIGTGG YQAAHNMIKA HARAWHSYDS LFREKQKGMV SLSLFCIWPQ PENPNSVLDQ
KAAERAINFQ FDFFAKPIFI DGDYPELVKS QIASMSEKQG YPSSRLSKFT EEEKKMIKGT
ADFFAVQYYT TRFIRHKENK EAELGILQDA EIELFSDPSW KGVGWVRVVP WGIRKLLNYI
KDTYNNPVIY ITENGFPQDD PPSIDDTQRW ECFRQTFEEL FKAIHVDKVN LQLYCAWSLL
DNFEWNDGYS KRFGLFHVDF EDPAKPRVPY TSAKEYAKII RNNGLERPQ
