ID H3DLT2_TETNG Unreviewed; 497 AA.
AC H3DLT2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Glucosylceramidase {ECO:0000256|RuleBase:RU361188};
DE EC=3.2.1.45 {ECO:0000256|RuleBase:RU361188};
GN Name=GBA1 {ECO:0000313|Ensembl:ENSTNIP00000021480.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000021480.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000021480.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(beta-D-galactosyl)-N-dodecanoylsphing-4-enine + cholesterol
CC = cholesteryl 3-beta-D-galactoside + N-dodecanoylsphing-4-enine;
CC Xref=Rhea:RHEA:70255, ChEBI:CHEBI:16113, ChEBI:CHEBI:72956,
CC ChEBI:CHEBI:73432, ChEBI:CHEBI:189066;
CC Evidence={ECO:0000256|ARBA:ARBA00033703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70256;
CC Evidence={ECO:0000256|ARBA:ARBA00033703};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70257;
CC Evidence={ECO:0000256|ARBA:ARBA00033703};
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:0000256|ARBA:ARBA00033698};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298;
CC Evidence={ECO:0000256|ARBA:ARBA00033698};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine +
CC cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-
CC galactoside; Xref=Rhea:RHEA:70235, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:18390, ChEBI:CHEBI:52639, ChEBI:CHEBI:189066;
CC Evidence={ECO:0000256|ARBA:ARBA00033611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70236;
CC Evidence={ECO:0000256|ARBA:ARBA00033611};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70237;
CC Evidence={ECO:0000256|ARBA:ARBA00033611};
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:0000256|ARBA:ARBA00001013};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270;
CC Evidence={ECO:0000256|ARBA:ARBA00001013};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol
CC = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside;
CC Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495,
CC ChEBI:CHEBI:22801, ChEBI:CHEBI:52639;
CC Evidence={ECO:0000256|ARBA:ARBA00033647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58265;
CC Evidence={ECO:0000256|ARBA:ARBA00033647};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58266;
CC Evidence={ECO:0000256|ARBA:ARBA00033647};
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:0000256|ARBA:ARBA00033608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70240;
CC Evidence={ECO:0000256|ARBA:ARBA00033608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1')-N-(15Z-tetracosenoyl)-sphing-4-enine
CC + cholesterol = cholesteryl 3-beta-D-glucoside + N-(15Z-
CC tetracosenoyl)-sphing-4-enine; Xref=Rhea:RHEA:70315,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:74450,
CC ChEBI:CHEBI:76302; Evidence={ECO:0000256|ARBA:ARBA00035592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70316;
CC Evidence={ECO:0000256|ARBA:ARBA00035592};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70317;
CC Evidence={ECO:0000256|ARBA:ARBA00035592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1)-N-octadecanoylsphing-4-enine +
CC cholesterol = cholesteryl 3-beta-D-glucoside + N-octadecanoylsphing-
CC 4-enine; Xref=Rhea:RHEA:70311, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495,
CC ChEBI:CHEBI:72961, ChEBI:CHEBI:84719;
CC Evidence={ECO:0000256|ARBA:ARBA00033636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70312;
CC Evidence={ECO:0000256|ARBA:ARBA00033636};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70313;
CC Evidence={ECO:0000256|ARBA:ARBA00033636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4E-enine +
CC cholesterol = cholesteryl 3-beta-D-glucoside + N-(9Z-octadecenoyl)-
CC sphing-4-enine; Xref=Rhea:RHEA:58324, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:17495, ChEBI:CHEBI:77996, ChEBI:CHEBI:139140;
CC Evidence={ECO:0000256|ARBA:ARBA00033685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58325;
CC Evidence={ECO:0000256|ARBA:ARBA00033685};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58326;
CC Evidence={ECO:0000256|ARBA:ARBA00033685};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-N-dodecanoylsphing-4-enine + cholesterol =
CC cholesteryl 3-beta-D-glucoside + N-dodecanoylsphing-4-enine;
CC Xref=Rhea:RHEA:70307, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495,
CC ChEBI:CHEBI:72956, ChEBI:CHEBI:76297;
CC Evidence={ECO:0000256|ARBA:ARBA00033694};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70308;
CC Evidence={ECO:0000256|ARBA:ARBA00033694};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70309;
CC Evidence={ECO:0000256|ARBA:ARBA00033694};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-N-octanoylsphing-4E-enine + cholesterol =
CC cholesteryl 3-beta-D-glucoside + N-octanoylsphing-4-enine;
CC Xref=Rhea:RHEA:70303, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495,
CC ChEBI:CHEBI:45815, ChEBI:CHEBI:65222;
CC Evidence={ECO:0000256|ARBA:ARBA00033641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70304;
CC Evidence={ECO:0000256|ARBA:ARBA00033641};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70305;
CC Evidence={ECO:0000256|ARBA:ARBA00033641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine +
CC cholesterol = cholesteryl 3-beta-D-xyloside + N-(9Z-octadecenoyl)-
CC sphing-4-enine; Xref=Rhea:RHEA:70251, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:77996, ChEBI:CHEBI:189067, ChEBI:CHEBI:189081;
CC Evidence={ECO:0000256|ARBA:ARBA00033633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70252;
CC Evidence={ECO:0000256|ARBA:ARBA00033633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D-
CC glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17495;
CC Evidence={ECO:0000256|ARBA:ARBA00033646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957;
CC Evidence={ECO:0000256|ARBA:ARBA00033646};
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000256|ARBA:ARBA00004731}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004207}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004207}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004207}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H3DLT2; -.
DR STRING; 99883.ENSTNIP00000021480; -.
DR Ensembl; ENSTNIT00000021715.1; ENSTNIP00000021480.1; ENSTNIG00000018314.1.
DR GeneTree; ENSGT00390000009464; -.
DR HOGENOM; CLU_014379_1_2_1; -.
DR InParanoid; H3DLT2; -.
DR OMA; FGGIAWH; -.
DR TreeFam; TF314254; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004336; F:galactosylceramidase activity; IEA:RHEA.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050295; F:steryl-beta-glucosidase activity; IEA:RHEA.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0036268; P:swimming; IEA:Ensembl.
DR GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR PRINTS; PR00843; GLHYDRLASE30.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361188};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919,
KW ECO:0000256|RuleBase:RU361188}.
FT DOMAIN 78..427
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT DOMAIN 430..492
FT /note="Glycosyl hydrolase family 30 beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17189"
SQ SEQUENCE 497 AA; 55123 MW; B1F3931EC98203C5 CRC64;
ASKCIGRDFG QDSVVCECNS TYCDSVGSIT LPPVGQFSSF LSSMSGSRLE ASQGRVQVNS
TAEGLRFTID LHQKYQKIRG FGGAMTDAAA INILSLSPAT QDQLLRQYFS AEGIGYTVVR
VPMASCDFST RLYTYADTPG DYNLDHFALA PEDVNMKIPL LQRAQAASPR PLSLMASAWS
APAWMKTNGA LTGKGSLKGQ PGGKEHKTWA HYYIRFLEEY AKHNLSFWAL TTGNEPTAGM
MTNYSFQALG FTPREQRDWV SLDLGPAVHA SAFPDTHILI LDDNRLLLPY WAKIVLNDVH
AGRYIHGVAV HWYMDGFVPA EMTLGITHHL YPEYYLFGTE ACAGFSPLDP GVKLGSWQRA
EQYAHDIIED LNHYVVGWTD WNLALDRIGG PNWVKNYVDS AVIVDAQRDV FYKQPTFYSL
AHFSKFLWEG SRRVGVSSNQ KTDLGYSAFV RPDGSVVLIV LNRSSSGVRF EVWDPSVGYI
PATAPAHSLL TLAWKTH
//
