ID H2YMC4_CIOSA Unreviewed; 474 AA.
AC H2YMC4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Glucosylceramidase {ECO:0000256|RuleBase:RU361188};
DE EC=3.2.1.45 {ECO:0000256|RuleBase:RU361188};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000006476.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000006476.1}
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}.
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DR AlphaFoldDB; H2YMC4; -.
DR Ensembl; ENSCSAVT00000006558.1; ENSCSAVP00000006476.1; ENSCSAVG00000003873.1.
DR GeneTree; ENSGT00390000009464; -.
DR HOGENOM; CLU_014379_1_2_1; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000007875; 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:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
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; 1.
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:UP000007875};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sphingolipid metabolism {ECO:0000256|RuleBase:RU361188}.
FT DOMAIN 74..436
FT /note="Glycosyl hydrolase family 30 TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF02055"
FT DOMAIN 439..474
FT /note="Glycosyl hydrolase family 30 beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17189"
SQ SEQUENCE 474 AA; 53186 MW; 53361AD82384C562 CRC64;
QPCAARMFTS DSVVCVCNSS YCDTISEMPA IAIDEALTYT TSKSGDRFKK GSLQFNSGIP
SQGKRFDQIA RVSGGAFTDS AGINIASLSN QVQDHLLRSY FSDEEKLKKH CFVLVTLNTF
KGIGYNMGRI PMASVDFSTR LYTYADTPND FEMKNFSLAP EDFQYKIPYI KKAVEMSNKK
FMLFASPWTA PAWMKTNNAL YGKGGLIGTA GNEYHKAWAL YFSRFLEEYK SNGVAVWGVT
AQNEPIDGLA GNFSFQCMGW TAEQQRDFIK TDLGPTLHSR GHGDVQVIIG DDQRLVFPEW
AHTVLNDQEA AQYVSGIGVH WYMDWILPPT RISDTHKAFP DFFILGTEAC SGAMPFQPDK
VILGSWTRGE RYSQFILEDL NHFVSGWVDW NLALDLEGGP NWVKNFVDAA IIVNAANDEF
YKQPIFYHLG HFSKFLREGA VRISVETQGS DLKDLKHVAF VDKENSTTTL IILN
//
