ID A0A2I2YDR7_GORGO Unreviewed; 915 AA.
AC A0A2I2YDR7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Non-lysosomal glucosylceramidase {ECO:0000256|PIRNR:PIRNR028944};
DE Short=NLGase {ECO:0000256|PIRNR:PIRNR028944};
DE EC=3.2.1.45 {ECO:0000256|PIRNR:PIRNR028944};
GN Name=GBA2 {ECO:0000313|Ensembl:ENSGGOP00000033073.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000033073.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000033073.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000033073.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000033073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the
CC hydrolysis of glucosylceramide (GlcCer) to free glucose and ceramide.
CC {ECO:0000256|PIRNR:PIRNR028944}.
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|PIRNR:PIRNR028944};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR028944}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028944}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR028944}. Golgi apparatus membrane
CC {ECO:0000256|PIRNR:PIRNR028944}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028944}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR028944}. Note=Localization to the plasma
CC membrane and alternative topologies have also been reported.
CC {ECO:0000256|PIRNR:PIRNR028944}.
CC -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase family.
CC {ECO:0000256|PIRNR:PIRNR028944}.
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DR EMBL; CABD030062876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2YDR7; -.
DR Ensembl; ENSGGOT00000042290.1; ENSGGOP00000033073.1; ENSGGOG00000007356.3.
DR GeneTree; ENSGT00390000010998; -.
DR Proteomes; UP000001519; Chromosome 9.
DR Bgee; ENSGGOG00000007356; Expressed in frontal cortex and 6 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006680; P:glucosylceramide catabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR014551; B_Glucosidase_GBA2-typ.
DR InterPro; IPR006775; GH116_catalytic.
DR InterPro; IPR024462; GH116_N.
DR PANTHER; PTHR12654; BILE ACID BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR12654:SF0; NON-LYSOSOMAL GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF04685; DUF608; 1.
DR Pfam; PF12215; Glyco_hydr_116N; 1.
DR PIRSF; PIRSF028944; Beta_gluc_GBA2; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR028944};
KW Glycosidase {ECO:0000256|PIRNR:PIRNR028944};
KW Golgi apparatus {ECO:0000256|PIRNR:PIRNR028944};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR028944};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR028944};
KW Membrane {ECO:0000256|PIRNR:PIRNR028944};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 151..455
FT /note="Glycosyl-hydrolase family 116 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12215"
FT DOMAIN 551..874
FT /note="Glycosyl-hydrolase family 116 catalytic region"
FT /evidence="ECO:0000259|Pfam:PF04685"
FT REGION 32..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102544 MW; 7FFBF9C762D3179A CRC64;
MGTHDPGNMG TGVPASEQIS CAKEDPQVYC PEETGSTKDV QVTDCKSPED SRPQKETDCC
NPEDSGQLMA SYEGKAMGYQ VPPFGWRICL AHEFTEKRKP FQANNVSLSN MIKHIGMGLR
YLQWWYRKTQ VEKKTPFIDM INSVPLRQIY GCPLGGIGGG TITRGWRGQF CRWQLNPGMY
QHRTVIADQF TVCLRREGQT VYQQVLSLER PSVLRTWNWG LCGYFAFYHA LYPRAWTVYQ
LPGQNVTLTC RQITPILPHD YQDSSLPVGV FVWDVENEGD EALDVSIMFS MRNGLGGGDD
APGGLWNEPF CLERSGETVR GLLLHHPTLP NPYTMAVAAR VTADTTVTHI TAFDPDSTGQ
QVWQDLLQDG QLDSPTGQST PTQKGVGIAG AVCVSSKLRP RGQCRLEFSL AWDMPRIMFG
AKGQVHYRRY TRFFGQDGDA APALSHYALC RYAEWEERIS AWQSPVLDDR SLPAWYKSAL
FNELYFLADG GTVWLEVLED SLPEELGRNM CHLRPTLRDY GRFGYLEGTG SVCPSSGMPI
PCLPSVSAPP ALATLREDLT RRRYLMSGVM APVKRRNVIP HDIGDPDDEP WLRVNAYLIH
DTADWKDLNL KFVLQVYRDY YLTGDQNFLK DMWPVCLAVM ESEMKFDKDH DGLIENGGYA
DQTYDGWVTT GPSAYCGGLW LAAVAVMVQM AALCGAQDIQ DKFSSILSRG QEAYERLLWN
GRYYNYDSSS RPQSRSVMSD QCAGQWFLKA CGLGEGDTEV FPTQHVVRAL QTIFELNVQA
FAGGAMGAVN GMQPHGVPDK SSVQSDEVWV GVVYGLAATM IQEGLTWEGF QTAEGCYRTV
WERLGLAFQT PEAYCQQRVF RSLAYMRPLS IWAMQLALQQ QQHKKASWPK VEQGTGLRTG
PMFGPKEAMA NLSPE
//
