ID   C3390_DROME             Reviewed;         948 AA.
AC   Q7KT91; B5RIG1; Q29R22; Q95TX3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Non-lysosomal glucosylceramidase;
DE            Short=NLGase;
DE            EC=3.2.1.45;
GN   ORFNames=CG33090;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-948.
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-667 AND SER-669, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the
CC       conversion of glucosylceramide to free glucose and ceramide.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL13692.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL13692.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=ABC86280.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE014134; AAO41192.2; -; Genomic_DNA.
DR   EMBL; BT024218; ABC86280.1; ALT_FRAME; mRNA.
DR   EMBL; BT044085; ACH92150.1; -; mRNA.
DR   EMBL; AY058463; AAL13692.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_788055.2; NM_176041.2.
DR   AlphaFoldDB; Q7KT91; -.
DR   SMR; Q7KT91; -.
DR   BioGRID; 60860; 1.
DR   STRING; 7227.FBpp0080197; -.
DR   CAZy; GH116; Glycoside Hydrolase Family 116.
DR   GlyGen; Q7KT91; 5 sites.
DR   iPTMnet; Q7KT91; -.
DR   PaxDb; 7227-FBpp0080197; -.
DR   DNASU; 34835; -.
DR   EnsemblMetazoa; FBtr0080624; FBpp0080197; FBgn0028916.
DR   GeneID; 34835; -.
DR   KEGG; dme:Dmel_CG33090; -.
DR   UCSC; CG33090-RB; d. melanogaster.
DR   AGR; FB:FBgn0028916; -.
DR   FlyBase; FBgn0028916; CG33090.
DR   VEuPathDB; VectorBase:FBgn0028916; -.
DR   eggNOG; KOG2119; Eukaryota.
DR   GeneTree; ENSGT00390000010998; -.
DR   InParanoid; Q7KT91; -.
DR   OMA; HDLGAPN; -.
DR   OrthoDB; 997839at2759; -.
DR   PhylomeDB; Q7KT91; -.
DR   Reactome; R-DME-9840310; Glycosphingolipid catabolism.
DR   BioGRID-ORCS; 34835; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34835; -.
DR   PRO; PR:Q7KT91; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0028916; Expressed in second segment of antenna (Drosophila) and 34 other cell types or tissues.
DR   ExpressionAtlas; Q7KT91; baseline and differential.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046527; F:glucosyltransferase activity; ISS:FlyBase.
DR   GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IEA:InterPro.
DR   GO; GO:0016139; P:glycoside catabolic process; ISS:UniProtKB.
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; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q7KT91; DM.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW   Membrane; Phosphoprotein; Reference proteome; Sphingolipid metabolism;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..948
FT                   /note="Non-lysosomal glucosylceramidase"
FT                   /id="PRO_0000283761"
FT   TOPO_DOM        1..736
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        737..753
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        754..948
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          177..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   948 AA;  108291 MW;  095184C4EC0F0DD7 CRC64;
     MAEPLAVETK PLSNGNANGN AVGIAESASA VFQEKLKLQQ QEESNEIAAV PKYGLKLKFD
     HVWPEKRIQN VRASIRQTLP MVPLVCRYAA YYWKVSREGR RVYMDYYYME NGKQIYGVPI
     GGIGGGTIGR GYAGEFCRFQ MRPGIYEYNV VLANQFIVTI KDPKGCTIFQ SLLSKCSTRD
     KTSDPDGDPD GERTKCQLPN CSSRAKQPLS AWHSNIEDTR CSYTGLYPRS WTEYDLSHYG
     VRLTCRQVSP VIPHEYRESS LPCAVFVWSV ENVCDQERKV SITFTFKNGT GNKKQDAEGG
     AESQLISEGN AKGVSIRQKI SEMPCSYNLA CRVLPEISIT RCPQFDPAGN GEQLWAQLKE
     HGQLSEHPTS EALKTKDIGV AVCGQVALKP MASHDLEFVL AWDMPKIQFP RKMQTHTRYY
     TKYFDDSGDS GPRICEYALR QYSTWERLID AWQRPILNDE TLPDWYKCAI FNQLYFISDG
     GTIWLKCDSS LGKELAYDDP RLAYGRFGYL EGHEYRMYNT YDVHFYASPA LAHLWPNLQV
     SLQYDFKDAI AAELNDTRKM LYDGKVMPRK VKNCVPHDLG DPDEEPFTLI NCYNIHDVND
     WKDLNTKFVL QVYRDYYVLN ELAQAQSDNA SKFSSIEFID KESLYELYSQ DNKRKNSADE
     KQQNRKSASM YINETNGKVY LMDAIGYLKA MYASCKAIME RTIEYDKDND GLIENTKMPD
     QTYDSWVMDG PSAYCSGLWL AALQAMSAMA TILDQPNDCL RYQDILEKGK RSLEEKLWNG
     SYYRFDLSHS HRDTIMADQL CGHWYLKSCG FDYEIYPKEN VRTALKRIYD NNVMGFHEGN
     IGAANGFIAN ASEPTKPGHV DNSNIQAEEV WPGVVYALAA TMIQEGMFEE AFQTAGGMYK
     TLSQRIGMNF ETPEALYGEK RYRSIGYMRP LSIWSMQVAL ERRRAQRD
//