C3390_DROME
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 03-AUG-2022, entry version 124.
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; Q7KT91; -.
DR DNASU; 34835; -.
DR EnsemblMetazoa; FBtr0080624; FBpp0080197; FBgn0028916.
DR GeneID; 34835; -.
DR KEGG; dme:Dmel_CG33090; -.
DR UCSC; CG33090-RB; d. melanogaster.
DR FlyBase; FBgn0028916; CG33090.
DR VEuPathDB; VectorBase:FBgn0028916; -.
DR eggNOG; KOG2119; Eukaryota.
DR GeneTree; ENSGT00390000010998; -.
DR InParanoid; Q7KT91; -.
DR OrthoDB; 207392at2759; -.
DR PhylomeDB; Q7KT91; -.
DR Reactome; R-DME-1660662; Glycosphingolipid metabolism.
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 tissues.
DR ExpressionAtlas; Q7KT91; baseline and differential.
DR Genevisible; Q7KT91; DM.
DR GO; GO:0016021; C:integral component of 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 Pfam; PF04685; DUF608; 1.
DR Pfam; PF12215; Glyco_hydr_116N; 1.
DR PIRSF; PIRSF028944; Beta_gluc_GBA2; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
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
