ID A0A0Q9W6A9_DROVI Unreviewed; 934 AA.
AC A0A0Q9W6A9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 29.
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=Dvir\GJ18180 {ECO:0000313|EMBL:KRF77831.1};
GN ORFNames=Dvir_GJ18180 {ECO:0000313|EMBL:KRF77831.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF77831.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:KRF77831.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase family.
CC {ECO:0000256|PIRNR:PIRNR028944}.
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DR EMBL; CH940654; KRF77831.1; -; Genomic_DNA.
DR RefSeq; XP_015025279.1; XM_015169793.1.
DR AlphaFoldDB; A0A0Q9W6A9; -.
DR EnsemblMetazoa; FBtr0442428; FBpp0398901; FBgn0205345.
DR GeneID; 6634135; -.
DR OrthoDB; 997839at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Glycosidase {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:UP000008792}.
FT DOMAIN 128..431
FT /note="Glycosyl-hydrolase family 116 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12215"
FT DOMAIN 491..922
FT /note="Glycosyl-hydrolase family 116 catalytic region"
FT /evidence="ECO:0000259|Pfam:PF04685"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 106796 MW; 81F80A93BEF74C85 CRC64;
MATPTAATEA TTTTTTIANG NAASAADSAS GVYAEQLQQE KKQEQEPELE QAGEPNELTA
VPRFGLKLKF DHVWPEKRNQ NLRPSIKQSL PMVPLVCRYA AYYWKVSREG RRVYMDYYYM
ENGKQIYGVP IGGIGGGSIG RGYAGEFCRF QMRPGIYEYN VVHANQFIVT IKDHKGCTIF
QSLLSRCSSR PRQPLSAWHS NIEDSRCSYT GLYPRAWTEY DLSHYGVRLI CRQISPVIPH
DYKESSLPCA VFVWSVQNVC DQERKVSITF TFKNGTGNKK QDADGNAESQ LISEGNAKGV
AIRQNIADMP CSYNLACRVL PEISITRCPQ FDPAGNGEQL WAQLKEHGQL SEQPTAETLR
SKDIGVAVCA QLALKPQAYH ELEFVLAWDM PKIQFPRKLQ THTRYYTKYF DDSGESGPRI
CEYALKHYAS WERLIDAWQR PILNDDGLPD WYKCAIFNQL YFISDGGTIW LKCDSSLGQS
LAFDDPRLAY GRFGYLEGHE YRMYNTYDVH FYASPALAHL WPNLQVSLQY DFKDAIAAEL
NDTRKMLYDG KVMPRKVKNC VPHDLGDPDE EPFTLINCYN IHDVNDWKDL NTKFVLQVYR
DYYVLNELAQ AQADNASKFS SIEFIDKESL YELYTQDNKR KNSAEEKQQN RKSASMYINE
TNGKVYLMDA MGYLKAMYGA CKAIMERTIE YDKDNDGLIE NTKMPDQTYD SWVMDGPSAY
CAGLWLAALQ TMSVMATLLD QPNDCLRYQD ILEKGKHSLE EKLWNGSYYR FDLSHNHRDT
IMADQLCGHW YLKSCGFDYE IYPKENVRTA LKRIYDNNVM GFHEGNIGAA NGFIANASEP
SKPGHVDNSN IQAEEVWPGV VYALAATMIQ EGMFEEAFQT AGGMYKTISQ RIGMNYETPE
ALYGEKRYRS IGYMRPLSIW SMQVAWERRR ALRD
//
