ID   NCASE_DROPS             Reviewed;         704 AA.
AC   Q29C43;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Neutral ceramidase;
DE            Short=N-CDase;
DE            Short=NCDase;
DE            EC=3.5.1.23;
DE   AltName: Full=Acylsphingosine deacylase;
DE   AltName: Full=N-acylsphingosine amidohydrolase;
DE   Flags: Precursor;
GN   Name=CDase; ORFNames=GA13191;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC       free fatty acid at an optimal pH of 6.5-7.5. Acts as a key regulator of
CC       sphingolipid signaling metabolites by generating sphingosine at the
CC       cell surface (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC         Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
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DR   EMBL; CM000070; EAL26803.1; -; Genomic_DNA.
DR   RefSeq; XP_015038524.1; XM_015183038.1.
DR   AlphaFoldDB; Q29C43; -.
DR   SMR; Q29C43; -.
DR   STRING; 7237.FBpp0282908; -.
DR   PRIDE; Q29C43; -.
DR   EnsemblMetazoa; FBtr0368768; FBpp0331472; FBgn0073228.
DR   GeneID; 4800384; -.
DR   KEGG; dpo:Dpse_GA13191; -.
DR   eggNOG; KOG2232; Eukaryota.
DR   HOGENOM; CLU_011300_2_0_1; -.
DR   InParanoid; Q29C43; -.
DR   OMA; VWHRTNT; -.
DR   PhylomeDB; Q29C43; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0073228; Expressed in insect adult head and 2 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046514; P:ceramide catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.2300; -; 1.
DR   InterPro; IPR006823; Ceramidase_alk.
DR   InterPro; IPR038445; NCDase_C_sf.
DR   InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR   InterPro; IPR031329; NEUT/ALK_ceramidase_N.
DR   PANTHER; PTHR12670; PTHR12670; 1.
DR   Pfam; PF04734; Ceramidase_alk; 1.
DR   Pfam; PF17048; Ceramidse_alk_C; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid metabolism; Reference proteome; Secreted;
KW   Signal; Sphingolipid metabolism.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..704
FT                   /note="Neutral ceramidase"
FT                   /id="PRO_0000247107"
FT   ACT_SITE        276
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   704 AA;  78092 MW;  6131255E84E15F38 CRC64;
     MAISKIAFLA LIALSGLCGL ASATYKVGVG RADITGPPVE INFMGYANIK QVGRGIHTRV
     FARAFVVEDE KGNRVAFVSA DAGMMGYGLK REVIKRLQAR YGNLYHTDNV AISGTHTHGA
     PGGFLMHLLY DISILGFVPQ TFEVMAQGLY LCIKRATDNL VDGRIFLSKT TVLNVNINRS
     PTSYLRNPEE ERAQYEHDTD KTLTQLRFVD LENNLLGAFN WYAVHATSMN NTNRLVTSDN
     VGYAALLLEK EYNPNKMPGK GKFVGAFCSS NLGDVSPNIM GPKCSISGNE CDLLTSRCPA
     GEGECFASGP GRDMVESTQI LGQRLADAAL GLLNEQSQES TAREVTGDVR FIHQFVDMPN
     YNGSAYNPLS RKIDKIRGCQ PAMGYSFAAG TTDGPGAFSF EQGTTTDNPM WNFVRDFIAT
     PTQEDIKCHE PKPILLATGR ATFPYEWQPK IVSDQLLKIG DVIIAAVPCE FTTMAGRRLR
     NQIRAAASAA GGLDTEVIIA GLTNIYTSYT VTPEEYQAQR YEAASTIFGP HTHSIYMDVF
     ERLTKALMRN ETVEPGPSPP YMNDVMLSLN TGVLFDGHPI NTDFGYVKTQ PEKEYGINDT
     VKVTYISGNP RNNLFTEKTY FTVERKINED RWKVAYTDAS WETKMIWHRT NTILGFSDLE
     IYWNISPQTL PGVYRIRHSG EYKYILGGKY PYEGLSHSFT VKED