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Reviewed, UniProtKB/Swiss-Prot Q9VA70 (NCASE_DROME)

Last modified November 3, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Neutral ceramidase
      Short name=N-CDase
      Short name=NCDase
    EC=3.5.1.23
Alternative name(s):
    Neutral acylsphingosine deacylase
    Neutral N-acylsphingosine amidohydrolase
    Slug-a-bed protein
Gene names
Name: CDase
Synonyms: slab
ORF Names: CG1471
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-7.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Regulates synaptic vesicle exocytosis and trafficking by controlling presynaptic terminal sphingolipid composition. Ref.6

Catalytic activity

N-acylsphingosine + H2O = a carboxylate + sphingosine. Ref.1

Subcellular location

Secreted. Ref.1

Tissue specificity

Widely expressed in different tissues but enriched in neurons at all stages of development. Ref.6

Post-translational modification

N-glycosylated. Ref.1

Miscellaneous

Overexpression rescues retinal degeneration in arrestin and phospholipase C mutants, probably by facilitating membrane turnover and endocytosis of rhodopsin in photoreceptors.

Sequence similarities

Belongs to the neutral ceramidase family.

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Ontologies

Keywords
   Biological processLipid metabolism
Sphingolipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processceramide catabolic process Ref.1

Inferred from direct assay. Source: UniProtKB

hatching behavior Ref.6

Inferred from mutant phenotype. Source: FlyBase

synaptic vesicle fusion to presynaptic membrane Ref.6

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentcytoplasm Ref.6

Inferred from direct assay. Source: FlyBase

extracellular region Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionceramidase activity Ref.1 Ref.5

Inferred from direct assay. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

par-6O971111EBI-98235,EBI-186645

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 704681Neutral ceramidase
PRO_0000247106

Sites

Active site2761Nucleophile By similarity

Amino acid modifications

Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis2641V → M in slab1; induces embryonic lethality. Ref.6
Sequence conflict211V → A in BAC77635. Ref.1
Sequence conflict211V → A in AAO42635. Ref.4
Sequence conflict3431R → L in BAC77635. Ref.1
Sequence conflict3761I → V in BAC77635. Ref.1
Sequence conflict6461V → I in BAC77635. Ref.1
Sequence conflict6461V → I in AAO42635. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q9VA70-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E65F61DF1AC2E455

FASTA70478,232
        10         20         30         40         50         60 
MANSKMAFLA FLAVSFLCGL VSATYKVGVG RADITGPPVE INFMGYANIK QVGRGIHTRV 

        70         80         90        100        110        120 
FARAFVVEDE KGNRVAFVSA DAGMMGYGLK REVIKRLQAR YGNIYHNDNV AISGTHTHGA 

       130        140        150        160        170        180 
PGGFLMHLLY DISILGFVPQ TFEVMAQGLY LCIKRATDNL VDGRILLSKT TVLNVNINRS 

       190        200        210        220        230        240 
PSSYLRNPAE ERAQYEHDTD KTLTQLRFVD LENNLLGAFN WYAVHATSMN NTNRLVTSDN 

       250        260        270        280        290        300 
VGYAALLLEK EYNPNKMPGK GKFVGAFCSS NLGDVSPNIM GPKCSISGNE CDLLTSRCPT 

       310        320        330        340        350        360 
GEGDCFASGP GKDMFESTQI LGQRLADAAL GLLNEQSQES TAREVTGDVR FIHQFVDMPN 

       370        380        390        400        410        420 
YNGSTYNPLS RKVDKIRGCQ PAMGYSFAAG TTDGPGAFSF EQGTTTDNPM WNFVRDFIAA 

       430        440        450        460        470        480 
PTQEDIKCHE PKPILLATGR ATFPYEWQPK IVSDQLLKIG DVIIAAVPCE FTTMAGRRLR 

       490        500        510        520        530        540 
NQIRAAASAV GGIDTEVIIA GLTNIYTSYT VTPEEYQAQR YEAASTIFGP HTHSIYMDVF 

       550        560        570        580        590        600 
ERLTKAMMRN ETVDAGPSPP YMNDVMLSLN TGVLFDGHPI NTDFGYVKSQ PNKEYGINET 

       610        620        630        640        650        660 
VKVTYISGNP RNNLFTEKTY FTIERKINED RWKVAYTDAS WETKMVWHRT NTILGFSEMD 

       670        680        690        700 
IYWDISPQTL PGEYRIRHSG EYKYILGGKY PYEGLTHSFT VKED

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a secretory neutral ceramidase of Drosophila melanogaster."
Yoshimura Y., Okino N., Tani M., Ito M.
J. Biochem. 132:229-236(2002) [PubMed: 12153720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
Tissue: Imaginal disk.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Modulating sphingolipid biosynthetic pathway rescues photoreceptor degeneration."
Acharya U., Patel S., Koundakjian E., Nagashima K., Han X., Acharya J.K.
Science 299:1740-1743(2003) [PubMed: 12637747] [Abstract]
Cited for: OVEREXPRESSION.
[6]"Ceramidase regulates synaptic vesicle exocytosis and trafficking."
Rohrbough J., Rushton E., Palanker L., Woodruff E. III, Matthies H.J.G., Acharya U., Acharya J.K., Broadie K.
J. Neurosci. 24:7789-7803(2004) [PubMed: 15356190] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF VAL-264.
[7]"Ceramidase expression facilitates membrane turnover and endocytosis of rhodopsin in photoreceptors."
Acharya U., Mowen M.B., Nagashima K., Acharya J.K.
Proc. Natl. Acad. Sci. U.S.A. 101:1922-1926(2004) [PubMed: 14769922] [Abstract]
Cited for: OVEREXPRESSION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB112076 mRNA. Translation: BAC77635.1.
AE014297 Genomic DNA. Translation: AAN14231.1.
BT004471 mRNA. Translation: AAO42635.1.
RefSeqNP_651797.1.
NP_733367.1.
NP_733368.1.
NP_733369.1.
NP_733370.1.
UniGeneDm.16294

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9VA70. 1 interaction.
STRINGQ9VA70.

Proteomic databases

PRIDEQ9VA70.

Genome annotation databases

EnsemblFBtr0085645; FBpp0085007; FBgn0039774; Drosophila melanogaster. [Genome view]
GeneID43618.
KEGGdme:Dmel_CG1471.
UCSCCG1471-RA. d. melanogaster.

Organism-specific databases

CTD43618.
FlyBaseFBgn0039774. CDase.

Phylogenomic databases

OMALNFTQGT.

Enzyme and pathway databases

BRENDA3.5.1.23. 48.

Gene expression databases

ArrayExpressQ9VA70.
GermOnlineCG1471. Drosophila melanogaster.

Family and domain databases

InterProIPR006823. Ceramidase_alk.
[Graphical view]
PANTHERPTHR12670. Ceramidase_alk. 1 hit.
PfamPF04734. Ceramidase_alk. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio834880.

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Entry information

Entry nameNCASE_DROME
AccessionPrimary (citable) accession number: Q9VA70
Secondary accession number(s): Q7YTD8, Q86NP1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents