ACASE_DROME
ID ACASE_DROME Reviewed; 283 AA.
AC Q9VIP7; Q8SYZ0; Q8WSF4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Alkaline ceramidase;
DE Short=AlkCDase;
DE EC=3.5.1.23;
DE AltName: Full=Alkaline N-acylsphingosine amidohydrolase;
DE AltName: Full=Alkaline acylsphingosine deacylase;
DE AltName: Full=Protein brainwashing;
GN Name=bwa; ORFNames=CG13969;
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 [MRNA].
RA Pascual A., Boquet I., Preat T.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10623899;
RX DOI=10.1002/(sici)1097-4695(200001)42:1<33::aid-neu4>3.0.co;2-t;
RA Boquet I., Hitier R., Dumas M., Chaminade M., Preat T.;
RT "Central brain postembryonic development in Drosophila: implication of
RT genes expressed at the interhemispheric junction.";
RL J. Neurobiol. 42:33-48(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14516700; DOI=10.1016/s0925-4773(03)00131-x;
RA Renault A.D., Starz-Gaiano M., Lehmann R.;
RT "Metabolism of sphingosine 1-phosphate and lysophosphatidic acid: a genome
RT wide analysis of gene expression in Drosophila.";
RL Mech. Dev. 119:S293-S301(2002).
CC -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC free fatty acid. {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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the central midgut of late embryos. In
CC brain, it is present at the interhemispheric junction and in groups of
CC cells in the central brain. {ECO:0000269|PubMed:10623899,
CC ECO:0000269|PubMed:14516700}.
CC -!- DISRUPTION PHENOTYPE: Discrete defect in the ellipsoid body.
CC {ECO:0000269|PubMed:10623899}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
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DR EMBL; AF323976; AAL55991.1; -; mRNA.
DR EMBL; AE014134; AAF53869.2; -; Genomic_DNA.
DR EMBL; AY071232; AAL48854.1; -; mRNA.
DR RefSeq; NP_610020.1; NM_136176.4.
DR AlphaFoldDB; Q9VIP7; -.
DR SMR; Q9VIP7; -.
DR BioGRID; 75346; 2.
DR STRING; 7227.FBpp0303611; -.
DR PaxDb; Q9VIP7; -.
DR DNASU; 250736; -.
DR EnsemblMetazoa; FBtr0081331; FBpp0080863; FBgn0045064.
DR GeneID; 250736; -.
DR KEGG; dme:Dmel_CG13969; -.
DR CTD; 250736; -.
DR FlyBase; FBgn0045064; bwa.
DR VEuPathDB; VectorBase:FBgn0045064; -.
DR eggNOG; KOG2329; Eukaryota.
DR GeneTree; ENSGT00730000110920; -.
DR InParanoid; Q9VIP7; -.
DR OMA; VRDQRVY; -.
DR OrthoDB; 969354at2759; -.
DR PhylomeDB; Q9VIP7; -.
DR BRENDA; 3.5.1.23; 1994.
DR Reactome; R-DME-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 250736; 0 hits in 3 CRISPR screens.
DR ChiTaRS; bwa; fly.
DR GenomeRNAi; 250736; -.
DR PRO; PR:Q9VIP7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0045064; Expressed in saliva-secreting gland and 60 other tissues.
DR ExpressionAtlas; Q9VIP7; baseline and differential.
DR Genevisible; Q9VIP7; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IDA:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0046514; P:ceramide catabolic process; IDA:FlyBase.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:UniProtKB.
DR InterPro; IPR008901; ACER.
DR PANTHER; PTHR46139; PTHR46139; 1.
DR Pfam; PF05875; Ceramidase; 1.
PE 2: Evidence at transcript level;
KW Calcium; Hydrolase; Lipid metabolism; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..283
FT /note="Alkaline ceramidase"
FT /id="PRO_0000247752"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT CONFLICT 19
FT /note="H -> Q (in Ref. 1; AAL55991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 32793 MW; C0DC37BCB69807A6 CRC64;
MGGMGGGGLL DIYAMAWEHL RPGSSPVDWC EGNYLISSNI AEFVNTFSNF LFILLPPVLI
MLFKEYGRFV TPGIHVIWVL LIVVGLSSMY FHATLSLIGQ LLDELAILWV FMAAFSLFYP
KRYYPKFVKN DRKTFSWLML LSAIAATGLS WWKPIVNAFV LMFMSVPTMV MLYTELQRVS
DQRVYRLGIR STTVWAVAVF CWINDRIFCE AWSSINFPYL HGFWHIFIFI AAYTVLVLFA
YFYVESELPQ RQPLLKYWPK NEFEFGIPFI SIRNPGKALR NTI
