ID   ACASE_CAEBR             Reviewed;         272 AA.
AC   Q60WT2; A8XUJ1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 70.
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;
GN   ORFNames=CBG18997;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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   -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
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DR   EMBL; HE601047; CAP36316.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q60WT2; -.
DR   SMR; Q60WT2; -.
DR   STRING; 6238.CBG18997; -.
DR   WormBase; CBG18997; CBP46843; WBGene00038287; -.
DR   eggNOG; KOG2329; Eukaryota.
DR   HOGENOM; CLU_088280_0_0_1; -.
DR   InParanoid; Q60WT2; -.
DR   OMA; VRDQRVY; -.
DR   OrthoDB; 969354at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
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; IEA:UniProtKB-EC.
DR   GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR   InterPro; IPR008901; ACER.
DR   PANTHER; PTHR46139; PTHR46139; 1.
DR   Pfam; PF05875; Ceramidase; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid metabolism; Membrane; Metal-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..272
FT                   /note="Alkaline ceramidase"
FT                   /id="PRO_0000247750"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   272 AA;  31262 MW;  CD1DB0CFE92258B7 CRC64;
     MDSSSISRWF EYESGHAWCE SAYKYQTLPY VAEFANTCTN LPIIVLPLVN IMLLRRYLHD
     VNGGLVFPQL LLTFNGLAST YYHATLNLFG QLVDELSLVW IITVFLVVYI PVMKWFPERF
     SKRLTVVRWV VLIVTAVVSA LCFLEPNLNA IALMLFSIPA AVVIRYEGKQ SGIPDIENFP
     SRILALWGVA FSFWFADRLL CDFWLYLGTP YLHALFHLLA GLAGYTIFIM FSMIDIESRS
     KTHRYTAAVR YFPDKNGSIF SFPYISLKER SQ