ID   ACASE_CAEEL             Reviewed;         272 AA.
AC   O45145;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 117.
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=W02F12.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; FO081630; CCD72931.1; -; Genomic_DNA.
DR   PIR; T32993; T32993.
DR   RefSeq; NP_504697.2; NM_072296.5.
DR   AlphaFoldDB; O45145; -.
DR   SMR; O45145; -.
DR   STRING; 6239.W02F12.2; -.
DR   PaxDb; O45145; -.
DR   PeptideAtlas; O45145; -.
DR   EnsemblMetazoa; W02F12.2.1; W02F12.2.1; WBGene00020947.
DR   UCSC; W02F12.2; c. elegans.
DR   WormBase; W02F12.2; CE33333; WBGene00020947; -.
DR   eggNOG; KOG2329; Eukaryota.
DR   GeneTree; ENSGT00730000110920; -.
DR   HOGENOM; CLU_088280_0_0_1; -.
DR   InParanoid; O45145; -.
DR   OMA; VRDQRVY; -.
DR   OrthoDB; 969354at2759; -.
DR   PhylomeDB; O45145; -.
DR   Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR   PRO; PR:O45145; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00020947; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0030173; C:integral component of Golgi membrane; ISS:WormBase.
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; ISS:WormBase.
DR   GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; ISS:WormBase.
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_0000247751"
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;  31162 MW;  B9E5357A054D10C4 CRC64;
     MESSSINRWF EYESGHAWCE SAYKYQTLPY VAEFANTCTN LPIIVLPLVN IMLLRRYLHD
     VNGGLIFPQL LLTFNGLAST YYHATLNLFG QLVDELSLVW IITVFLVVYI PVMKWFPEKF
     SKRLTLVRWV VLIVTALVSG LCFLEPNLNA IALMLFSIPA AVVINYEGKQ SGIPDIESFP
     SRILALWGVA FSFWFADRLL CDFWLYLGTP YLHALFHLLA GLAGYTIFIM FSMIDIESRT
     KTHKYTAAVR YFPGKNGSIF SFPYISLKER SQ