ACER1_DANRE
ID ACER1_DANRE Reviewed; 266 AA.
AC Q568I2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Alkaline ceramidase 1 {ECO:0000305};
DE Short=AlkCDase 1;
DE Short=Alkaline CDase 1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q8TDN7};
DE EC=3.5.1.23 {ECO:0000250|UniProtKB:Q8TDN7};
DE AltName: Full=Acylsphingosine deacylase 3;
DE AltName: Full=N-acylsphingosine amidohydrolase 3;
GN Name=acer1; Synonyms=asah3; ORFNames=zgc:110285;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoplasmic reticulum ceramidase that catalyzes the
CC hydrolysis of ceramides into sphingosine and free fatty acids at
CC alkaline pH. Ceramides, sphingosine, and its phosphorylated form
CC sphingosine-1-phosphate are bioactive lipids that mediate cellular
CC signaling pathways regulating several biological processes including
CC cell proliferation, apoptosis and differentiation. May also hydrolyze
CC dihydroceramides to produce dihydrosphingosine.
CC {ECO:0000250|UniProtKB:Q8TDN7}.
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 Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetracosanoyl-sphing-4-enine = sphing-4-enine +
CC tetracosanoate; Xref=Rhea:RHEA:41283, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57756, ChEBI:CHEBI:72965;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41284;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + H2O = a fatty acid + sphinganine;
CC Xref=Rhea:RHEA:33551, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:31488, ChEBI:CHEBI:57817;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33552;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate
CC + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(15Z-tetracosenoyl)-sphing-4-enine = (15Z)-
CC tetracosenoate + sphing-4-enine; Xref=Rhea:RHEA:41267,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:74450; Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41268;
CC Evidence={ECO:0000250|UniProtKB:Q8TDN7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NUN7};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q8TDN7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TDN7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
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DR EMBL; BC092849; AAH92849.1; -; mRNA.
DR RefSeq; NP_001017603.1; NM_001017603.1.
DR AlphaFoldDB; Q568I2; -.
DR SMR; Q568I2; -.
DR STRING; 7955.ENSDARP00000120885; -.
DR PaxDb; Q568I2; -.
DR PRIDE; Q568I2; -.
DR GeneID; 550266; -.
DR KEGG; dre:550266; -.
DR CTD; 125981; -.
DR ZFIN; ZDB-GENE-050417-70; acer1.
DR eggNOG; KOG2329; Eukaryota.
DR InParanoid; Q568I2; -.
DR Reactome; R-DRE-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q568I2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0071633; F:dihydroceramidase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046514; P:ceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0046512; P:sphingosine biosynthetic 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; Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Metal-binding; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..266
FT /note="Alkaline ceramidase 1"
FT /id="PRO_0000247747"
FT TOPO_DOM 1..27
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..83
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..139
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN7"
SQ SEQUENCE 266 AA; 30908 MW; 0619331570BE647C CRC64;
MAGVFSYESS EVDWCEDNYK HSENVVEYFN TMSSFIFFVI SPIMLYLLHP YAKERNLAVH
LVWIMMVFVG IFSMYFHMTL SFMGQMLDEL SILWVLAIGY SLWFPRKHFP SFVKDRTSFA
RLVLTITIIS TLSSFVKPTA NAYALNCFAI HILYSLFVEL KSCTDERVLR LAWASIGLWV
LAISCWISDR FGCSFWQKLD FCYLHGIWHI LIVMATAYAS TLIAYLDASQ EIPYSLPDLQ
YWPRNNWAIG LPYIVLKGTN TTRKTC
