ASAH1_CAEEL
ID ASAH1_CAEEL Reviewed; 393 AA.
AC O45686;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acid ceramidase {ECO:0000305};
DE EC=3.5.1.23 {ECO:0000250|UniProtKB:Q13510};
DE AltName: Full=Acylsphingosine amidohydrolase 1;
DE Contains:
DE RecName: Full=Acid ceramidase subunit alpha {ECO:0000250|UniProtKB:Q13510};
DE Contains:
DE RecName: Full=Acid ceramidase subunit beta {ECO:0000250|UniProtKB:Q13510};
DE Flags: Precursor;
GN Name=asah-1; ORFNames=K11D2.2;
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: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides
CC into sphingosine and free fatty acids at acidic pH.
CC {ECO:0000250|UniProtKB:Q13510}.
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:Q13510};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q13510}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. The heterodimer is composed of
CC the disulfide-linked alpha and beta chains produced by autocatalytic
CC cleavage of the precursor. {ECO:0000250|UniProtKB:Q13510}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted
CC {ECO:0000250|UniProtKB:Q13510}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13510}.
CC -!- PTM: Proteolytically cleaved into two chains alpha and beta that remain
CC associated via a disulfide bond. Cleavage gives rise to a conformation
CC change that activates the enzyme. The same catalytic Cys residue
CC mediates the autoproteolytic cleavage and subsequent hydrolysis of
CC lipid substrates. The beta chain may undergo an additional C-terminal
CC processing. {ECO:0000250|UniProtKB:Q13510}.
CC -!- SIMILARITY: Belongs to the acid ceramidase family. {ECO:0000305}.
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DR EMBL; Z83115; CAB05556.1; -; Genomic_DNA.
DR PIR; T23602; T23602.
DR RefSeq; NP_493173.1; NM_060772.8.
DR AlphaFoldDB; O45686; -.
DR SMR; O45686; -.
DR BioGRID; 38517; 5.
DR DIP; DIP-26864N; -.
DR IntAct; O45686; 2.
DR STRING; 6239.K11D2.2.1; -.
DR MEROPS; C89.A02; -.
DR PaxDb; O45686; -.
DR PeptideAtlas; O45686; -.
DR EnsemblMetazoa; K11D2.2.1; K11D2.2.1; WBGene00010769.
DR GeneID; 173120; -.
DR KEGG; cel:CELE_K11D2.2; -.
DR UCSC; K11D2.2; c. elegans.
DR CTD; 173120; -.
DR WormBase; K11D2.2; CE12120; WBGene00010769; asah-1.
DR eggNOG; ENOG502QVBG; Eukaryota.
DR GeneTree; ENSGT00530000063548; -.
DR HOGENOM; CLU_054401_0_0_1; -.
DR InParanoid; O45686; -.
DR OMA; RWKNPLF; -.
DR OrthoDB; 745108at2759; -.
DR PhylomeDB; O45686; -.
DR Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; O45686; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:O45686; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00010769; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IBA:GO_Central.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR Pfam; PF02275; CBAH; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid metabolism; Lysosome;
KW Reference proteome; Secreted; Signal; Sphingolipid metabolism; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..393
FT /note="Acid ceramidase"
FT /id="PRO_0000002322"
FT CHAIN 17..139
FT /note="Acid ceramidase subunit alpha"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT /id="PRO_0000446618"
FT CHAIN 140..393
FT /note="Acid ceramidase subunit beta"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT /id="PRO_0000446619"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT SITE 159
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT SITE 318
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT SITE 331
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..338
FT /note="Interchain (between alpha and beta subunits)"
FT /evidence="ECO:0000250|UniProtKB:Q13510"
FT DISULFID 386..390
FT /evidence="ECO:0000250|UniProtKB:A0A0P6JG37"
SQ SEQUENCE 393 AA; 44823 MW; 7545366601FDFFF0 CRC64;
MLRELSVLLL VAVCAAKHVE LPAPFKDHCI LDDKQNLYDP SKQFDIKWYD VNLDLPPSER
WVQIATANKE HIADLIGVLI NLITPWFPNA IDFVDDVFGD LAPKLAQPYR DEIFSIANAT
GIPLGQITMY NIFYEIFTVC TSVIAQDKDG HVFHARNLDF GLFMGWDPVL HDWQISQKLR
KMIINVNWLK DGKLLYKSNN FAGYIGIYNG LKPNAFSLTA DDRFQLVGGY YGILKWVFGL
EADGKWMSWL ARETLETKTT YLDAKEHLMN TPMLSPVYFI LGGSKKDEGC IIARSLDKTA
LLTEMATSPH GWYLLETNYD QGTEDLYLDD RDTPGFRCMD KLTQKNVGFE GIFNVLSSRT
NLNKLTTYTV LMSVETSRFE TILQSCPGEC YPW
