ASAH2_CAEEL
ID ASAH2_CAEEL Reviewed; 401 AA.
AC Q09551;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable acid ceramidase {ECO:0000305};
DE Short=AC {ECO:0000250|UniProtKB:Q13510};
DE Short=ACDase {ECO:0000250|UniProtKB:Q13510};
DE Short=Acid CDase {ECO:0000250|UniProtKB:Q13510};
DE EC=3.5.1.23 {ECO:0000250|UniProtKB:Q13510};
DE AltName: Full=Acylsphingosine deacylase {ECO:0000250|UniProtKB:Q13510};
DE AltName: Full=N-acylsphingosine amidohydrolase {ECO:0000312|WormBase:F27E5.1};
DE Flags: Precursor;
GN Name=asah-2 {ECO:0000312|WormBase:F27E5.1};
GN ORFNames=F27E5.1 {ECO:0000312|WormBase:F27E5.1};
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|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 -!- SIMILARITY: Belongs to the acid ceramidase family. {ECO:0000305}.
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DR EMBL; Z48582; CAA88464.1; -; Genomic_DNA.
DR PIR; T21456; T21456.
DR RefSeq; NP_496187.1; NM_063786.3.
DR AlphaFoldDB; Q09551; -.
DR SMR; Q09551; -.
DR BioGRID; 49800; 1.
DR IntAct; Q09551; 1.
DR MINT; Q09551; -.
DR STRING; 6239.F27E5.1; -.
DR MEROPS; C89.A01; -.
DR PaxDb; Q09551; -.
DR PeptideAtlas; Q09551; -.
DR EnsemblMetazoa; F27E5.1.1; F27E5.1.1; WBGene00009192.
DR GeneID; 185021; -.
DR KEGG; cel:CELE_F27E5.1; -.
DR UCSC; F27E5.1; c. elegans.
DR CTD; 185021; -.
DR WormBase; F27E5.1; CE01562; WBGene00009192; asah-2.
DR eggNOG; ENOG502QVBG; Eukaryota.
DR GeneTree; ENSGT00530000063548; -.
DR HOGENOM; CLU_054401_0_0_1; -.
DR InParanoid; Q09551; -.
DR OMA; FQCAREK; -.
DR OrthoDB; 745108at2759; -.
DR PhylomeDB; Q09551; -.
DR PRO; PR:Q09551; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009192; Expressed in larva and 2 other tissues.
DR GO; GO:0005764; C:lysosome; IEA:InterPro.
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-KW.
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 Glycoprotein; Hydrolase; Lipid metabolism; Reference proteome; Signal;
KW Sphingolipid metabolism.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..401
FT /note="Probable acid ceramidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000002321"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 401 AA; 45235 MW; 054A771C3BCF36C3 CRC64;
MKPVAISLSL LLLVTLLPGS EQRKVDNPDF QPNCLVGGPD IYDPAQSEKV LWFDVNLDLP
PRQRFQQIAK AYKKEIHAVF DVLNYFLTII PGVNAWELIG NMTASALDKG MIMNPYRDEV
LGIAEVLDVP LGNLVFLNLF YEMSRFCTSI VAQTEDNKDL YHARNLDFGQ LFVWDIAAQS
WGLTEALKKV SVNINFFKNG KLLFKGSTLA GHVGVLTAMK PHKFSLSMNA KVQPDIINVA
KWYMGAYENT DLQFVMYFDR WLFENCDDFQ CAREKIAGVK LLTGAYFILG GANPGEGSVL
VRNTTSVQFE RKLFDGANDW FLLQTNYDPD KDPLFIDNRR DPGNACMNKL TRANVGMKGI
FTVLSSKPNL NKTTVHTVIM SVTKGYFETF IQKCPNPCWA F
