ID E3LWH7_CAERE Unreviewed; 353 AA.
AC E3LWH7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase {ECO:0000256|ARBA:ARBA00040404};
DE EC=3.5.1.60 {ECO:0000256|ARBA:ARBA00039046};
GN ORFNames=CRE_02891 {ECO:0000313|EMBL:EFO83649.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, produced by
CC autocatalytic cleavage. {ECO:0000256|ARBA:ARBA00038527}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the acid ceramidase family.
CC {ECO:0000256|ARBA:ARBA00005730, ECO:0000256|PIRNR:PIRNR017632}.
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DR EMBL; DS268417; EFO83649.1; -; Genomic_DNA.
DR RefSeq; XP_003111788.1; XM_003111740.1.
DR AlphaFoldDB; E3LWH7; -.
DR STRING; 31234.E3LWH7; -.
DR MEROPS; C89.002; -.
DR EnsemblMetazoa; CRE02891.1; CRE02891.1; WBGene00055335.
DR GeneID; 9811743; -.
DR KEGG; crq:GCK72_010858; -.
DR CTD; 9811743; -.
DR eggNOG; ENOG502QT7H; Eukaryota.
DR HOGENOM; CLU_054401_0_0_1; -.
DR InParanoid; E3LWH7; -.
DR OMA; RYSINLD; -.
DR OrthoDB; 5485766at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01903; Ntn_AC_NAAA; 1.
DR InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR PANTHER; PTHR28583; ACID AMIDASE; 1.
DR PANTHER; PTHR28583:SF4; N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE; 1.
DR Pfam; PF02275; CBAH; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR017632};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017632}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..353
FT /note="N-acylethanolamine-hydrolyzing acid amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003174732"
FT DOMAIN 22..79
FT /note="Acid ceramidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15508"
FT DOMAIN 123..290
FT /note="Choloylglycine hydrolase/NAAA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02275"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ SEQUENCE 353 AA; 40225 MW; 7219B1BDA7DEF014 CRC64;
MLLLPPLIPI LLLVIPISST RTPPRYTIDL DEHPSQRWNQ VIKDHLDYLP GVVEESKKYI
PKPLQPFVWW VASKVERFFP PDTRLELEGI ATQSGLPLGE IVGLNILYDI AAFDRRHIFG
LGCTSIVAQN SAGRIFHGRN LDYDMTGLLK NITVYVDFTR NGTVIYSGIT FALYNGVLTG
QRPGAYSVSL NARYSGAYID NILMELYTKF KRPVSFFIRD VLESQETYTD AVATLSNTHL
LSPSYIIVAG TKKNEGVVIP RNRWAAANVY PLDMDSNQWF LVETNYDNWQ KQGDNRRITA
IQKLKELGKE NFNEKSMVEV LSTIPVRNNL TVFSSVIEPK IPKVFEDFTW VWD
//
