ID A0A3B3WJC2_9TELE Unreviewed; 351 AA.
AC A0A3B3WJC2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase {ECO:0000256|ARBA:ARBA00040404};
DE EC=3.5.1.23 {ECO:0000256|ARBA:ARBA00011891};
DE EC=3.5.1.60 {ECO:0000256|ARBA:ARBA00039046};
DE AltName: Full=Acylsphingosine deacylase NAAA {ECO:0000256|ARBA:ARBA00042519};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000002901.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000002901.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain
CC fatty acid + ethanolamine; Xref=Rhea:RHEA:17505, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15897, ChEBI:CHEBI:57560, ChEBI:CHEBI:57603; EC=3.5.1.60;
CC Evidence={ECO:0000256|ARBA:ARBA00036451};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17506;
CC Evidence={ECO:0000256|ARBA:ARBA00036451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC Evidence={ECO:0000256|ARBA:ARBA00036827};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC Evidence={ECO:0000256|ARBA:ARBA00036827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72956;
CC Evidence={ECO:0000256|ARBA:ARBA00035891};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292;
CC Evidence={ECO:0000256|ARBA:ARBA00035891};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine +
CC hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464;
CC Evidence={ECO:0000256|ARBA:ARBA00036896};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065;
CC Evidence={ECO:0000256|ARBA:ARBA00036896};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC Evidence={ECO:0000256|ARBA:ARBA00035825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC Evidence={ECO:0000256|ARBA:ARBA00035825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoylethanolamine = ethanolamine +
CC tetradecanoate; Xref=Rhea:RHEA:45452, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57603, ChEBI:CHEBI:85262;
CC Evidence={ECO:0000256|ARBA:ARBA00036924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45453;
CC Evidence={ECO:0000256|ARBA:ARBA00036924};
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:0000256|ARBA:ARBA00000595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000256|ARBA:ARBA00000595};
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 AlphaFoldDB; A0A3B3WJC2; -.
DR Ensembl; ENSPMET00000011741.1; ENSPMEP00000002901.1; ENSPMEG00000003992.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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:0017040; F:N-acylsphingosine amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..351
FT /note="N-acylethanolamine-hydrolyzing acid amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017185875"
FT DOMAIN 26..84
FT /note="Acid ceramidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15508"
FT DOMAIN 120..288
FT /note="Choloylglycine hydrolase/NAAA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02275"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ SEQUENCE 351 AA; 39949 MW; 332ABECCB0D1046B CRC64;
QLAVIMVWSS ALLVLLGLSG SLWAQQTPTV LVNLDLSPEQ RWEHLQQAFD TDLMKKAAQI
LISSQVPNWF HKAISPIVMS LEKHIPQLYA REIRGIASTM KMKLADVVIL NFAYEFTAYC
TSIVAQDKNG NIYHGRNFDF PHSVLRNLTM NVVFFKNGEP AYFGTSLAGY VGLWTGMSPY
KFTVSGNQRG KTVWSNWWKN VVSAVFVHRF PVSWLIRVTL EEAKDFEDAV TRLSTTPLIT
GVYYIVGGVR AGEGVVITRD RKGPADIWPL EPLNGGWYRV QTNVDHWLPP PKKLNRRLVT
SQSDDTAIMF NFYYYTAVIT TIYTTLMSAA TPREYTTILR EKVLKLYLKC Y
//
