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Database: UniProt
Entry: A0A3B3QTE5_9TELE
LinkDB: A0A3B3QTE5_9TELE
Original site: A0A3B3QTE5_9TELE 
ID   A0A3B3QTE5_9TELE        Unreviewed;       349 AA.
AC   A0A3B3QTE5;
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};
GN   Name=NAAA {ECO:0000313|Ensembl:ENSPKIP00000008890.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000008890.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000008890.1}
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; A0A3B3QTE5; -.
DR   STRING; 1676925.ENSPKIP00000008890; -.
DR   Ensembl; ENSPKIT00000032981.1; ENSPKIP00000008890.1; ENSPKIG00000024203.1.
DR   GeneTree; ENSGT00530000063548; -.
DR   OrthoDB; 5485766at2759; -.
DR   Proteomes; UP000261540; 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   CDD; cd01903; Ntn_AC_NAAA; 1.
DR   Gene3D; 1.10.10.2120; -; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..349
FT                   /note="N-acylethanolamine-hydrolyzing acid amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017215942"
FT   DOMAIN          21..80
FT                   /note="Acid ceramidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15508"
FT   DOMAIN          115..263
FT                   /note="Choloylglycine hydrolase/NAAA C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02275"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ   SEQUENCE   349 AA;  39208 MW;  E0240E38644E6375 CRC64;
     MKCSLALIPL TLAAWCYADF APPIVNISLD EPPKERWAPL MKVIDVRYYR KIAPLIIDSI
     VPKWVHQAIK PVVEALEDYI PQHYAGEIQG LASLSGVDVT DIILLNFAYE ITAFCTSIVA
     QDTNGRIYHG RNMDYPFVEI LRNLTVDILF IRDGKVAYRG TSFAGYVGLW TGQSANNFTI
     SGDERDVGFW WENVISAFIL KSIPASWLMR ETLEEAASYQ DALERLSKVP IISTVYYIVG
     GVQPGEGAVV TRDRSGAADV WVLDPLHGQW FRVETNYDHW NPPPHGDDRR TPTIKALNAT
     GQENINLDSL FKVLSASPTC NRITIYTTVM SAGTPEKYRT VMREKCNLE
//
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