FAAH1_PIG
ID FAAH1_PIG Reviewed; 579 AA.
AC Q9TUI8;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Fatty-acid amide hydrolase 1;
DE EC=3.5.1.99 {ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
DE AltName: Full=Anandamide amidase;
DE AltName: Full=Anandamide amidohydrolase 1;
DE AltName: Full=Fatty acid ester hydrolase;
DE EC=3.1.1.- {ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
DE AltName: Full=Oleamide hydrolase 1;
GN Name=FAAH; Synonyms=FAAH1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF SER-217; SER-218; ASP-237;
RP SER-241 AND CYS-249, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Brain;
RX PubMed=10526230; DOI=10.1016/s1388-1981(99)00143-2;
RA Goparaju S.K., Kurahashi Y., Suzuki H., Ueda N., Yamamoto S.;
RT "Anandamide amidohydrolase of porcine brain: cDNA cloning, functional
RT expression and site-directed mutagenesis.";
RL Biochim. Biophys. Acta 1441:77-84(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12664593; DOI=10.1007/978-1-4615-0193-0_38;
RA Ueda N., Katayama K., Goparaju S.K., Kurahashi Y., Yamanaka K., Suzuki H.,
RA Yamamoto S.;
RT "Catalytic properties of purified recombinant anandamide amidohydrolase.";
RL Adv. Exp. Med. Biol. 507:251-256(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like
CC the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the
CC endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC ethanolamine), as well as other fatty amides, to their corresponding
CC fatty acids, thereby regulating the signaling functions of these
CC molecules (PubMed:10526230, PubMed:12664593). Also catalyzes the
CC hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:10526230,
CC PubMed:12664593). FAAH cooperates with PM20D1 in the hydrolysis of
CC amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-
CC fatty acyl-L-serine, thereby acting as a physiological regulator of
CC specific subsets of intracellular, but not of extracellular, N-fatty
CC acyl amino acids (By similarity). {ECO:0000250|UniProtKB:O08914,
CC ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine;
CC Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenamide + H2O = (9Z)-octadecenoate + NH4(+);
CC Xref=Rhea:RHEA:26506, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:116314; EC=3.5.1.99;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:12664593};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + methanol;
CC Xref=Rhea:RHEA:63052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:32395, ChEBI:CHEBI:78033;
CC Evidence={ECO:0000269|PubMed:10526230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63053;
CC Evidence={ECO:0000269|PubMed:10526230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienamide + H2O = (9Z,12Z,15Z)-
CC octadecatrienoate + NH4(+); Xref=Rhea:RHEA:62976, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:32387, ChEBI:CHEBI:142684;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62977;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenamide + H2O = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + NH4(+); Xref=Rhea:RHEA:63016, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:32395, ChEBI:CHEBI:137830;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63017;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z)-octadecenamide + H2O = (6Z)-octadecenoate + NH4(+);
CC Xref=Rhea:RHEA:63008, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32375, ChEBI:CHEBI:146168;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63009;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15Z)-tetracosenamide + H2O = (15Z)-tetracosenoate + NH4(+);
CC Xref=Rhea:RHEA:63028, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32392, ChEBI:CHEBI:146166;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63029;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z)-eicosatrienamide + H2O = (8Z,11Z,14Z)-
CC eicosatrienoate + NH4(+); Xref=Rhea:RHEA:62996, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:71589, ChEBI:CHEBI:146163;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62997;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienamide + H2O = (11Z,14Z,17Z)-
CC eicosatrienoate + NH4(+); Xref=Rhea:RHEA:63000, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:77223, ChEBI:CHEBI:146164;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63001;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienamide + H2O = (11Z,14Z)-eicosadienoate +
CC NH4(+); Xref=Rhea:RHEA:63004, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:77220, ChEBI:CHEBI:146165;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63005;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienamide + H2O = (9Z,12Z)-octadecadienoate +
CC NH4(+); Xref=Rhea:RHEA:63020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:82984;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63021;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecamide = NH4(+) + tetradecanoate;
CC Xref=Rhea:RHEA:62992, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:137125;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62993;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl) ethanolamine = (9Z)-octadecenoate +
CC ethanolamine; Xref=Rhea:RHEA:45060, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57603, ChEBI:CHEBI:71466;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45061;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-taurine = (9Z)-octadecenoate +
CC taurine; Xref=Rhea:RHEA:63148, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:146191, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63149;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-eicosenamide + H2O = (11Z)-eicosenoate + NH4(+);
CC Xref=Rhea:RHEA:63120, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:32426, ChEBI:CHEBI:146167;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63121;
CC Evidence={ECO:0000250|UniProtKB:P97612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-hexadecenoyl) ethanolamine = (9Z)-hexadecenoate +
CC ethanolamine; Xref=Rhea:RHEA:35563, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57603, ChEBI:CHEBI:71465;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35564;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl ethanolamine = ethanolamine +
CC octadecanoate; Xref=Rhea:RHEA:63124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57603, ChEBI:CHEBI:85299;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63125;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-docosanoyl-ethanolamine = docosanoate + ethanolamine;
CC Xref=Rhea:RHEA:63128, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:146186;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63129;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetracosanoyl-taurine = taurine + tetracosanoate;
CC Xref=Rhea:RHEA:63140, ChEBI:CHEBI:15377, ChEBI:CHEBI:31014,
CC ChEBI:CHEBI:132049, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63141;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(15Z-tetracosenoyl)-ethanolamine = (15Z)-
CC tetracosenoate + ethanolamine; Xref=Rhea:RHEA:63144,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:146187; Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63145;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-docosanoyl-taurine = docosanoate + taurine;
CC Xref=Rhea:RHEA:63156, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858,
CC ChEBI:CHEBI:146196, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63157;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(15Z-tetracosenoyl)-taurine = (15Z)-tetracosenoate +
CC taurine; Xref=Rhea:RHEA:63160, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392,
CC ChEBI:CHEBI:146198, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63161;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tricosanoyl-taurine = taurine + tricosanoate;
CC Xref=Rhea:RHEA:63164, ChEBI:CHEBI:15377, ChEBI:CHEBI:79007,
CC ChEBI:CHEBI:146197, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63165;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-
CC octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:59002; Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:149697; Evidence={ECO:0000250|UniProtKB:O08914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117;
CC Evidence={ECO:0000250|UniProtKB:O08914};
CC -!- ACTIVITY REGULATION: inhibited by trifluoromethyl ketone.
CC {ECO:0000250|UniProtKB:P97612}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=65 nmol/min/mg enzyme for the hydrolysis of oleamide ((9Z)-
CC octadecenamide) {ECO:0000269|PubMed:10526230};
CC Vmax=733 nmol/min/mg enzyme for the hydrolysis of 2-
CC arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol)
CC {ECO:0000269|PubMed:10526230};
CC Vmax=118 nmol/min/mg enzyme for the hydrolysis of methyl ester of
CC arachidonic acid (1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate)
CC {ECO:0000269|PubMed:10526230};
CC Vmax=207 nmol/min/mg enzyme for the hydrolysis of anandamide (N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine)
CC {ECO:0000269|PubMed:10526230};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P97612}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P97612}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P97612}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P97612}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P97612}. Note=Seems to be associated with the
CC endoplasmic reticulum and/or Golgi apparatus.
CC {ECO:0000250|UniProtKB:P97612}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB027132; BAA86917.1; -; mRNA.
DR RefSeq; NP_999079.1; NM_213914.1.
DR AlphaFoldDB; Q9TUI8; -.
DR SMR; Q9TUI8; -.
DR STRING; 9823.ENSSSCP00000004216; -.
DR ChEMBL; CHEMBL4295969; -.
DR PaxDb; Q9TUI8; -.
DR PeptideAtlas; Q9TUI8; -.
DR PRIDE; Q9TUI8; -.
DR Ensembl; ENSSSCT00030033806; ENSSSCP00030015282; ENSSSCG00030024291.
DR Ensembl; ENSSSCT00035018848; ENSSSCP00035006628; ENSSSCG00035014837.
DR Ensembl; ENSSSCT00060027540; ENSSSCP00060011758; ENSSSCG00060020342.
DR GeneID; 396949; -.
DR KEGG; ssc:396949; -.
DR CTD; 2166; -.
DR eggNOG; KOG1212; Eukaryota.
DR InParanoid; Q9TUI8; -.
DR OrthoDB; 852596at2759; -.
DR BRENDA; 3.5.1.4; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0103073; F:anandamide amidohydrolase activity; ISS:UniProtKB.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; ISS:UniProtKB.
DR GO; GO:0102077; F:oleamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR030560; FAAH.
DR PANTHER; PTHR45847:SF3; PTHR45847:SF3; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..579
FT /note="Fatty-acid amide hydrolase 1"
FT /id="PRO_0000105266"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 404..433
FT /evidence="ECO:0000250"
FT TOPO_DOM 434..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238..241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00519"
FT MUTAGEN 217
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10526230"
FT MUTAGEN 218
FT /note="S->A: Lowers activity by at least 98%."
FT /evidence="ECO:0000269|PubMed:10526230"
FT MUTAGEN 237
FT /note="D->E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10526230"
FT MUTAGEN 241
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10526230"
FT MUTAGEN 249
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10526230"
SQ SEQUENCE 579 AA; 62857 MW; 0600F2FDC9879D7C CRC64;
MVQEELWAAF SGPSGVALAC CLVAAALALR WSSRRMARGA AARARQRQQA ALETMDKAAQ
RFRLQNPDLD SEMLLALPLP QLVQKVRSGE LSPEAVLFSY LQKAWEVNRG TNCVTTYLAD
CEAQLCQAPG QGLLYGVPVS LKECFSCKGH DSTLGLSRNQ GTPAECDCVV VQVLKLQGAV
PFVHTNVPQS MFSYDCSNPL FGQTTNPWMS SKSPGGSSGG EGALIAAGGS PLGLGTDIGG
SIRFPSAFCG ICGIKPTGNR ISKSGLKGSV YGQVAVQLSV GPMARDVESL ALCLRALLCE
DMFRLDPTVP PLPFNEEVYA SSRPLRVGYY ETDNYTMPTP AMRRALLETK RSLEAAGHTL
IPFLPANIPH ALEALSTGGL FSDGGKRLLQ NFEGDYVDSC LGDLISILRL PKWLKGLLAF
MLRPLLPRLA GFLSSLRPRS AGKLWELQHE IEMYRHSVIA QWRALDLDVV LTPMLSPALD
LNAPGKATGA VSYTLLYNCL DFPAGVVPVT TVTAEDEAQM EHYKGYFGDI WDKVVQKAMK
RSVGLPVAVQ CVALPWQEEL CLRFMREVER LMAPGRQPS
