ID   FAAH1_RAT               Reviewed;         579 AA.
AC   P97612; Q5BKA3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Fatty-acid amide hydrolase 1;
DE            EC=3.5.1.99 {ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:11128635, ECO:0000269|PubMed:17649977, ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9299394, ECO:0000269|PubMed:9790682};
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:15533037, ECO:0000269|PubMed:17649977};
DE   AltName: Full=Oleamide hydrolase 1;
GN   Name=Faah; Synonyms=Faah1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=8900284; DOI=10.1038/384083a0;
RA   Cravatt B.F., Giang D.K., Mayfield S.P., Boger D.L., Lerner R.A.,
RA   Gilula N.B.;
RT   "Molecular characterization of an enzyme that degrades neuromodulatory
RT   fatty-acid amides.";
RL   Nature 384:83-87(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=9122178; DOI=10.1073/pnas.94.6.2238;
RA   Giang D.K., Cravatt B.F.;
RT   "Molecular characterization of human and mouse fatty acid amide
RT   hydrolases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:2238-2242(1997).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=9452020;
RX   DOI=10.1002/(sici)1097-4547(19971215)50:6<1047::aid-jnr16>3.0.co;2-1;
RA   Thomas E.A., Cravatt B.F., Danielson P.E., Gilula N.B., Sutcliffe J.G.;
RT   "Fatty acid amide hydrolase, the degradative enzyme for anandamide and
RT   oleamide, has selective distribution in neurons within the rat central
RT   nervous system.";
RL   J. Neurosci. Res. 50:1047-1052(1997).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9299394; DOI=10.1006/bbrc.1997.7180;
RA   Kurahashi Y., Ueda N., Suzuki H., Suzuki M., Yamamoto S.;
RT   "Reversible hydrolysis and synthesis of anandamide demonstrated by
RT   recombinant rat fatty-acid amide hydrolase.";
RL   Biochem. Biophys. Res. Commun. 237:512-515(1997).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9790682; DOI=10.1021/bi981733n;
RA   Patricelli M.P., Lashuel H.A., Giang D.K., Kelly J.W., Cravatt B.F.;
RT   "Comparative characterization of a wild type and transmembrane domain-
RT   deleted fatty acid amide hydrolase: identification of the transmembrane
RT   domain as a site for oligomerization.";
RL   Biochemistry 37:15177-15187(1998).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11128635; DOI=10.1016/s0960-894x(00)00528-x;
RA   Boger D.L., Fecik R.A., Patterson J.E., Miyauchi H., Patricelli M.P.,
RA   Cravatt B.F.;
RT   "Fatty acid amide hydrolase substrate specificity.";
RL   Bioorg. Med. Chem. Lett. 10:2613-2616(2000).
RN   [9]
RP   CHARACTERIZATION, AND MUTAGENESIS OF LYS-142 AND SER-217.
RX   PubMed=12734197; DOI=10.1074/jbc.m303922200;
RA   McKinney M.K., Cravatt B.F.;
RT   "Evidence for distinct roles in catalysis for residues of the serine-
RT   serine-lysine catalytic triad of fatty acid amide hydrolase.";
RL   J. Biol. Chem. 278:37393-37399(2003).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15533037; DOI=10.1021/bi0480335;
RA   Saghatelian A., Trauger S.A., Want E.J., Hawkins E.G., Siuzdak G.,
RA   Cravatt B.F.;
RT   "Assignment of endogenous substrates to enzymes by global metabolite
RT   profiling.";
RL   Biochemistry 43:14332-14339(2004).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17649977; DOI=10.1021/bi7005898;
RA   Vila A., Rosengarth A., Piomelli D., Cravatt B., Marnett L.J.;
RT   "Hydrolysis of prostaglandin glycerol esters by the endocannabinoid-
RT   hydrolyzing enzymes, monoacylglycerol lipase and fatty acid amide
RT   hydrolase.";
RL   Biochemistry 46:9578-9585(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-573 IN COMPLEX WITH INHIBITOR
RP   METHOXY-ARACHIDONYL FLUOROPHOSPHATE, SUBUNIT, AND TOPOLOGY.
RX   PubMed=12459591; DOI=10.1126/science.1076535;
RA   Bracey M.H., Hanson M.A., Masuda K.R., Stevens R.C., Cravatt B.F.;
RT   "Structural adaptations in a membrane enzyme that terminates
RT   endocannabinoid signaling.";
RL   Science 298:1793-1796(2002).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 32-579 IN COMPLEX WITH INHIBITOR
RP   PF-750, TOPOLOGY, AND SUBUNIT.
RX   PubMed=18753625; DOI=10.1073/pnas.0806121105;
RA   Mileni M., Johnson D.S., Wang Z., Everdeen D.S., Liimatta M., Pabst B.,
RA   Bhattacharya K., Nugent R.A., Kamtekar S., Cravatt B.F., Ahn K.,
RA   Stevens R.C.;
RT   "Structure-guided inhibitor design for human FAAH by interspecies active
RT   site conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:12820-12824(2008).
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:9122178, PubMed:9299394, PubMed:9790682,
CC       PubMed:10526230, PubMed:11128635, PubMed:15533037, PubMed:17649977).
CC       Hydrolyzes polyunsaturated substrate anandamide preferentially as
CC       compared to monounsaturated substrates (PubMed:9122178,
CC       PubMed:11128635). It can also catalyze the hydrolysis of the
CC       endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-
CC       eicosatetraenoyl)-glycerol) (PubMed:10526230, PubMed:15533037,
CC       PubMed:17649977). 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:11128635,
CC       ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:17649977,
CC       ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9299394,
CC       ECO:0000269|PubMed:9790682}.
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:11128635,
CC         ECO:0000269|PubMed:17649977, ECO:0000269|PubMed:9122178,
CC         ECO:0000269|PubMed:9299394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137;
CC         Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:11128635,
CC         ECO:0000269|PubMed:17649977, ECO:0000269|PubMed:9122178,
CC         ECO:0000269|PubMed:9299394};
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:11128635,
CC         ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9299394,
CC         ECO:0000269|PubMed:9790682};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507;
CC         Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:11128635,
CC         ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9299394,
CC         ECO:0000269|PubMed:9790682};
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:15533037,
CC         ECO:0000269|PubMed:17649977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC         Evidence={ECO:0000269|PubMed:10526230, ECO:0000269|PubMed:15533037,
CC         ECO:0000269|PubMed:17649977};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62977;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635, ECO:0000269|PubMed:9299394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63017;
CC         Evidence={ECO:0000269|PubMed:11128635, ECO:0000269|PubMed:9299394};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63009;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63029;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62997;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63001;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63005;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63021;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:9122178};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62993;
CC         Evidence={ECO:0000269|PubMed:9122178};
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:0000269|PubMed:15533037};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45061;
CC         Evidence={ECO:0000269|PubMed:15533037};
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:0000269|PubMed:15533037};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63149;
CC         Evidence={ECO:0000269|PubMed:15533037};
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:9299394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63053;
CC         Evidence={ECO:0000269|PubMed:9299394};
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:0000269|PubMed:11128635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63121;
CC         Evidence={ECO:0000269|PubMed:11128635};
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:0000269|PubMed:9122178}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23 uM for oleamide ((9Z)-octadecenamide)
CC         {ECO:0000269|PubMed:9790682};
CC         KM=100 uM for arachidonamide ((5Z,8Z,11Z,14Z)-eicosatetraenamide)
CC         {ECO:0000269|PubMed:9299394};
CC         KM=45 uM for methyl arachidonate
CC         (1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate)
CC         {ECO:0000269|PubMed:9299394};
CC         KM=18 uM for anandamide
CC         (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine)
CC         {ECO:0000269|PubMed:9299394};
CC         KM=34 uM for anandamide
CC         (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine)
CC         {ECO:0000269|PubMed:17649977};
CC         KM=89 uM for 2-arachidonoylglycerol
CC         (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol)
CC         {ECO:0000269|PubMed:17649977};
CC         Vmax=0.11 umol/min/mg enzyme for the hydrolysis of anandamide
CC         (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine)
CC         {ECO:0000269|PubMed:10526230};
CC         Note=kcat is 7.1 sec(-1) with oleamide ((9Z)-octadecenamide)
CC         (PubMed:9790682). kcat is 28 min(-1) with 2-arachidonoylglycerol
CC         (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:17649977). kcat
CC         is 16 min(-1) with anandamide
CC         (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) (PubMed:17649977).
CC         {ECO:0000269|PubMed:17649977, ECO:0000269|PubMed:9790682};
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:9790682};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12459591,
CC       ECO:0000269|PubMed:18753625}.
CC   -!- INTERACTION:
CC       P97612; P97612: Faah; NbExp=2; IntAct=EBI-15726093, EBI-15726093;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9790682}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:9122178}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:9122178, ECO:0000269|PubMed:9790682}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:9122178}. Note=Seems to be
CC       associated with the endoplasmic reticulum and/or Golgi apparatus.
CC   -!- TISSUE SPECIFICITY: Found in neuronal cells throughout the CNS.
CC       Expressed in liver and brain, and to a lesser extent in spleen, lung,
CC       kidney and testes. {ECO:0000269|PubMed:9452020}.
CC   -!- DEVELOPMENTAL STAGE: In the CNS it accumulates progressively between
CC       embryonic day 14 and postnatal day 10, remains high until postnatal day
CC       30, then decreases into adulthood.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; U72497; AAB26961.1; -; mRNA.
DR   EMBL; BC091148; AAH91148.1; -; mRNA.
DR   RefSeq; NP_077046.1; NM_024132.3.
DR   RefSeq; XP_003750049.1; XM_003750001.4.
DR   RefSeq; XP_008774266.1; XM_008776044.2.
DR   PDB; 1MT5; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=37-573.
DR   PDB; 2VYA; X-ray; 2.75 A; A/B=32-579.
DR   PDB; 2WAP; X-ray; 2.80 A; A/B=31-573.
DR   PDB; 2WJ1; X-ray; 1.84 A; A/B=30-579.
DR   PDB; 2WJ2; X-ray; 2.55 A; A/B=30-579.
DR   PDB; 3K7F; X-ray; 1.95 A; A/B=30-579.
DR   PDB; 3K83; X-ray; 2.25 A; A/B=30-579.
DR   PDB; 3K84; X-ray; 2.25 A; A/B=30-579.
DR   PDB; 3LJ6; X-ray; 2.42 A; A/B=30-579.
DR   PDB; 3LJ7; X-ray; 2.30 A; A/B=30-579.
DR   PDB; 3OJ8; X-ray; 1.90 A; A/B=30-579.
DR   PDB; 3PPM; X-ray; 1.78 A; A/B=30-579.
DR   PDB; 3PR0; X-ray; 2.20 A; A/B=30-579.
DR   PDB; 3QJ8; X-ray; 2.90 A; A/B=32-579.
DR   PDB; 3QJ9; X-ray; 2.30 A; A/B=32-579.
DR   PDB; 3QK5; X-ray; 2.20 A; A/B=32-579.
DR   PDB; 3QKV; X-ray; 3.10 A; A/B=32-579.
DR   PDB; 4DO3; X-ray; 2.25 A; A/B=32-575.
DR   PDB; 4HBP; X-ray; 2.91 A; A/B=30-579.
DR   PDB; 4J5P; X-ray; 2.30 A; A/B=30-579.
DR   PDB; 6MRG; X-ray; 2.77 A; A/B/C/D=32-579.
DR   PDBsum; 1MT5; -.
DR   PDBsum; 2VYA; -.
DR   PDBsum; 2WAP; -.
DR   PDBsum; 2WJ1; -.
DR   PDBsum; 2WJ2; -.
DR   PDBsum; 3K7F; -.
DR   PDBsum; 3K83; -.
DR   PDBsum; 3K84; -.
DR   PDBsum; 3LJ6; -.
DR   PDBsum; 3LJ7; -.
DR   PDBsum; 3OJ8; -.
DR   PDBsum; 3PPM; -.
DR   PDBsum; 3PR0; -.
DR   PDBsum; 3QJ8; -.
DR   PDBsum; 3QJ9; -.
DR   PDBsum; 3QK5; -.
DR   PDBsum; 3QKV; -.
DR   PDBsum; 4DO3; -.
DR   PDBsum; 4HBP; -.
DR   PDBsum; 4J5P; -.
DR   PDBsum; 6MRG; -.
DR   AlphaFoldDB; P97612; -.
DR   SMR; P97612; -.
DR   DIP; DIP-46284N; -.
DR   IntAct; P97612; 1.
DR   STRING; 10116.ENSRNOP00000015667; -.
DR   BindingDB; P97612; -.
DR   ChEMBL; CHEMBL3229; -.
DR   DrugCentral; P97612; -.
DR   GuidetoPHARMACOLOGY; 1400; -.
DR   SwissLipids; SLP:000001428; -.
DR   iPTMnet; P97612; -.
DR   PhosphoSitePlus; P97612; -.
DR   jPOST; P97612; -.
DR   PaxDb; 10116-ENSRNOP00000015667; -.
DR   Ensembl; ENSRNOT00000015667.8; ENSRNOP00000015667.6; ENSRNOG00000045949.3.
DR   Ensembl; ENSRNOT00055054982; ENSRNOP00055045429; ENSRNOG00055031772.
DR   Ensembl; ENSRNOT00060047749; ENSRNOP00060039713; ENSRNOG00060027493.
DR   Ensembl; ENSRNOT00065026704; ENSRNOP00065020953; ENSRNOG00065016061.
DR   UCSC; RGD:61808; rat.
DR   AGR; RGD:61808; -.
DR   RGD; 61808; Faah.
DR   eggNOG; KOG1212; Eukaryota.
DR   GeneTree; ENSGT00940000161237; -.
DR   HOGENOM; CLU_009600_9_3_1; -.
DR   InParanoid; P97612; -.
DR   OMA; GMQPWKY; -.
DR   OrthoDB; 731186at2759; -.
DR   BRENDA; 3.5.1.4; 5301.
DR   BRENDA; 3.5.1.99; 5301.
DR   Reactome; R-RNO-2142753; Arachidonic acid metabolism.
DR   SABIO-RK; P97612; -.
DR   EvolutionaryTrace; P97612; -.
DR   PRO; PR:P97612; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000011019; Expressed in jejunum and 13 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR   GO; GO:0004040; F:amidase activity; IDA:RGD.
DR   GO; GO:0017064; F:fatty acid amide hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR   GO; GO:0008289; F:lipid binding; IDA:RGD.
DR   GO; GO:0005543; F:phospholipid binding; IMP:RGD.
DR   GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:RGD.
DR   GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR45847; FATTY ACID AMIDE HYDROLASE; 1.
DR   PANTHER; PTHR45847:SF3; FATTY-ACID AMIDE HYDROLASE 1; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   PIRSF; PIRSF001221; Amidase_fungi; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
DR   Genevisible; P97612; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW   Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..579
FT                   /note="Fatty-acid amide hydrolase 1"
FT                   /id="PRO_0000105267"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        404..433
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        434..579
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT   ACT_SITE        241
FT                   /note="Acyl-ester intermediate"
FT   BINDING         191
FT                   /ligand="substrate"
FT   BINDING         217
FT                   /ligand="substrate"
FT   BINDING         238..241
FT                   /ligand="substrate"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00519"
FT   MUTAGEN         142
FT                   /note="K->A: Lowers activity 40000-fold. Lowers activity
FT                   70000-fold; when associated with A-217."
FT                   /evidence="ECO:0000269|PubMed:12734197"
FT   MUTAGEN         217
FT                   /note="S->A: Lowers activity 3000-fold. Lowers activity
FT                   70000-fold; when associated with A-142."
FT                   /evidence="ECO:0000269|PubMed:12734197"
FT   HELIX           35..65
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           79..87
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:3OJ8"
FT   HELIX           93..111
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           121..127
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   TURN            133..136
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           169..176
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:3QK5"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          231..240
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           243..249
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           258..260
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          279..286
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           287..297
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           300..305
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           316..319
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          326..329
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           340..355
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          359..362
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           368..373
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           375..380
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   TURN            382..385
FT                   /evidence="ECO:0007829|PDB:1MT5"
FT   HELIX           386..389
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           399..401
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           404..408
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           412..422
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   TURN            423..425
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           427..435
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          436..438
FT                   /evidence="ECO:0007829|PDB:3LJ7"
FT   HELIX           441..464
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          468..473
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           484..486
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           488..491
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           492..499
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          504..511
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           514..520
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           530..538
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   STRAND          546..552
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           558..572
FT                   /evidence="ECO:0007829|PDB:3PPM"
FT   HELIX           574..576
FT                   /evidence="ECO:0007829|PDB:3PR0"
SQ   SEQUENCE   579 AA;  63357 MW;  606491C0B033E1AA CRC64;
     MVLSEVWTTL SGVSGVCLAC SLLSAAVVLR WTGRQKARGA ATRARQKQRA SLETMDKAVQ
     RFRLQNPDLD SEALLTLPLL QLVQKLQSGE LSPEAVFFTY LGKAWEVNKG TNCVTSYLTD
     CETQLSQAPR QGLLYGVPVS LKECFSYKGH DSTLGLSLNE GMPSESDCVV VQVLKLQGAV
     PFVHTNVPQS MLSFDCSNPL FGQTMNPWKS SKSPGGSSGG EGALIGSGGS PLGLGTDIGG
     SIRFPSAFCG ICGLKPTGNR LSKSGLKGCV YGQTAVQLSL GPMARDVESL ALCLKALLCE
     HLFTLDPTVP PLPFREEVYR SSRPLRVGYY ETDNYTMPSP AMRRALIETK QRLEAAGHTL
     IPFLPNNIPY ALEVLSAGGL FSDGGRSFLQ NFKGDFVDPC LGDLILILRL PSWFKRLLSL
     LLKPLFPRLA AFLNSMRPRS AEKLWKLQHE IEMYRQSVIA QWKAMNLDVL LTPMLGPALD
     LNTPGRATGA ISYTVLYNCL DFPAGVVPVT TVTAEDDAQM ELYKGYFGDI WDIILKKAMK
     NSVGLPVAVQ CVALPWQEEL CLRFMREVEQ LMTPQKQPS
//