FAAH1_MOUSE
ID FAAH1_MOUSE Reviewed; 579 AA.
AC O08914; Q922S0; Q9DBF5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Fatty-acid amide hydrolase 1;
DE EC=3.5.1.99 {ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712};
DE AltName: Full=Anandamide amidohydrolase 1;
DE AltName: Full=Fatty acid ester hydrolase;
DE EC=3.1.1.- {ECO:0000250|UniProtKB:P97612};
DE AltName: Full=Oleamide hydrolase 1;
GN Name=Faah; Synonyms=Faah1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9878243; DOI=10.1006/geno.1998.5597;
RA Wan M., Cravatt B.F., Ring H.Z., Zhang X., Francke U.;
RT "Conserved chromosomal location and genomic structure of human and mouse
RT fatty-acid amide hydrolase genes and evaluation of clasper as a candidate
RT neurological mutation.";
RL Genomics 54:408-414(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=32271712; DOI=10.7554/elife.55211;
RA Kim J.T., Terrell S.M., Li V.L., Wei W., Fischer C.R., Long J.Z.;
RT "Cooperative enzymatic control of N-acyl amino acids by PM20D1 and FAAH.";
RL Elife 9:0-0(2020).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like
CC the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC ethanolamine), as well as other fatty amides such as the taurine-
CC conjugated fatty acids (a structural class of central nervous system
CC (CNS) metabolites), to their corresponding fatty acids, thereby
CC regulating the signaling functions of these molecules (PubMed:15533037,
CC PubMed:32271712). 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 (PubMed:32271712). It can also catalyze the hydrolysis
CC of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-glycerol) (By similarity).
CC {ECO:0000250|UniProtKB:P97612, ECO:0000269|PubMed:15533037,
CC ECO:0000269|PubMed:32271712}.
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:15533037, ECO:0000269|PubMed:32271712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137;
CC Evidence={ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712};
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:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507;
CC Evidence={ECO:0000250|UniProtKB:P97612};
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:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35564;
CC Evidence={ECO:0000269|PubMed:15533037};
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-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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63125;
CC Evidence={ECO:0000269|PubMed:15533037};
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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63129;
CC Evidence={ECO:0000269|PubMed:15533037};
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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63141;
CC Evidence={ECO:0000269|PubMed:15533037};
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:0000305|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63145;
CC Evidence={ECO:0000305|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:0000305|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63149;
CC Evidence={ECO:0000305|PubMed:15533037};
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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63157;
CC Evidence={ECO:0000269|PubMed:15533037};
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:0000305|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63161;
CC Evidence={ECO:0000305|PubMed:15533037};
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:0000269|PubMed:15533037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63165;
CC Evidence={ECO:0000269|PubMed:15533037};
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=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:0000250|UniProtKB:P97612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63053;
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=(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:0000269|PubMed:32271712};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318;
CC Evidence={ECO:0000269|PubMed:32271712};
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:0000269|PubMed:32271712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109;
CC Evidence={ECO:0000269|PubMed:32271712};
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:0000269|PubMed:32271712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117;
CC Evidence={ECO:0000269|PubMed:32271712};
CC -!- ACTIVITY REGULATION: Inhibited the trifluoromethyl compound PF-3845.
CC {ECO:0000269|PubMed:32271712}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P97612}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:32271712}; 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 -!- DISRUPTION PHENOTYPE: Genetic ablation of FAAH bidirectionally
CC dysregulates a subset of intracellular, but not circulating, N-fatty
CC acyl amino acids. {ECO:0000269|PubMed:32271712}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; U82536; AAB58506.1; -; mRNA.
DR EMBL; AF098009; AAD11788.1; -; Genomic_DNA.
DR EMBL; AF097997; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF097998; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF097999; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098000; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098001; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098002; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098003; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098004; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098005; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098006; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098007; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AF098008; AAD11788.1; JOINED; Genomic_DNA.
DR EMBL; AK004985; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC006863; AAH06863.1; -; mRNA.
DR EMBL; BC052321; AAH52321.1; -; mRNA.
DR CCDS; CCDS18501.1; -.
DR RefSeq; NP_034303.3; NM_010173.4.
DR AlphaFoldDB; O08914; -.
DR SMR; O08914; -.
DR IntAct; O08914; 1.
DR MINT; O08914; -.
DR STRING; 10090.ENSMUSP00000041543; -.
DR BindingDB; O08914; -.
DR ChEMBL; CHEMBL3455; -.
DR DrugCentral; O08914; -.
DR GuidetoPHARMACOLOGY; 1400; -.
DR SwissLipids; SLP:000001980; -.
DR iPTMnet; O08914; -.
DR PhosphoSitePlus; O08914; -.
DR SwissPalm; O08914; -.
DR EPD; O08914; -.
DR jPOST; O08914; -.
DR MaxQB; O08914; -.
DR PaxDb; O08914; -.
DR PeptideAtlas; O08914; -.
DR PRIDE; O08914; -.
DR ProteomicsDB; 267703; -.
DR Antibodypedia; 1478; 400 antibodies from 36 providers.
DR DNASU; 14073; -.
DR Ensembl; ENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171.
DR GeneID; 14073; -.
DR KEGG; mmu:14073; -.
DR UCSC; uc008ufs.2; mouse.
DR CTD; 2166; -.
DR MGI; MGI:109609; Faah.
DR VEuPathDB; HostDB:ENSMUSG00000034171; -.
DR eggNOG; KOG1212; Eukaryota.
DR GeneTree; ENSGT00940000161237; -.
DR HOGENOM; CLU_009600_9_3_1; -.
DR InParanoid; O08914; -.
DR OMA; GMQPWKY; -.
DR OrthoDB; 852596at2759; -.
DR PhylomeDB; O08914; -.
DR TreeFam; TF314455; -.
DR BRENDA; 3.5.1.4; 3474.
DR BRENDA; 3.5.1.99; 3474.
DR Reactome; R-MMU-2142753; Arachidonic acid metabolism.
DR BioGRID-ORCS; 14073; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Faah; mouse.
DR PRO; PR:O08914; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O08914; protein.
DR Bgee; ENSMUSG00000034171; Expressed in dentate gyrus of hippocampal formation granule cell and 208 other tissues.
DR Genevisible; O08914; MM.
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; IMP:MGI.
DR GO; GO:0004040; F:amidase activity; ISO:MGI.
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:0016788; F:hydrolase activity, acting on ester bonds; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0102077; F:oleamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
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_0000105265"
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 CONFLICT 72
FT /note="E -> Q (in Ref. 4; AAH06863)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="S -> P (in Ref. 3; AK004985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63221 MW; 11B2DF6CBC110015 CRC64;
MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA GLETMDKAVQ
RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY LGKAWEVNKG TNCVTSYLTD
CETQLSQAPR QGLLYGVPVS LKECFSYKGH ASTLGLSLNE GVTSESDCVV VQVLKLQGAV
PFVHTNVPQS MLSYDCSNPL FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG
SIRFPSAFCG ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE
DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK QSLEAAGHTL
VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC LGDLVLVLKL PRWFKKLLSF
LLKPLFPRLA AFLNSMCPRS AEKLWELQHE IEMYRQSVIA QWKAMNLDVV LTPMLGPALD
LNTPGRATGA ISYTVLYNCL DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK
KGIGLPVAVQ CVALPWQEEL CLRFMREVER LMTPEKRPS
