Fatty-acid amide hydrolase 1

FAAH
Identifiers
Aliases	FAAH, fatty acid amide hydrolase, FAAH-1, PSAB
External IDs	OMIM: 602935; MGI: 109609; HomoloGene: 68184; GeneCards: FAAH; OMA:FAAH - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	46,413,848 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	115,875,123 bp
RNA expression pattern
	Top expressed in
	right lobe of thyroid gland; ; left lobe of thyroid gland; ; mucosa of transverse colon; ; C1 segment; ; right hemisphere of cerebellum; ; left testis; ; right testis; ; right lobe of liver; ; nucleus accumbens; ; body of pancreas;
	Top expressed in
	dentate gyrus of hippocampal formation granule cell; ; left lobe of liver; ; primary visual cortex; ; CA3 field; ; perirhinal cortex; ; superior frontal gyrus; ; entorhinal cortex; ; right kidney; ; gallbladder; ; hippocampus proper;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding; hydrolase activity; acylglycerol lipase activity; fatty acid amide hydrolase activity; amidase activity;
Cellular component	cytoplasm; organelle membrane; integral component of membrane; cytoskeleton; endoplasmic reticulum membrane; endomembrane system; membrane;
Biological process	arachidonic acid metabolic process; fatty acid catabolic process; monoacylglycerol catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	2166
	14073
	ENSG00000117480
	ENSMUSG00000034171
	O00519
	O08914
	NM_001441
	NM_010173
	NP_001432
	NP_034303
	Wikidata
View/Edit Human	View/Edit Mouse

Fatty-acid amide hydrolase 1 (FAAH)^[5] is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide (AEA), an N-acylethanolamine (NAE) in 1993.^[6] In humans, it is encoded by the gene FAAH.^[7]^[8]^[9]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000117480 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034171 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "UniProt". www.uniprot.org. Retrieved 18 July 2023.
^ Deutsch DG, Chin SA (September 1993). "Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist". Biochemical Pharmacology. 46 (5): 791–796. doi:10.1016/0006-2952(93)90486-G. PMID 8373432.
^ Cravatt BF, Giang DK, Mayfield SP, Boger DL, Lerner RA, Gilula NB (November 1996). "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides". Nature. 384 (6604): 83–87. Bibcode:1996Natur.384...83C. doi:10.1038/384083a0. PMID 8900284. S2CID 4288981.
^ Giang DK, Cravatt BF (March 1997). "Molecular characterization of human and mouse fatty acid amide hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 94 (6): 2238–2242. Bibcode:1997PNAS...94.2238G. doi:10.1073/pnas.94.6.2238. PMC 20071. PMID 9122178.
^ PDB: 1MT5; Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (November 2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling". Science. 298 (5599): 1793–1796. Bibcode:2002Sci...298.1793B. doi:10.1126/science.1076535. PMID 12459591. S2CID 22656813.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000117480 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034171 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[UniProt-5] "UniProt". www.uniprot.org. Retrieved 18 July 2023.

[pmid8373432-6] Deutsch DG, Chin SA (September 1993). "Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist". Biochemical Pharmacology. 46 (5): 791–796. doi:10.1016/0006-2952(93)90486-G. PMID 8373432.

[pmid8900284-7] Cravatt BF, Giang DK, Mayfield SP, Boger DL, Lerner RA, Gilula NB (November 1996). "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides". Nature. 384 (6604): 83–87. Bibcode:1996Natur.384...83C. doi:10.1038/384083a0. PMID 8900284. S2CID 4288981.

[pmid9122178-8] Giang DK, Cravatt BF (March 1997). "Molecular characterization of human and mouse fatty acid amide hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 94 (6): 2238–2242. Bibcode:1997PNAS...94.2238G. doi:10.1073/pnas.94.6.2238. PMC 20071. PMID 9122178.

[pmid12459591-9] PDB: 1MT5; Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (November 2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling". Science. 298 (5599): 1793–1796. Bibcode:2002Sci...298.1793B. doi:10.1126/science.1076535. PMID 12459591. S2CID 22656813.

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