Fatty-acid amide hydrolase 1
Details
- Name
- Fatty-acid amide hydrolase 1
- Synonyms
- 3.5.1.99
- Anandamide amidohydrolase 1
- FAAH1
- Fatty acid ester hydrolase
- Oleamide hydrolase 1
- Gene Name
- FAAH
- UniProtKB Entry
- O00519Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0011585|Fatty-acid amide hydrolase 1 MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQ RFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLAD CETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAV PFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGG SIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCE DMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTL VPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAF LVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALD LNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMK KSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS
- Number of residues
- 579
- Molecular Weight
- 63065.28
- Theoretical pI
- 7.72
- GO Classification
- Functionsamidase activity / identical protein binding / phospholipid bindingProcessesmonoacylglycerol catabolic process / positive regulation of vasoconstriction
- General Function
- Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:17015445, PubMed:19926788, PubMed:9122178). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed:17015445, PubMed:9122178). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:21049984). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (By similarity)
- Specific Function
- acylglycerol lipase activity
- Pfam Domain Function
- Amidase (PF01425)
- Signal Regions
- Not Available
- Transmembrane Regions
- 9-29
- Cellular Location
- Endomembrane system
- Gene sequence
>lcl|BSEQ0011586|Fatty-acid amide hydrolase 1 (FAAH) ATGGTGCAGTACGAGCTGTGGGCCGCGCTGCCTGGCGCCTCCGGGGTCGCCCTGGCCTGC TGCTTCGTGGCGGCGGCCGTGGCCCTGCGCTGGTCCGGGCGCCGGACGGCGCGGGGCGCG GTGGTCCGGGCGCGACAGAGGCAGCGAGCGGGCCTGGAGAACATGGACAGGGCGGCGCAG CGCTTCCGGCTCCAGAACCCAGACCTGGACTCAGAGGCGCTGCTAGCCCTGCCCCTGCCT CAGCTGGTGCAGAAGTTACACAGTAGAGAGCTGGCCCCTGAGGCCGTGCTCTTCACCTAT GTGGGAAAGGCCTGGGAAGTGAACAAAGGGACCAACTGTGTGACCTCCTATCTGGCTGAC TGTGAGACTCAGCTGTCTCAGGCCCCAAGGCAGGGCCTGCTCTATGGCGTCCCTGTGAGC CTCAAGGAGTGCTTCACCTACAAGGGCCAGGACTCCACGCTGGGCTTGAGCCTGAATGAA GGGGTGCCGGCGGAGTGCGACAGCGTAGTGGTGCATGTGCTGAAGCTGCAGGGTGCCGTG CCCTTCGTGCACACCAATGTTCCACAGTCCATGTTCAGCTATGACTGCAGTAACCCCCTC TTTGGCCAGACCGTGAACCCATGGAAGTCCTCCAAAAGCCCAGGGGGCTCCTCAGGGGGT GAAGGGGCCCTCATCGGGTCTGGAGGCTCCCCCCTGGGCTTAGGCACTGATATCGGAGGC AGCATCCGCTTCCCCTCCTCCTTCTGCGGCATCTGCGGCCTCAAGCCCACAGGGAACCGC CTCAGCAAGAGTGGCCTGAAGGGCTGTGTCTATGGACAGGAGGCAGTGCGTCTCTCCGTG GGCCCCATGGCCCGGGACGTGGAGAGCCTGGCACTGTGCCTGCGAGCCCTGCTGTGCGAG GACATGTTCCGCTTGGACCCCACTGTGCCTCCCTTGCCCTTCAGAGAAGAGGTCTACACC AGCTCTCAGCCCCTGCGTGTGGGGTACTATGAGACTGACAACTATACCATGCCCTCCCCG GCCATGAGGCGGGCCGTGCTGGAGACCAAACAGAGCCTTGAGGCTGCGGGGCACACGCTG GTTCCCTTCTTGCCAAGCAACATACCCCATGCTCTGGAGACCCTGTCAACAGGTGGGCTC TTCAGTGATGGTGGCCACACCTTCCTACAGAACTTCAAAGGTGATTTCGTGGACCCCTGC CTGGGGGACCTGGTCTCAATTCTGAAGCTTCCCCAATGGCTTAAAGGACTGCTGGCCTTC CTGGTGAAGCCTCTGCTGCCAAGGCTGTCAGCTTTCCTCAGCAACATGAAGTCTCGTTCG GCTGGAAAACTCTGGGAACTGCAGCACGAGATCGAGGTGTACCGCAAAACCGTGATTGCC CAGTGGAGGGCGCTGGACCTGGATGTGGTGCTGACCCCCATGCTGGCCCCTGCTCTGGAC TTGAATGCCCCAGGCAGGGCCACAGGGGCCGTCAGCTACACTATGCTGTACAACTGCCTG GACTTCCCTGCAGGGGTGGTGCCTGTCACCACGGTGACTGCTGAGGACGAGGCCCAGATG GAACATTACAGGGGCTACTTTGGGGATATCTGGGACAAGATGCTGCAGAAGGGCATGAAG AAGAGTGTGGGGCTGCCGGTGGCCGTGCAGTGTGTGGCTCTGCCCTGGCAAGAAGAGTTG TGTCTGCGGTTCATGCGGGAGGTGGAGCGACTGATGACCCCTGAAAAGCAGTCATCCTGA
- Chromosome Location
- 1
- Locus
- 1p33
- External Identifiers
Resource Link UniProtKB ID O00519 UniProtKB Entry Name FAAH1_HUMAN GenBank Protein ID 2149156 GenBank Gene ID U82535 GeneCard ID FAAH GenAtlas ID FAAH HGNC ID HGNC:3553 KEGG ID hsa:2166 IUPHAR/Guide To Pharmacology ID 1400 NCBI Gene ID 2166 - General References
- Giang DK, Cravatt BF: Molecular characterization of human and mouse fatty acid amide hydrolases. Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2238-42. [Article]
- Wan M, Cravatt BF, Ring HZ, Zhang X, Francke U: Conserved chromosomal location and genomic structure of human and mouse fatty-acid amide hydrolase genes and evaluation of clasper as a candidate neurological mutation. Genomics. 1998 Dec 15;54(3):408-14. [Article]
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- Wei BQ, Mikkelsen TS, McKinney MK, Lander ES, Cravatt BF: A second fatty acid amide hydrolase with variable distribution among placental mammals. J Biol Chem. 2006 Dec 1;281(48):36569-78. Epub 2006 Oct 2. [Article]
- Sipe JC, Chiang K, Gerber AL, Beutler E, Cravatt BF: A missense mutation in human fatty acid amide hydrolase associated with problem drug use. Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8394-9. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Chiang KP, Gerber AL, Sipe JC, Cravatt BF: Reduced cellular expression and activity of the P129T mutant of human fatty acid amide hydrolase: evidence for a link between defects in the endocannabinoid system and problem drug use. Hum Mol Genet. 2004 Sep 15;13(18):2113-9. Epub 2004 Jul 14. [Article]
- Flanagan JM, Gerber AL, Cadet JL, Beutler E, Sipe JC: The fatty acid amide hydrolase 385 A/A (P129T) variant: haplotype analysis of an ancient missense mutation and validation of risk for drug addiction. Hum Genet. 2006 Nov;120(4):581-8. Epub 2006 Sep 14. [Article]
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- Sim MS, Hatim A, Reynolds GP, Mohamed Z: Association of a functional FAAH polymorphism with methamphetamine-induced symptoms and dependence in a Malaysian population. Pharmacogenomics. 2013 Apr;14(5):505-14. doi: 10.2217/pgs.13.25. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Fatty-acid amide hydrolase 1 (Humans) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Methoxy arachidonyl fluorophosphonate experimental unknown target Details Thiopental approved, vet_approved unknown target inhibitor Details Propofol approved, investigational, vet_approved unknown enzyme substrate Details 1-Dodecanol experimental unknown target Details 4-(quinolin-3-ylmethyl)piperidine-1-carboxylic acid experimental unknown target Details 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid experimental unknown target Details Cannabidiol approved, investigational unknown enzyme inhibitor Details Fostamatinib approved, investigational unknown target inhibitor Details Medical Cannabis experimental, investigational unknown target inhibitor Details Nabiximols investigational unknown target inhibitorinducer Details Acetaminophen approved unknown enzyme substrate Details JNJ-42165279 investigational yes target inhibitor Details