Fatty-acid amide hydrolase 1
Details
- Name
- Fatty-acid amide hydrolase 1
- Synonyms
- 3.5.1.99
- Anandamide amidohydrolase 1
- FAAH1
- Oleamide hydrolase 1
- Gene Name
- FAAH
- Organism
- Humans
- 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
- Functionsacylglycerol lipase activity / carbon-nitrogen ligase activity, with glutamine as amido-N-donor / fatty acid amide hydrolase activityProcessesarachidonic acid metabolic process / fatty acid catabolic process / small molecule metabolic processComponentscytoskeleton / endoplasmic reticulum membrane / integral component of membrane / organelle membrane
- General Function
- Fatty acid amide hydrolase activity
- Specific Function
- Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates.
- Pfam Domain Function
- Amidase (PF01425)
- 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
- 1p35-p34
- External Identifiers
Resource Link UniProtKB ID O00519 UniProtKB Entry Name FAAH1_HUMAN GenBank Protein ID 2149156 GenBank Gene ID U82535 GenAtlas ID FAAH HGNC ID HGNC:3553 - 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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- 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]
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- 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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Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02465 Methoxy arachidonyl fluorophosphonate experimental unknown Details DB00599 Thiopental approved, vet_approved unknown inhibitor Details DB00818 Propofol approved, investigational, vet_approved unknown substrate Details DB06894 1-Dodecanol experimental unknown Details DB08385 4-(quinolin-3-ylmethyl)piperidine-1-carboxylic acid experimental unknown Details DB08400 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid experimental unknown Details DB09061 Cannabidiol approved, investigational unknown inhibitor Details DB12010 Fostamatinib approved, investigational unknown inhibitor Details DB14009 Medical Cannabis experimental, investigational unknown inhibitor Details DB14011 Nabiximols investigational unknown inhibitorinducer Details DB00316 Acetaminophen approved unknown substrate Details