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FAAH

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:9122178, PubMed:17015445, PubMed:19926788). Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (PubMed:9122178, PubMed:17015445). 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).

Sequence similarities

Belongs to the amidase family.

Tissue specificity

Highly expressed in the brain, small intestine, pancreas, skeletal muscle and testis. Also expressed in the kidney, liver, lung, placenta and prostate.

Cellular localization

  • Endomembrane system
  • Single-pass membrane protein
  • Cytoplasm
  • Cytoskeleton
  • Seems to be attached to intracellular membranes and a portion of the cytoskeletal network.

Alternative names

  • Fatty-acid amide hydrolase 1
  • Anandamide amidohydrolase 1
  • Fatty acid ester hydrolase
  • Oleamide hydrolase 1
  • FAAH1
  • FAAH

Target type

Proteins

Primary research area

Immunology & Infectious Disease

Molecular weight

63066Da