FAAH2

Fatty acid amide hydrolase 2 or FAAH2 is a member of the serine hydrolase family of enzymes.^[3]

FAAH2
Identifiers
Aliases	FAAH2, AMDD, fatty acid amide hydrolase 2
External IDs	OMIM: 300654; HomoloGene: 45263; GeneCards: FAAH2; OMA:FAAH2 - orthologs
Gene location (Human) Chr. X chromosome (human)[1] Band Xp11.21 Start 57,286,706 bp[1] End 57,489,193 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube body of pancreas right lobe of liver olfactory zone of nasal mucosa pituitary gland anterior pituitary islet of Langerhans skin of abdomen skin of leg minor salivary glands n/a More reference expression data BioGPS n/a
Gene ontology Molecular function hydrolase activity fatty acid amide hydrolase activity Cellular component integral component of membrane lipid droplet membrane Biological process arachidonic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 158584 n/a Ensembl ENSG00000165591 n/a UniProt Q6GMR7 n/a RefSeq (mRNA) NM_174912 NM_001353840 NM_001353841 n/a RefSeq (protein) NP_777572 NP_001340769 NP_001340770 n/a Location (UCSC) Chr X: 57.29 – 57.49 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Fatty acid amide hydrolase 2 degrades many types of fatty acid amides, including the sleep-inducing oleamide and endocannabinoids such as anandamide.^[4] It has a tissue distribution quite distinct from the paralogous FAAH (or "FAAH1"). Compared to FAAH, it is less active on N-acyl ethanolamines (e.g. anandamide) and N-acyl taurines.^[3]

OrthoDB indicates that FAAH2 (as a gene distinct from FAAH) has orthologs all across Metazoa, with the notable exclusion of rodents.^[5] This complicates the translation of FAAH-related results from rodent models to human biology.^[3]

Clinical significance

Defects in this enzyme have been associated with neurologic and psychiatric disorders. Specifically, a Canadian male with autism, anxiety, severe dysarthria, and a number of other issues have a Ala458Ser mutation inherited from his healthy carrier mother. In cell models this mutation is associated with a decreased function of this gene. This patient has a very abnormal blood lipid composition consistent with a loss of function.^[6]

ClinVar reports a missense mutation that produces an early stop codon (Trp392Ter) is associated with Meckel-like syndrome.^[7]

UniProt Variant Viewer lists a large number of other variants found in surveyed human genomes. Several are predicted to have consequences by PolyPhen and/or SIFT.^[4]