Q6GMR7 · FAAH2_HUMAN
- ProteinFatty-acid amide hydrolase 2
- GeneFAAH2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids532 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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).
Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates
Hydrolyzes monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates
Catalytic activity
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl) ethanolamine = (9Z)-octadecenoate + ethanolamineThis reaction proceeds in the forward direction.
- H2O + N-hexadecanoylethanolamine = ethanolamine + hexadecanoateThis reaction proceeds in the forward direction.
Activity regulation
Inhibited by O-aryl carbamates and alpha-keto heterocytes.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
7.9 μM | anandamide | N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine | ||||
4.3 μM | palmitoylethanolamine | N-hexadecanoylethanolamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.2 nmol/min/mg | 9.0 | for palmitoylethanolamine (N-hexadecanoylethanolamine) | |||
1.21 nmol/min/mg | 9.0 | for palmitoylethanolamine (N-hexadecanoylethanolamine) | |||
0.46 nmol/min/mg | 9.0 | for anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) | |||
0.71 nmol/min/mg | 9.0 | for anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine) |
pH Dependence
Optimum pH is around 9.0.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 131 | Charge relay system | ||||
Sequence: K | ||||||
Active site | 206 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 230 | Acyl-ester intermediate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lipid droplet | |
Cellular Component | membrane | |
Molecular Function | fatty acid amide hydrolase activity | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameFatty-acid amide hydrolase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6GMR7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 11-31 | Helical | ||||
Sequence: LFLLRALGFLIGLVGRAALVL |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 732 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000291993 | 1-532 | Fatty-acid amide hydrolase 2 | |||
Sequence: MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in kidney, liver, lung, prostate, heart and ovary.
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length532
- Mass (Da)58,304
- Last updated2004-07-19 v1
- Checksum1D83E34BFF186E5E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 98 | in Ref. 1; BAB71007 | ||||
Sequence: K → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK055766 EMBL· GenBank· DDBJ | BAB71007.1 EMBL· GenBank· DDBJ | mRNA | ||
AL928898 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590394 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL606754 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z83745 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC048279 EMBL· GenBank· DDBJ | AAH48279.1 EMBL· GenBank· DDBJ | mRNA | ||
BC073922 EMBL· GenBank· DDBJ | AAH73922.1 EMBL· GenBank· DDBJ | mRNA |