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Fatty-acid amide hydrolase 1 (EC 3.5.1.99) (Anandamide amidohydrolase 1) (Oleamide hydrolase 1)

 FAAH1_HUMAN             Reviewed;         579 AA.
O00519; D3DQ19; Q52M86; Q5TDF8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 2.
20-JUN-2018, entry version 156.
RecName: Full=Fatty-acid amide hydrolase 1;
EC=3.5.1.99;
AltName: Full=Anandamide amidohydrolase 1;
AltName: Full=Oleamide hydrolase 1;
Name=FAAH; Synonyms=FAAH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9122178; DOI=10.1073/pnas.94.6.2238;
Giang D.K., Cravatt B.F.;
"Molecular characterization of human and mouse fatty acid amide
hydrolases.";
Proc. Natl. Acad. Sci. U.S.A. 94:2238-2242(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9878243; DOI=10.1006/geno.1998.5597;
Wan M., Cravatt B.F., Ring H.Z., 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 54:408-414(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-129.
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-129.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 456-463.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, ENZYME REGULATION, AND
TISSUE SPECIFICITY.
PubMed=17015445; DOI=10.1074/jbc.M606646200;
Wei B.Q., Mikkelsen T.S., McKinney M.K., Lander E.S., Cravatt B.F.;
"A second fatty acid amide hydrolase with variable distribution among
placental mammals.";
J. Biol. Chem. 281:36569-36578(2006).
[9]
POLYMORPHISM, ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO
POLYSUBSTANCE ABUSE, AND CHARACTERIZATION OF VARIANT THR-129.
PubMed=12060782; DOI=10.1073/pnas.082235799;
Sipe J.C., Chiang K., Gerber A.L., Beutler E., Cravatt B.F.;
"A missense mutation in human fatty acid amide hydrolase associated
with problem drug use.";
Proc. Natl. Acad. Sci. U.S.A. 99:8394-8399(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[11]
CHARACTERIZATION OF VARIANT THR-129.
PubMed=15254019; DOI=10.1093/hmg/ddh216;
Chiang K.P., Gerber A.L., Sipe J.C., Cravatt B.F.;
"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. 13:2113-2119(2004).
[12]
ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO POLYSUBSTANCE
ABUSE.
PubMed=16972078; DOI=10.1007/s00439-006-0250-x;
Flanagan J.M., Gerber A.L., Cadet J.L., Beutler E., Sipe J.C.;
"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. 120:581-588(2006).
[13]
VARIANT [LARGE SCALE ANALYSIS] ASP-345.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[14]
ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO METHAMPHETAMINE
DEPENDENCE.
PubMed=23556448; DOI=10.2217/pgs.13.25;
Sim M.S., Hatim A., Reynolds G.P., Mohamed Z.;
"Association of a functional FAAH polymorphism with methamphetamine-
induced symptoms and dependence in a Malaysian population.";
Pharmacogenomics 14:505-514(2013).
-!- 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. {ECO:0000269|PubMed:17015445}.
-!- CATALYTIC ACTIVITY: Anandamide + H(2)O = arachidonic acid +
ethanolamine.
-!- CATALYTIC ACTIVITY: Oleamide + H(2)O = oleic acid + NH(3).
-!- ENZYME REGULATION: Inhibited by O-aryl carbamates and alpha-keto
heterocytes. {ECO:0000269|PubMed:17015445}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- INTERACTION:
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-1389829, EBI-945833;
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000269|PubMed:17015445}; Single-pass membrane protein
{ECO:0000269|PubMed:17015445}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:17015445}. Note=Seems to be attached to
intracellular membranes and a portion of the cytoskeletal network.
-!- TISSUE SPECIFICITY: Highly expressed in the brain, small
intestine, pancreas, skeletal muscle and testis. Also expressed in
the kidney, liver, lung, placenta and prostate.
{ECO:0000269|PubMed:17015445}.
-!- POLYMORPHISM: Genetic variations in FAAH can be associated with
susceptibility to polysubstance abuse [MIM:606581]. At
homozygosity, variant Thr-129 is strongly associated with drug and
alcohol abuse, and methamphetamine dependence.
{ECO:0000269|PubMed:12060782, ECO:0000269|PubMed:16972078,
ECO:0000269|PubMed:23556448}.
-!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/faah/";
-----------------------------------------------------------------------
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EMBL; U82535; AAB58505.1; -; mRNA.
EMBL; AF098019; AAD13768.1; -; Genomic_DNA.
EMBL; AF098010; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098011; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098012; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098013; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098014; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098015; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098016; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098017; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AF098018; AAD13768.1; JOINED; Genomic_DNA.
EMBL; AY842444; AAV88095.1; -; Genomic_DNA.
EMBL; AL122001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06912.1; -; Genomic_DNA.
EMBL; CH471059; EAX06919.1; -; Genomic_DNA.
EMBL; BC093632; AAH93632.1; -; mRNA.
EMBL; BC110404; AAI10405.1; -; mRNA.
EMBL; BC111941; AAI11942.1; -; mRNA.
CCDS; CCDS535.1; -.
RefSeq; NP_001432.2; NM_001441.2.
UniGene; Hs.720143; -.
ProteinModelPortal; O00519; -.
SMR; O00519; -.
BioGrid; 108464; 2.
IntAct; O00519; 3.
STRING; 9606.ENSP00000243167; -.
BindingDB; O00519; -.
ChEMBL; CHEMBL2243; -.
DrugBank; DB06894; 1-DODECANOL.
DrugBank; DB08400; 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid.
DrugBank; DB08385; 4-(quinolin-3-ylmethyl)piperidine-1-carboxylic acid.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB02465; Methoxy arachidonyl fluorophosphonate.
DrugBank; DB00818; Propofol.
DrugBank; DB00599; Thiopental.
GuidetoPHARMACOLOGY; 1400; -.
SwissLipids; SLP:000000145; -.
iPTMnet; O00519; -.
PhosphoSitePlus; O00519; -.
BioMuta; FAAH; -.
EPD; O00519; -.
MaxQB; O00519; -.
PaxDb; O00519; -.
PeptideAtlas; O00519; -.
PRIDE; O00519; -.
ProteomicsDB; 47952; -.
Ensembl; ENST00000243167; ENSP00000243167; ENSG00000117480.
GeneID; 2166; -.
KEGG; hsa:2166; -.
UCSC; uc001cpu.3; human.
CTD; 2166; -.
DisGeNET; 2166; -.
EuPathDB; HostDB:ENSG00000117480.15; -.
GeneCards; FAAH; -.
H-InvDB; HIX0000550; -.
HGNC; HGNC:3553; FAAH.
HPA; HPA007425; -.
MalaCards; FAAH; -.
MIM; 602935; gene.
MIM; 606581; phenotype.
neXtProt; NX_O00519; -.
OpenTargets; ENSG00000117480; -.
PharmGKB; PA27955; -.
eggNOG; KOG1212; Eukaryota.
eggNOG; COG0154; LUCA.
GeneTree; ENSGT00550000074673; -.
HOGENOM; HOG000016500; -.
HOVERGEN; HBG005632; -.
InParanoid; O00519; -.
KO; K15528; -.
OMA; TSMPGQE; -.
OrthoDB; EOG091G05JU; -.
PhylomeDB; O00519; -.
TreeFam; TF314455; -.
BioCyc; MetaCyc:HS04139-MONOMER; -.
BRENDA; 3.5.1.4; 2681.
BRENDA; 3.5.1.99; 2681.
Reactome; R-HSA-2142753; Arachidonic acid metabolism.
SIGNOR; O00519; -.
ChiTaRS; FAAH; human.
GenomeRNAi; 2166; -.
PRO; PR:O00519; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117480; -.
ExpressionAtlas; O00519; baseline and differential.
Genevisible; O00519; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
GO; GO:0047372; F:acylglycerol lipase activity; IEA:Ensembl.
GO; GO:0004040; F:amidase activity; IEA:InterPro.
GO; GO:0103073; F:anandamide amidohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0017064; F:fatty acid amide hydrolase activity; IDA:UniProtKB.
GO; GO:0102077; F:oleamide hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
Gene3D; 3.90.1300.10; -; 1.
InterPro; IPR000120; Amidase.
InterPro; IPR020556; Amidase_CS.
InterPro; IPR023631; Amidase_dom.
InterPro; IPR036928; AS_sf.
InterPro; IPR030560; FAAH.
PANTHER; PTHR11895; PTHR11895; 1.
PANTHER; PTHR11895:SF91; PTHR11895:SF91; 1.
Pfam; PF01425; Amidase; 1.
SUPFAM; SSF75304; SSF75304; 1.
PROSITE; PS00571; AMIDASES; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Hydrolase; Membrane; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 579 Fatty-acid amide hydrolase 1.
/FTId=PRO_0000105264.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 403 Cytoplasmic. {ECO:0000250}.
INTRAMEM 404 433 {ECO:0000250}.
TOPO_DOM 434 579 Cytoplasmic. {ECO:0000250}.
REGION 238 241 Substrate binding. {ECO:0000250}.
ACT_SITE 142 142 Charge relay system. {ECO:0000250}.
ACT_SITE 217 217 Charge relay system. {ECO:0000250}.
ACT_SITE 241 241 Acyl-ester intermediate. {ECO:0000250}.
BINDING 191 191 Substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 217 217 Substrate. {ECO:0000250}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 129 129 P -> T (polymorphism associated with
susceptibility to drug abuse; the mutant
enzyme is more sensitive to proteolytic
degradation; displays reduced cellular
expression probably due to a post-
translational mechanism preceding
productive folding; dbSNP:rs324420).
{ECO:0000269|PubMed:12060782,
ECO:0000269|PubMed:15254019,
ECO:0000269|PubMed:16972078,
ECO:0000269|PubMed:23556448,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_013563.
VARIANT 345 345 A -> D (in a breast cancer sample;
somatic mutation; dbSNP:rs772931153).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035704.
CONFLICT 47 47 R -> K (in Ref. 1; AAB58505 and 2;
AAD13768). {ECO:0000305}.
SEQUENCE 579 AA; 63066 MW; 633A92DC36940C18 CRC64;
MVQYELWAAL PGASGVALAC CFVAAAVALR WSGRRTARGA VVRARQRQRA GLENMDRAAQ
RFRLQNPDLD SEALLALPLP QLVQKLHSRE LAPEAVLFTY VGKAWEVNKG TNCVTSYLAD
CETQLSQAPR QGLLYGVPVS LKECFTYKGQ DSTLGLSLNE GVPAECDSVV VHVLKLQGAV
PFVHTNVPQS MFSYDCSNPL FGQTVNPWKS SKSPGGSSGG EGALIGSGGS PLGLGTDIGG
SIRFPSSFCG ICGLKPTGNR LSKSGLKGCV YGQEAVRLSV GPMARDVESL ALCLRALLCE
DMFRLDPTVP PLPFREEVYT SSQPLRVGYY ETDNYTMPSP AMRRAVLETK QSLEAAGHTL
VPFLPSNIPH ALETLSTGGL FSDGGHTFLQ NFKGDFVDPC LGDLVSILKL PQWLKGLLAF
LVKPLLPRLS AFLSNMKSRS AGKLWELQHE IEVYRKTVIA QWRALDLDVV LTPMLAPALD
LNAPGRATGA VSYTMLYNCL DFPAGVVPVT TVTAEDEAQM EHYRGYFGDI WDKMLQKGMK
KSVGLPVAVQ CVALPWQEEL CLRFMREVER LMTPEKQSS


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