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Protein

Fatty-acid amide hydrolase 1

Gene

Faah

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Anandamide + H2O = arachidonic acid + ethanolamine.
Oleamide + H2O = oleic acid + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei142 – 1421Charge relay system
Binding sitei191 – 1911Substrate; via carbonyl oxygen
Active sitei217 – 2171Charge relay system
Binding sitei217 – 2171Substrate
Active sitei241 – 2411Acyl-ester intermediate

GO - Molecular functioni

  • amidase activity Source: RGD
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
  • fatty acid amide hydrolase activity Source: UniProtKB
  • hydrolase activity, acting on ester bonds Source: RGD
  • lipid binding Source: RGD
  • phospholipid binding Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • fatty acid catabolic process Source: UniProtKB
  • fatty acid metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.4. 5301.
3.5.1.99. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty-acid amide hydrolase 1 (EC:3.5.1.99)
Alternative name(s):
Anandamide amidohydrolase 1
Oleamide hydrolase 1
Gene namesi
Name:Faah
Synonyms:Faah1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi61808. Faah.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 403374CytoplasmicCuratedAdd
BLAST
Intramembranei404 – 43330CuratedAdd
BLAST
Topological domaini434 – 579146CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: RGD
  • organelle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi142 – 1421K → A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217. 1 Publication
Mutagenesisi217 – 2171S → A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Fatty-acid amide hydrolase 1PRO_0000105267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP97612.
PRIDEiP97612.

PTM databases

PhosphoSiteiP97612.

Expressioni

Tissue specificityi

Found in neuronal cells throughout the CNS. Expressed in liver and brain, and to a lesser extent in spleen, lung, kidney and testes.1 Publication

Developmental stagei

In the CNS it accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood.

Gene expression databases

GenevestigatoriP97612.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-46284N.
MINTiMINT-4567335.
STRINGi10116.ENSRNOP00000015667.

Structurei

Secondary structure

1
579
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 6531Combined sources
Helixi71 – 766Combined sources
Helixi79 – 879Combined sources
Beta strandi89 – 913Combined sources
Helixi93 – 11119Combined sources
Beta strandi114 – 1174Combined sources
Helixi121 – 1277Combined sources
Turni133 – 1364Combined sources
Beta strandi138 – 1425Combined sources
Helixi157 – 1593Combined sources
Beta strandi164 – 1663Combined sources
Helixi169 – 1768Combined sources
Beta strandi180 – 1856Combined sources
Helixi189 – 1913Combined sources
Beta strandi193 – 1953Combined sources
Turni199 – 2013Combined sources
Beta strandi216 – 2183Combined sources
Helixi219 – 2268Combined sources
Beta strandi231 – 24010Combined sources
Helixi243 – 2497Combined sources
Beta strandi252 – 2554Combined sources
Helixi258 – 2603Combined sources
Beta strandi279 – 2868Combined sources
Helixi287 – 29711Combined sources
Helixi300 – 3056Combined sources
Helixi316 – 3194Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi334 – 3363Combined sources
Helixi340 – 35516Combined sources
Beta strandi359 – 3624Combined sources
Helixi368 – 3736Combined sources
Helixi375 – 3806Combined sources
Turni382 – 3854Combined sources
Helixi386 – 3894Combined sources
Helixi390 – 3923Combined sources
Helixi399 – 4013Combined sources
Helixi404 – 4085Combined sources
Helixi412 – 42211Combined sources
Turni423 – 4253Combined sources
Helixi427 – 4359Combined sources
Beta strandi436 – 4383Combined sources
Helixi441 – 46424Combined sources
Beta strandi468 – 4736Combined sources
Helixi484 – 4863Combined sources
Helixi488 – 4914Combined sources
Helixi492 – 4998Combined sources
Beta strandi504 – 5118Combined sources
Helixi514 – 5207Combined sources
Helixi530 – 5389Combined sources
Beta strandi546 – 5527Combined sources
Helixi558 – 57215Combined sources
Helixi574 – 5763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT5X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P37-573[»]
2VYAX-ray2.75A/B32-579[»]
2WAPX-ray2.80A/B31-573[»]
2WJ1X-ray1.84A/B30-579[»]
2WJ2X-ray2.55A/B30-579[»]
3K7FX-ray1.95A/B30-579[»]
3K83X-ray2.25A/B30-579[»]
3K84X-ray2.25A/B30-579[»]
3LJ6X-ray2.42A/B30-579[»]
3LJ7X-ray2.30A/B30-579[»]
3OJ8X-ray1.90A/B30-579[»]
3PPMX-ray1.78A/B30-579[»]
3PR0X-ray2.20A/B30-579[»]
3QJ8X-ray2.90A/B32-579[»]
3QJ9X-ray2.30A/B32-579[»]
3QK5X-ray2.20A/B32-579[»]
3QKVX-ray3.10A/B32-579[»]
4DO3X-ray2.25A/B32-575[»]
4HBPX-ray2.91A/B30-579[»]
4J5PX-ray2.30A/B30-579[»]
ProteinModelPortaliP97612.
SMRiP97612. Positions 37-573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97612.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2414Substrate binding

Sequence similaritiesi

Belongs to the amidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiP97612.
KOiK15528.
OMAiLKECFTY.
OrthoDBiEOG72JWG0.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR030560. FAAH.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PTHR11895:SF51. PTHR11895:SF51. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMiSSF75304. SSF75304. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSEVWTTL SGVSGVCLAC SLLSAAVVLR WTGRQKARGA ATRARQKQRA
60 70 80 90 100
SLETMDKAVQ RFRLQNPDLD SEALLTLPLL QLVQKLQSGE LSPEAVFFTY
110 120 130 140 150
LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH
160 170 180 190 200
DSTLGLSLNE GMPSESDCVV VQVLKLQGAV PFVHTNVPQS MLSFDCSNPL
210 220 230 240 250
FGQTMNPWKS SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG
260 270 280 290 300
ICGLKPTGNR LSKSGLKGCV YGQTAVQLSL GPMARDVESL ALCLKALLCE
310 320 330 340 350
HLFTLDPTVP PLPFREEVYR SSRPLRVGYY ETDNYTMPSP AMRRALIETK
360 370 380 390 400
QRLEAAGHTL IPFLPNNIPY ALEVLSAGGL FSDGGRSFLQ NFKGDFVDPC
410 420 430 440 450
LGDLILILRL PSWFKRLLSL LLKPLFPRLA AFLNSMRPRS AEKLWKLQHE
460 470 480 490 500
IEMYRQSVIA QWKAMNLDVL LTPMLGPALD LNTPGRATGA ISYTVLYNCL
510 520 530 540 550
DFPAGVVPVT TVTAEDDAQM ELYKGYFGDI WDIILKKAMK NSVGLPVAVQ
560 570
CVALPWQEEL CLRFMREVEQ LMTPQKQPS
Length:579
Mass (Da):63,357
Last modified:May 1, 1997 - v1
Checksum:i606491C0B033E1AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72497 mRNA. Translation: AAB26961.1.
BC091148 mRNA. Translation: AAH91148.1.
RefSeqiNP_077046.1. NM_024132.3.
XP_003750049.1. XM_003750001.3.
XP_008774266.1. XM_008776044.1.
UniGeneiRn.89119.

Genome annotation databases

EnsembliENSRNOT00000015667; ENSRNOP00000015667; ENSRNOG00000045949.
ENSRNOT00000015961; ENSRNOP00000015961; ENSRNOG00000011019.
GeneIDi100911581.
29347.
KEGGirno:100911581.
rno:29347.
UCSCiRGD:61808. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72497 mRNA. Translation: AAB26961.1.
BC091148 mRNA. Translation: AAH91148.1.
RefSeqiNP_077046.1. NM_024132.3.
XP_003750049.1. XM_003750001.3.
XP_008774266.1. XM_008776044.1.
UniGeneiRn.89119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT5X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P37-573[»]
2VYAX-ray2.75A/B32-579[»]
2WAPX-ray2.80A/B31-573[»]
2WJ1X-ray1.84A/B30-579[»]
2WJ2X-ray2.55A/B30-579[»]
3K7FX-ray1.95A/B30-579[»]
3K83X-ray2.25A/B30-579[»]
3K84X-ray2.25A/B30-579[»]
3LJ6X-ray2.42A/B30-579[»]
3LJ7X-ray2.30A/B30-579[»]
3OJ8X-ray1.90A/B30-579[»]
3PPMX-ray1.78A/B30-579[»]
3PR0X-ray2.20A/B30-579[»]
3QJ8X-ray2.90A/B32-579[»]
3QJ9X-ray2.30A/B32-579[»]
3QK5X-ray2.20A/B32-579[»]
3QKVX-ray3.10A/B32-579[»]
4DO3X-ray2.25A/B32-575[»]
4HBPX-ray2.91A/B30-579[»]
4J5PX-ray2.30A/B30-579[»]
ProteinModelPortaliP97612.
SMRiP97612. Positions 37-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46284N.
MINTiMINT-4567335.
STRINGi10116.ENSRNOP00000015667.

Chemistry

BindingDBiP97612.
ChEMBLiCHEMBL3229.

PTM databases

PhosphoSiteiP97612.

Proteomic databases

PaxDbiP97612.
PRIDEiP97612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015667; ENSRNOP00000015667; ENSRNOG00000045949.
ENSRNOT00000015961; ENSRNOP00000015961; ENSRNOG00000011019.
GeneIDi100911581.
29347.
KEGGirno:100911581.
rno:29347.
UCSCiRGD:61808. rat.

Organism-specific databases

CTDi2166.
RGDi61808. Faah.

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiP97612.
KOiK15528.
OMAiLKECFTY.
OrthoDBiEOG72JWG0.

Enzyme and pathway databases

BRENDAi3.5.1.4. 5301.
3.5.1.99. 5301.

Miscellaneous databases

EvolutionaryTraceiP97612.
NextBioi608844.
PROiP97612.

Gene expression databases

GenevestigatoriP97612.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR030560. FAAH.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PTHR11895:SF51. PTHR11895:SF51. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMiSSF75304. SSF75304. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides."
    Cravatt B.F., Giang D.K., Mayfield S.P., Boger D.L., Lerner R.A., Gilula N.B.
    Nature 384:83-87(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  3. "Molecular characterization of human and mouse fatty acid amide hydrolases."
    Giang D.K., Cravatt B.F.
    Proc. Natl. Acad. Sci. U.S.A. 94:2238-2242(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system."
    Thomas E.A., Cravatt B.F., Danielson P.E., Gilula N.B., Sutcliffe J.G.
    J. Neurosci. Res. 50:1047-1052(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase."
    McKinney M.K., Cravatt B.F.
    J. Biol. Chem. 278:37393-37399(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-142 AND SER-217.
  6. "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling."
    Bracey M.H., Hanson M.A., Masuda K.R., Stevens R.C., Cravatt B.F.
    Science 298:1793-1796(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-573 IN COMPLEX WITH INHIBITOR METHOXY-ARACHIDONYL FLUOROPHOSPHATE, SUBUNIT, TOPOLOGY.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 32-579 IN COMPLEX WITH INHIBITOR PF-750, TOPOLOGY, SUBUNIT.

Entry informationi

Entry nameiFAAH1_RAT
AccessioniPrimary (citable) accession number: P97612
Secondary accession number(s): Q5BKA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: May 27, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.