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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)DescriptionActionsGraphical viewLength
Active sitei142Charge relay system1
Binding sitei191Substrate; via carbonyl oxygen1
Active sitei217Charge relay system1
Binding sitei217Substrate1
Active sitei241Acyl-ester intermediate1

GO - Molecular functioni

  • amidase activity Source: RGD
  • anandamide amidohydrolase activity Source: UniProtKB-EC
  • 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
  • oleamide hydrolase activity Source: UniProtKB-EC
  • 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.
ReactomeiR-RNO-2142753. Arachidonic acid metabolism.

Chemistry databases

SwissLipidsiSLP:000001428.

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
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi61808. Faah.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei9 – 29HelicalSequence analysisAdd BLAST21
Topological domaini30 – 403CytoplasmicCuratedAdd BLAST374
Intramembranei404 – 433CuratedAdd BLAST30
Topological domaini434 – 579CytoplasmicCuratedAdd BLAST146

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)DescriptionActionsGraphical viewLength
Mutagenesisi142K → A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217. 1 Publication1
Mutagenesisi217S → A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3229.
GuidetoPHARMACOLOGYi1400.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001052671 – 579Fatty-acid amide hydrolase 1Add BLAST579

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei241PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP97612.
PRIDEiP97612.

PTM databases

iPTMnetiP97612.
PhosphoSitePlusiP97612.

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

BgeeiENSRNOG00000011019.
GenevisibleiP97612. RN.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

DIPiDIP-46284N.
MINTiMINT-4567335.
STRINGi10116.ENSRNOP00000015961.

Chemistry databases

BindingDBiP97612.

Structurei

Secondary structure

1579
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 65Combined sources31
Helixi71 – 76Combined sources6
Helixi79 – 87Combined sources9
Beta strandi89 – 91Combined sources3
Helixi93 – 111Combined sources19
Beta strandi114 – 117Combined sources4
Helixi121 – 127Combined sources7
Turni133 – 136Combined sources4
Beta strandi138 – 142Combined sources5
Helixi157 – 159Combined sources3
Beta strandi164 – 166Combined sources3
Helixi169 – 176Combined sources8
Beta strandi180 – 185Combined sources6
Helixi189 – 191Combined sources3
Beta strandi193 – 195Combined sources3
Turni199 – 201Combined sources3
Beta strandi216 – 218Combined sources3
Helixi219 – 226Combined sources8
Beta strandi231 – 240Combined sources10
Helixi243 – 249Combined sources7
Beta strandi252 – 255Combined sources4
Helixi258 – 260Combined sources3
Beta strandi279 – 286Combined sources8
Helixi287 – 297Combined sources11
Helixi300 – 305Combined sources6
Helixi316 – 319Combined sources4
Beta strandi326 – 329Combined sources4
Beta strandi334 – 336Combined sources3
Helixi340 – 355Combined sources16
Beta strandi359 – 362Combined sources4
Helixi368 – 373Combined sources6
Helixi375 – 380Combined sources6
Turni382 – 385Combined sources4
Helixi386 – 389Combined sources4
Helixi390 – 392Combined sources3
Helixi399 – 401Combined sources3
Helixi404 – 408Combined sources5
Helixi412 – 422Combined sources11
Turni423 – 425Combined sources3
Helixi427 – 435Combined sources9
Beta strandi436 – 438Combined sources3
Helixi441 – 464Combined sources24
Beta strandi468 – 473Combined sources6
Helixi484 – 486Combined sources3
Helixi488 – 491Combined sources4
Helixi492 – 499Combined sources8
Beta strandi504 – 511Combined sources8
Helixi514 – 520Combined sources7
Helixi530 – 538Combined sources9
Beta strandi546 – 552Combined sources7
Helixi558 – 572Combined sources15
Helixi574 – 576Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97612.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 241Substrate binding4

Sequence similaritiesi

Belongs to the amidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1212. Eukaryota.
COG0154. LUCA.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiP97612.
KOiK15528.
OMAiNKETNCV.
OrthoDBiEOG091G05JU.

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:SF91. PTHR11895:SF91. 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_003750001.4.
XP_008774266.1. XM_008776044.2.
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_003750001.4.
XP_008774266.1. XM_008776044.2.
UniGeneiRn.89119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46284N.
MINTiMINT-4567335.
STRINGi10116.ENSRNOP00000015961.

Chemistry databases

BindingDBiP97612.
ChEMBLiCHEMBL3229.
GuidetoPHARMACOLOGYi1400.
SwissLipidsiSLP:000001428.

PTM databases

iPTMnetiP97612.
PhosphoSitePlusiP97612.

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

eggNOGiKOG1212. Eukaryota.
COG0154. LUCA.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiP97612.
KOiK15528.
OMAiNKETNCV.
OrthoDBiEOG091G05JU.

Enzyme and pathway databases

BRENDAi3.5.1.4. 5301.
3.5.1.99. 5301.
ReactomeiR-RNO-2142753. Arachidonic acid metabolism.

Miscellaneous databases

EvolutionaryTraceiP97612.
PROiP97612.

Gene expression databases

BgeeiENSRNOG00000011019.
GenevisibleiP97612. RN.

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:SF91. PTHR11895:SF91. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMiSSF75304. SSF75304. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 132 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

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 one 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.