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P97612

- FAAH1_RAT

UniProt

P97612 - FAAH1_RAT

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Protein
Fatty-acid amide hydrolase 1
Gene
Faah, Faah1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

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

  1. amidase activity Source: RGD
  2. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
  3. fatty acid amide hydrolase activity Source: UniProtKB
  4. hydrolase activity, acting on ester bonds Source: RGD
  5. lipid binding Source: RGD
  6. phospholipid binding Source: RGD
  7. protein homodimerization activity Source: RGD
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

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: Chromosome 5

Organism-specific databases

RGDi61808. Faah.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein
Note: Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921Helical; Reviewed prediction
Add
BLAST
Topological domaini30 – 403374Cytoplasmic Inferred
Add
BLAST
Intramembranei404 – 43330 Inferred
Add
BLAST
Topological domaini434 – 579146Cytoplasmic Inferred
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: RGD
  4. 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 1
PRO_0000105267Add
BLAST

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP97612.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the amidase family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
KOiK15528.
OMAiCCFVAAA.
OrthoDBiEOG72JWG0.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun_type.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001221. Amidase_fungi. 1 hit.
SUPFAMiSSF75304. SSF75304. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97612-1 [UniParc]FASTAAdd to Basket

« Hide

MVLSEVWTTL SGVSGVCLAC SLLSAAVVLR WTGRQKARGA ATRARQKQRA    50
SLETMDKAVQ RFRLQNPDLD SEALLTLPLL QLVQKLQSGE LSPEAVFFTY 100
LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH 150
DSTLGLSLNE GMPSESDCVV VQVLKLQGAV PFVHTNVPQS MLSFDCSNPL 200
FGQTMNPWKS SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG 250
ICGLKPTGNR LSKSGLKGCV YGQTAVQLSL GPMARDVESL ALCLKALLCE 300
HLFTLDPTVP PLPFREEVYR SSRPLRVGYY ETDNYTMPSP AMRRALIETK 350
QRLEAAGHTL IPFLPNNIPY ALEVLSAGGL FSDGGRSFLQ NFKGDFVDPC 400
LGDLILILRL PSWFKRLLSL LLKPLFPRLA AFLNSMRPRS AEKLWKLQHE 450
IEMYRQSVIA QWKAMNLDVL LTPMLGPALD LNTPGRATGA ISYTVLYNCL 500
DFPAGVVPVT TVTAEDDAQM ELYKGYFGDI WDIILKKAMK NSVGLPVAVQ 550
CVALPWQEEL CLRFMREVEQ LMTPQKQPS 579
Length:579
Mass (Da):63,357
Last modified:May 1, 1997 - v1
Checksum:i606491C0B033E1AA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U72497 mRNA. Translation: AAB26961.1.
BC091148 mRNA. Translation: AAH91148.1.
RefSeqiNP_077046.1. NM_024132.3.
XP_003750049.1. XM_003750001.2.
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:
EMBL
GenBank
DDBJ
Links Updated
U72497 mRNA. Translation: AAB26961.1 .
BC091148 mRNA. Translation: AAH91148.1 .
RefSeqi NP_077046.1. NM_024132.3.
XP_003750049.1. XM_003750001.2.
UniGenei Rn.89119.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MT5 X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 37-573 [» ]
2VYA X-ray 2.75 A/B 32-579 [» ]
2WAP X-ray 2.80 A/B 31-573 [» ]
2WJ1 X-ray 1.84 A/B 30-579 [» ]
2WJ2 X-ray 2.55 A/B 30-579 [» ]
3K7F X-ray 1.95 A/B 30-579 [» ]
3K83 X-ray 2.25 A/B 30-579 [» ]
3K84 X-ray 2.25 A/B 30-579 [» ]
3LJ6 X-ray 2.42 A/B 30-579 [» ]
3LJ7 X-ray 2.30 A/B 30-579 [» ]
3OJ8 X-ray 1.90 A/B 30-579 [» ]
3PPM X-ray 1.78 A/B 30-579 [» ]
3PR0 X-ray 2.20 A/B 30-579 [» ]
3QJ8 X-ray 2.90 A/B 32-579 [» ]
3QJ9 X-ray 2.30 A/B 32-579 [» ]
3QK5 X-ray 2.20 A/B 32-579 [» ]
3QKV X-ray 3.10 A/B 32-579 [» ]
4DO3 X-ray 2.25 A/B 32-575 [» ]
4HBP X-ray 2.91 A/B 30-579 [» ]
4J5P X-ray 2.30 A/B 30-579 [» ]
ProteinModelPortali P97612.
SMRi P97612. Positions 37-573.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-46284N.
MINTi MINT-4567335.
STRINGi 10116.ENSRNOP00000015667.

Chemistry

BindingDBi P97612.
ChEMBLi CHEMBL3229.

PTM databases

PhosphoSitei P97612.

Proteomic databases

PaxDbi P97612.
PRIDEi P97612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015667 ; ENSRNOP00000015667 ; ENSRNOG00000045949 .
ENSRNOT00000015961 ; ENSRNOP00000015961 ; ENSRNOG00000011019 .
GeneIDi 100911581.
29347.
KEGGi rno:100911581.
rno:29347.
UCSCi RGD:61808. rat.

Organism-specific databases

CTDi 2166.
RGDi 61808. Faah.

Phylogenomic databases

eggNOGi COG0154.
GeneTreei ENSGT00550000074673.
HOGENOMi HOG000016500.
HOVERGENi HBG005632.
KOi K15528.
OMAi CCFVAAA.
OrthoDBi EOG72JWG0.

Miscellaneous databases

EvolutionaryTracei P97612.
NextBioi 608844.
PROi P97612.

Gene expression databases

Genevestigatori P97612.

Family and domain databases

Gene3Di 3.90.1300.10. 1 hit.
InterProi IPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun_type.
[Graphical view ]
PANTHERi PTHR11895. PTHR11895. 1 hit.
Pfami PF01425. Amidase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001221. Amidase_fungi. 1 hit.
SUPFAMi SSF75304. SSF75304. 1 hit.
PROSITEi PS00571. AMIDASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 111 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

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