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P97612

- FAAH1_RAT

UniProt

P97612 - FAAH1_RAT

Protein

Fatty-acid amide hydrolase 1

Gene

Faah

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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

    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

    GO - Biological processi

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

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

    GO - Cellular componenti

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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97612.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 403374CytoplasmicCuratedAdd
    BLAST
    Topological domaini434 – 579146CytoplasmicCuratedAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei404 – 43330CuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921HelicalSequence AnalysisAdd
    BLAST

    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 112 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