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O08914

- FAAH1_MOUSE

UniProt

O08914 - FAAH1_MOUSE

Protein

Fatty-acid amide hydrolase 1

Gene

Faah

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jul 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 systemBy similarity
    Binding sitei191 – 1911Substrate; via carbonyl oxygenBy similarity
    Active sitei217 – 2171Charge relay systemBy similarity
    Binding sitei217 – 2171SubstrateBy similarity
    Active sitei241 – 2411Acyl-ester intermediateBy similarity

    GO - Molecular functioni

    1. acylglycerol lipase activity Source: MGI
    2. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
    3. fatty acid amide hydrolase activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid catabolic process Source: UniProtKB

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:109609. 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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579Fatty-acid amide hydrolase 1PRO_0000105265Add
    BLAST

    Proteomic databases

    MaxQBiO08914.
    PaxDbiO08914.
    PRIDEiO08914.

    PTM databases

    PhosphoSiteiO08914.

    Expressioni

    Gene expression databases

    ArrayExpressiO08914.
    BgeeiO08914.
    CleanExiMM_FAAH.
    GenevestigatoriO08914.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    MINTiMINT-1838003.

    Structurei

    3D structure databases

    ProteinModelPortaliO08914.
    SMRiO08914. Positions 35-575.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Intramembrane

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

    Transmembrane

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

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the amidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0154.
    GeneTreeiENSGT00550000074673.
    HOGENOMiHOG000016500.
    HOVERGENiHBG005632.
    KOiK15528.
    OMAiCCFVAAA.
    OrthoDBiEOG72JWG0.
    PhylomeDBiO08914.
    TreeFamiTF314455.

    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.

    O08914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA    50
    GLETMDKAVQ RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY 100
    LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH 150
    ASTLGLSLNE GVTSESDCVV VQVLKLQGAV PFVHTNVPQS MLSYDCSNPL 200
    FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG 250
    ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE 300
    DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK 350
    QSLEAAGHTL VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC 400
    LGDLVLVLKL PRWFKKLLSF LLKPLFPRLA AFLNSMCPRS AEKLWELQHE 450
    IEMYRQSVIA QWKAMNLDVV LTPMLGPALD LNTPGRATGA ISYTVLYNCL 500
    DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK KGIGLPVAVQ 550
    CVALPWQEEL CLRFMREVER LMTPEKRPS 579
    Length:579
    Mass (Da):63,221
    Last modified:July 1, 1997 - v1
    Checksum:i11B2DF6CBC110015
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721E → Q in AAH06863. (PubMed:15489334)Curated
    Sequence conflicti230 – 2301S → P in AK004985. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82536 mRNA. Translation: AAB58506.1.
    AF098009
    , AF097997, AF097998, AF097999, AF098000, AF098001, AF098002, AF098003, AF098004, AF098005, AF098006, AF098007, AF098008 Genomic DNA. Translation: AAD11788.1.
    AK004985 mRNA. No translation available.
    BC006863 mRNA. Translation: AAH06863.1.
    BC052321 mRNA. Translation: AAH52321.1.
    CCDSiCCDS18501.1.
    RefSeqiNP_034303.3. NM_010173.4.
    UniGeneiMm.256025.

    Genome annotation databases

    EnsembliENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171.
    GeneIDi14073.
    KEGGimmu:14073.
    UCSCiuc008ufs.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82536 mRNA. Translation: AAB58506.1 .
    AF098009
    , AF097997 , AF097998 , AF097999 , AF098000 , AF098001 , AF098002 , AF098003 , AF098004 , AF098005 , AF098006 , AF098007 , AF098008 Genomic DNA. Translation: AAD11788.1 .
    AK004985 mRNA. No translation available.
    BC006863 mRNA. Translation: AAH06863.1 .
    BC052321 mRNA. Translation: AAH52321.1 .
    CCDSi CCDS18501.1.
    RefSeqi NP_034303.3. NM_010173.4.
    UniGenei Mm.256025.

    3D structure databases

    ProteinModelPortali O08914.
    SMRi O08914. Positions 35-575.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1838003.

    Chemistry

    BindingDBi O08914.
    ChEMBLi CHEMBL3455.

    PTM databases

    PhosphoSitei O08914.

    Proteomic databases

    MaxQBi O08914.
    PaxDbi O08914.
    PRIDEi O08914.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049095 ; ENSMUSP00000041543 ; ENSMUSG00000034171 .
    GeneIDi 14073.
    KEGGi mmu:14073.
    UCSCi uc008ufs.2. mouse.

    Organism-specific databases

    CTDi 2166.
    MGIi MGI:109609. Faah.

    Phylogenomic databases

    eggNOGi COG0154.
    GeneTreei ENSGT00550000074673.
    HOGENOMi HOG000016500.
    HOVERGENi HBG005632.
    KOi K15528.
    OMAi CCFVAAA.
    OrthoDBi EOG72JWG0.
    PhylomeDBi O08914.
    TreeFami TF314455.

    Miscellaneous databases

    NextBioi 285074.
    PROi O08914.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08914.
    Bgeei O08914.
    CleanExi MM_FAAH.
    Genevestigatori O08914.

    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 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: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Conserved chromosomal location and genomic structure of human and mouse fatty-acid amide hydrolase genes and evaluation of clasper as a candidate neurological mutation."
      Wan M., Cravatt B.F., Ring H.Z., Zhang X., Francke U.
      Genomics 54:408-414(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    4. "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].
      Strain: FVB/N-3.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiFAAH1_MOUSE
    AccessioniPrimary (citable) accession number: O08914
    Secondary accession number(s): Q922S0, Q9DBF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 113 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3