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Q7XJJ7

- FAAH_ARATH

UniProt

Q7XJJ7 - FAAH_ARATH

Protein

Fatty acid amide hydrolase

Gene

FAAH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Degrades bioactive fatty acid amides to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Converts N-actylethanolamine (NAE) to ethanolamine. Can also use oleamide or 2-arachidonylglycerol as substrates, but not indole-3-acetamide, 1-naphtalene-acetamide, nicotinic acid amide or L-asparagine. Might be involved in abscisic acid signaling and plant defense through distinctly different mechanisms not involving the catalytic activity.4 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by methylarachidonyl fluorophosphonate (MAFP).1 Publication

    Kineticsi

    1. KM=13.6 µM for N-actylethanolamine 20:41 Publication
    2. KM=26.2 µM for N-actylethanolamine 18:21 Publication
    3. KM=50.8 µM for N-actylethanolamine 16:01 Publication
    4. KM=37.0 µM for N-actylethanolamine 14:01 Publication
    5. KM=17.6 µM for N-actylethanolamine 12:01 Publication

    Vmax=17.9 µmol/h/mg enzyme with N-actylethanolamine 20:4 as substrate1 Publication

    Vmax=14.1 µmol/h/mg enzyme with N-actylethanolamine 18:2 as substrate1 Publication

    Vmax=12.1 µmol/h/mg enzyme with N-actylethanolamine 16:0 as substrate1 Publication

    Vmax=9.1 µmol/h/mg enzyme with N-actylethanolamine 14:0 as substrate1 Publication

    Vmax=13.9 µmol/h/mg enzyme with N-actylethanolamine 12:0 as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei205 – 2051Charge relay systemCurated
    Active sitei281 – 2811Charge relay systemCurated
    Active sitei305 – 3051Acyl-ester intermediateCurated

    GO - Molecular functioni

    1. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
    2. N-(long-chain-acyl)ethanolamine deacylase activity Source: TAIR

    GO - Biological processi

    1. defense response to bacterium Source: TAIR
    2. N-acylethanolamine metabolic process Source: TAIR

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT5G64440-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid amide hydrolase (EC:3.5.1.99)
    Alternative name(s):
    N-acylethanolamine amidohydrolase
    Gene namesi
    Name:FAAH
    Ordered Locus Names:At5g64440
    ORF Names:T12B11.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G64440.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: TAIR
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: TAIR
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: TAIR
    6. vacuolar membrane Source: TAIR
    7. vacuole Source: TAIR

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype and enhanced sensitivity to growth inhibition induced by exogenous N-actylethanolamine.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi205 – 2051K → A: Loss of activity. 1 Publication
    Mutagenesisi281 – 2822SS → AA: Loss of activity.
    Mutagenesisi305 – 3051S → A: Loss of activity. 1 Publication
    Mutagenesisi307 – 3071R → A: Loss of activity. 1 Publication
    Mutagenesisi360 – 3601S → A: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 607607Fatty acid amide hydrolasePRO_0000414026Add
    BLAST

    Proteomic databases

    PaxDbiQ7XJJ7.
    PRIDEiQ7XJJ7.

    Expressioni

    Tissue specificityi

    Expressed in seedlings, flowers, roots, siliques, seeds and leaves. Lower levels in stems.2 Publications

    Developmental stagei

    Up-regulated during seed germination and early postgerminative seedling growth.1 Publication

    Gene expression databases

    GenevestigatoriQ7XJJ7.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G64440.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7XJJ7.
    SMRiQ7XJJ7. Positions 143-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni302 – 3054Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the amidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0154.
    HOGENOMiHOG000116697.
    InParanoidiQ7XJJ7.
    OMAiPNYGTTR.
    PhylomeDBiQ7XJJ7.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q7XJJ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKYQVMKRA SEVDLSTVKY KAETMKAPHL TGLSFKLFVN LLEAPLIGSL    50
    IVDYLKKDNG MTKIFRNTVI PEEPMFRPEF PSQEPEHDVV IVGEDESPID 100
    RLETALKCLP QYDPSRSLHA DPVSSFRYWK IRDYAYAYRS KLTTPLQVAK 150
    RIISIIEEFG YDKPPTPFLI RFDANEVIKQ AEASTRRFEQ GNPISVLDGI 200
    FVTIKDDIDC LPHPTNGGTT WLHEDRSVEK DSAVVSKLRS CGAILLGKAN 250
    MHELGMGTTG NNSNYGTTRN PHDPKRYTGG SSSGSAAIVA AGLCSAALGT 300
    DGGGSVRIPS ALCGITGLKT TYGRTDMTGS LCEGGTVEII GPLASSLEDA 350
    FLVYAAILGS SSADRYNLKP SPPCFPKLLS HNGSNAIGSL RLGKYTKWFN 400
    DVSSSDISDK CEDILKLLSN NHGCKVVEIV VPELEEMRAA HVISIGSPTL 450
    SSLTPYCEAG KNSKLSYDTR TSFAIFRSFS ASDYIAAQCL RRRLMEYHLN 500
    IFKDVDVIVT PTTGMTAPVI PPDALKNGET NIQVTTDLMR FVLAANLLGF 550
    PAISVPVGYD KEGLPIGLQI MGRPWAEATV LGLAAAVEEL APVTKKPAIF 600
    YDILNTN 607
    Length:607
    Mass (Da):66,079
    Last modified:October 1, 2003 - v1
    Checksum:iB659CFA60EFC1633
    GO

    Sequence cautioni

    The sequence AAL09742.1 differs from that shown. Reason: Frameshift at position 148.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271R → W in BAB11605. 1 PublicationCurated
    Sequence conflicti127 – 1271R → W in AAF73891. 1 PublicationCurated
    Sequence conflicti571 – 5711M → R in AAF73891. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF223949 mRNA. Translation: AAF73891.1.
    AY308736 mRNA. Translation: AAP83139.1.
    AB025640 Genomic DNA. Translation: BAB11605.1.
    CP002688 Genomic DNA. Translation: AED97893.1.
    AY057501 mRNA. Translation: AAL09742.1. Frameshift.
    AY143870 mRNA. Translation: AAN28809.1.
    RefSeqiNP_201249.2. NM_125840.3.
    UniGeneiAt.19619.

    Genome annotation databases

    EnsemblPlantsiAT5G64440.1; AT5G64440.1; AT5G64440.
    GeneIDi836565.
    KEGGiath:AT5G64440.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF223949 mRNA. Translation: AAF73891.1 .
    AY308736 mRNA. Translation: AAP83139.1 .
    AB025640 Genomic DNA. Translation: BAB11605.1 .
    CP002688 Genomic DNA. Translation: AED97893.1 .
    AY057501 mRNA. Translation: AAL09742.1 . Frameshift.
    AY143870 mRNA. Translation: AAN28809.1 .
    RefSeqi NP_201249.2. NM_125840.3.
    UniGenei At.19619.

    3D structure databases

    ProteinModelPortali Q7XJJ7.
    SMRi Q7XJJ7. Positions 143-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G64440.1-P.

    Proteomic databases

    PaxDbi Q7XJJ7.
    PRIDEi Q7XJJ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G64440.1 ; AT5G64440.1 ; AT5G64440 .
    GeneIDi 836565.
    KEGGi ath:AT5G64440.

    Organism-specific databases

    TAIRi AT5G64440.

    Phylogenomic databases

    eggNOGi COG0154.
    HOGENOMi HOG000116697.
    InParanoidi Q7XJJ7.
    OMAi PNYGTTR.
    PhylomeDBi Q7XJJ7.

    Enzyme and pathway databases

    BioCyci ARA:AT5G64440-MONOMER.

    Gene expression databases

    Genevestigatori Q7XJJ7.

    Family and domain databases

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

    Publicationsi

    1. "Cloning and characterization of an amidase gene frome Arabidopsis thaliana."
      Chang W.-Z., Soll D.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana."
      Shrestha R., Dixon R.A., Chapman K.D.
      J. Biol. Chem. 278:34990-34997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
      Tissue: Leaf.
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
      Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. Cited for: 3D-STRUCTURE MODELING.
    7. "Subcellular localization and tissue specific expression of amidase 1 from Arabidopsis thaliana."
      Pollmann S., Neu D., Lehmann T., Berkowitz O., Schaefer T., Weiler E.W.
      Planta 224:1241-1253(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    8. "Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies plant growth and sensitivity to N-acylethanolamines."
      Wang Y.S., Shrestha R., Kilaru A., Wiant W., Venables B.J., Chapman K.D., Blancaflor E.B.
      Proc. Natl. Acad. Sci. U.S.A. 103:12197-12202(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    9. "Overexpression of a fatty acid amide hydrolase compromises innate immunity in Arabidopsis."
      Kang L., Wang Y.S., Uppalapati S.R., Wang K., Tang Y., Vadapalli V., Venables B.J., Chapman K.D., Blancaflor E.B., Mysore K.S.
      Plant J. 56:336-349(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens."
      Kim S.C., Kang L., Nagaraj S., Blancaflor E.B., Mysore K.S., Chapman K.D.
      J. Biol. Chem. 284:34065-34074(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-205; 281-SER-SER-282; SER-305; ARG-307 AND SER-360.

    Entry informationi

    Entry nameiFAAH_ARATH
    AccessioniPrimary (citable) accession number: Q7XJJ7
    Secondary accession number(s): Q93ZI9, Q9FGF2, Q9LLC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2011
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3