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Protein

Fatty acid amide hydrolase

Gene

FAAH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

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

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
Complete GO annotation...

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. 1 Publication
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...

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.
OMAiKSELKWG.
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

        10         20         30         40         50
MGKYQVMKRA SEVDLSTVKY KAETMKAPHL TGLSFKLFVN LLEAPLIGSL
60 70 80 90 100
IVDYLKKDNG MTKIFRNTVI PEEPMFRPEF PSQEPEHDVV IVGEDESPID
110 120 130 140 150
RLETALKCLP QYDPSRSLHA DPVSSFRYWK IRDYAYAYRS KLTTPLQVAK
160 170 180 190 200
RIISIIEEFG YDKPPTPFLI RFDANEVIKQ AEASTRRFEQ GNPISVLDGI
210 220 230 240 250
FVTIKDDIDC LPHPTNGGTT WLHEDRSVEK DSAVVSKLRS CGAILLGKAN
260 270 280 290 300
MHELGMGTTG NNSNYGTTRN PHDPKRYTGG SSSGSAAIVA AGLCSAALGT
310 320 330 340 350
DGGGSVRIPS ALCGITGLKT TYGRTDMTGS LCEGGTVEII GPLASSLEDA
360 370 380 390 400
FLVYAAILGS SSADRYNLKP SPPCFPKLLS HNGSNAIGSL RLGKYTKWFN
410 420 430 440 450
DVSSSDISDK CEDILKLLSN NHGCKVVEIV VPELEEMRAA HVISIGSPTL
460 470 480 490 500
SSLTPYCEAG KNSKLSYDTR TSFAIFRSFS ASDYIAAQCL RRRLMEYHLN
510 520 530 540 550
IFKDVDVIVT PTTGMTAPVI PPDALKNGET NIQVTTDLMR FVLAANLLGF
560 570 580 590 600
PAISVPVGYD KEGLPIGLQI MGRPWAEATV LGLAAAVEEL APVTKKPAIF

YDILNTN
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi3702.AT5G64440.1-P.

Proteomic databases

PaxDbiQ7XJJ7.
PRIDEiQ7XJJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT5G64440.

Phylogenomic databases

eggNOGiCOG0154.
HOGENOMiHOG000116697.
InParanoidiQ7XJJ7.
OMAiKSELKWG.
PhylomeDBiQ7XJJ7.

Enzyme and pathway databases

BioCyciARA:AT5G64440-MONOMER.

Gene expression databases

GenevestigatoriQ7XJJ7.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 70 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

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 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.