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Q7XJJ7 (FAAH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid amide hydrolase

EC=3.5.1.99
Alternative name(s):
N-acylethanolamine amidohydrolase
Gene names
Name:FAAH
Ordered Locus Names:At5g64440
ORF Names:T12B11.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.9 Ref.10

Catalytic activity

Anandamide + H2O = arachidonic acid + ethanolamine. Ref.2 Ref.7

Oleamide + H2O = oleic acid + NH3. Ref.2 Ref.7

Enzyme regulation

Inhibited by methylarachidonyl fluorophosphonate (MAFP). Ref.2

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Potential. Cell membrane; Single-pass membrane protein Potential Ref.9.

Tissue specificity

Expressed in seedlings, flowers, roots, siliques, seeds and leaves. Lower levels in stems. Ref.7 Ref.8

Developmental stage

Up-regulated during seed germination and early postgerminative seedling growth. Ref.8

Disruption phenotype

No visible phenotype and enhanced sensitivity to growth inhibition induced by exogenous N-actylethanolamine. Ref.8

Sequence similarities

Belongs to the amidase family.

Biophysicochemical properties

Kinetic parameters:

KM=13.6 µM for N-actylethanolamine 20:4 Ref.2

KM=26.2 µM for N-actylethanolamine 18:2

KM=50.8 µM for N-actylethanolamine 16:0

KM=37.0 µM for N-actylethanolamine 14:0

KM=17.6 µM for N-actylethanolamine 12:0

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

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

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

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

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Fatty acid amide hydrolase
PRO_0000414026

Regions

Transmembrane32 – 5221Helical; Potential
Region302 – 3054Substrate binding By similarity

Sites

Active site2051Charge relay system Probable
Active site2811Charge relay system Probable
Active site3051Acyl-ester intermediate Probable

Experimental info

Mutagenesis2051K → A: Loss of activity. Ref.10
Mutagenesis281 – 2822SS → AA: Loss of activity.
Mutagenesis3051S → A: Loss of activity. Ref.10
Mutagenesis3071R → A: Loss of activity. Ref.10
Mutagenesis3601S → A: No effect. Ref.10
Sequence conflict1271R → W in BAB11605. Ref.3
Sequence conflict1271R → W in AAF73891. Ref.1
Sequence conflict5711M → R in AAF73891. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7XJJ7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B659CFA60EFC1633

FASTA60766,079
        10         20         30         40         50         60 
MGKYQVMKRA SEVDLSTVKY KAETMKAPHL TGLSFKLFVN LLEAPLIGSL IVDYLKKDNG 

        70         80         90        100        110        120 
MTKIFRNTVI PEEPMFRPEF PSQEPEHDVV IVGEDESPID RLETALKCLP QYDPSRSLHA 

       130        140        150        160        170        180 
DPVSSFRYWK IRDYAYAYRS KLTTPLQVAK RIISIIEEFG YDKPPTPFLI RFDANEVIKQ 

       190        200        210        220        230        240 
AEASTRRFEQ GNPISVLDGI FVTIKDDIDC LPHPTNGGTT WLHEDRSVEK DSAVVSKLRS 

       250        260        270        280        290        300 
CGAILLGKAN MHELGMGTTG NNSNYGTTRN PHDPKRYTGG SSSGSAAIVA AGLCSAALGT 

       310        320        330        340        350        360 
DGGGSVRIPS ALCGITGLKT TYGRTDMTGS LCEGGTVEII GPLASSLEDA FLVYAAILGS 

       370        380        390        400        410        420 
SSADRYNLKP SPPCFPKLLS HNGSNAIGSL RLGKYTKWFN DVSSSDISDK CEDILKLLSN 

       430        440        450        460        470        480 
NHGCKVVEIV VPELEEMRAA HVISIGSPTL SSLTPYCEAG KNSKLSYDTR TSFAIFRSFS 

       490        500        510        520        530        540 
ASDYIAAQCL RRRLMEYHLN IFKDVDVIVT PTTGMTAPVI PPDALKNGET NIQVTTDLMR 

       550        560        570        580        590        600 
FVLAANLLGF PAISVPVGYD KEGLPIGLQI MGRPWAEATV LGLAAAVEEL APVTKKPAIF 


YDILNTN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Plant fatty acid (ethanol) amide hydrolases."
Shrestha R., Kim S.C., Dyer J.M., Dixon R.A., Chapman K.D.
Biochim. Biophys. Acta 1761:324-334(2006) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_201249.2. NM_125840.3.
UniGeneAt.19619.

3D structure databases

ProteinModelPortalQ7XJJ7.
SMRQ7XJJ7. Positions 143-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G64440.1-P.

Proteomic databases

PaxDbQ7XJJ7.
PRIDEQ7XJJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G64440.1; AT5G64440.1; AT5G64440.
GeneID836565.
KEGGath:AT5G64440.

Organism-specific databases

TAIRAT5G64440.

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000116697.
InParanoidQ7XJJ7.
OMAFEPLSRD.
PhylomeDBQ7XJJ7.
ProtClustDBCLSN2694572.

Enzyme and pathway databases

BioCycARA:AT5G64440-MONOMER.

Gene expression databases

GenevestigatorQ7XJJ7.

Family and domain databases

Gene3D3.90.1300.10. 1 hit.
InterProIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
[Graphical view]
PANTHERPTHR11895. PTHR11895. 1 hit.
PfamPF01425. Amidase. 1 hit.
[Graphical view]
SUPFAMSSF75304. SSF75304. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFAAH_ARATH
AccessionPrimary (citable) accession number: Q7XJJ7
Secondary accession number(s): Q93ZI9, Q9FGF2, Q9LLC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names