Fatty acid amide hydrolase - Arabidopsis thaliana (Mouse-ear cress)

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Q7XJJ7 (FAAH_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=13.6 µM for N-actylethanolamine 20:4 Ref.2 K_M=26.2 µM for N-actylethanolamine 18:2 K_M=50.8 µM for N-actylethanolamine 16:0 K_M=37.0 µM for N-actylethanolamine 14:0 K_M=17.6 µM for N-actylethanolamine 12:0 V_max=17.9 µmol/h/mg enzyme with N-actylethanolamine 20:4 as substrate V_max=14.1 µmol/h/mg enzyme with N-actylethanolamine 18:2 as substrate V_max=12.1 µmol/h/mg enzyme with N-actylethanolamine 16:0 as substrate V_max=9.1 µmol/h/mg enzyme with N-actylethanolamine 14:0 as substrate V_max=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.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-acylethanolamine metabolic process Inferred from mutant phenotype PubMed 21372125. Source: TAIR defense response to bacterium Inferred from mutant phenotype Ref.9. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR endoplasmic reticulum Inferred from direct assay PubMed 16618929. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.9. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	N-(long-chain-acyl)ethanolamine deacylase activity Inferred from mutant phenotype Ref.8. Source: TAIR carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 607

607

Fatty acid amide hydrolase

PRO_0000414026

Regions

Transmembrane

32 – 52

Helical; Potential

Region

302 – 305

Substrate binding By similarity

Sites

Active site

205

Charge relay system Probable

Active site

281

Charge relay system Probable

Active site

305

Acyl-ester intermediate Probable

Experimental info

Mutagenesis

205

K → A: Loss of activity. Ref.10

Mutagenesis

281 – 282

SS → AA: Loss of activity.

Mutagenesis

305

S → A: Loss of activity. Ref.10

Mutagenesis

307

R → A: Loss of activity. Ref.10

Mutagenesis

360

S → A: No effect. Ref.10

Sequence conflict

127

R → W in BAB11605. Ref.3

Sequence conflict

127

R → W in AAF73891. Ref.1

Sequence conflict

571

M → R in AAF73891. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q7XJJ7 [UniParc].

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

607

66,079

        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' referencesShow '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. 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.
+	Additional computationally mapped references.

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.
IPI	IPI00528940.
RefSeq	NP_201249.2. NM_125840.3.
UniGene	At.19619.
3D structure databases
HSSP	HSSP built from PDB template 1M22 based on UniProtKB Q8RJN5.
ProteinModelPortal	Q7XJJ7.
SMR	Q7XJJ7. Positions 143-589.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G64440.1-P.
Proteomic databases
PaxDb	Q7XJJ7.
PRIDE	Q7XJJ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G64440.1; AT5G64440.1; AT5G64440.
GeneID	836565.
KEGG	ath:AT5G64440.
Organism-specific databases
TAIR	At5g64440.
Phylogenomic databases
eggNOG	COG0154.
HOGENOM	HOG000116697.
InParanoid	Q7XJJ7.
OMA	FEPLSRD.
PhylomeDB	Q7XJJ7.
ProtClustDB	CLSN2694572.
Gene expression databases
ArrayExpress	Q7XJJ7.
Genevestigator	Q7XJJ7.
Family and domain databases
Gene3D	3.90.1300.10. 1 hit.
InterPro	IPR000120. Amidase. IPR020556. Amidase_CS. IPR023631. Amidase_dom. [Graphical view]
PANTHER	PTHR11895. PTHR11895. 1 hit.
Pfam	PF01425. Amidase. 1 hit. [Graphical view]
SUPFAM	SSF75304. Amidase_sig_enz. 1 hit.
PROSITE	PS00571. AMIDASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FAAH_ARATH

Accession

Primary (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:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents