SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7XJJ7

- FAAH_ARATH

UniProt

Q7XJJ7 - FAAH_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fatty acid amide hydrolase

Gene
FAAH, At5g64440, T12B11.3
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.2 Publications
Oleamide + H2O = oleic acid + NH3.2 Publications

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 18:2
  3. KM=50.8 µM for N-actylethanolamine 16:0
  4. KM=37.0 µM for N-actylethanolamine 14:0
  5. 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

Sites

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

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

Endoplasmic reticulum membrane; Single-pass membrane protein Reviewed prediction. Cell membrane; Single-pass membrane protein Reviewed prediction 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei32 – 5221Helical; Reviewed predictionAdd
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.
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the amidase family.

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.

Sequence conflict

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

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

« 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: May 14, 2014
This is version 67 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