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Q9TUI8 (FAAH1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fatty-acid amide hydrolase 1
EC=3.5.1.99
Alternative name(s):
Anandamide amidohydrolase 1
Oleamide hydrolase 1
Gene names
Name:FAAH
Synonyms:FAAH1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates By similarity.

Catalytic activity

Anandamide + H2O = arachidonic acid + ethanolamine.

Oleamide + H2O = oleic acid + NH3.

Subunit structure

Homodimer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Note: Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus.

Sequence similarities

Belongs to the amidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Fatty-acid amide hydrolase 1
PRO_0000105266

Regions

Transmembrane9 – 2921Helical; Potential
Topological domain30 – 403374Cytoplasmic By similarity
Intramembrane404 – 43330 By similarity
Topological domain434 – 579146Cytoplasmic By similarity
Region238 – 2414Substrate binding By similarity

Sites

Active site1421Charge relay system By similarity
Active site2171Charge relay system By similarity
Active site2411Acyl-ester intermediate By similarity
Binding site1911Substrate; via carbonyl oxygen By similarity
Binding site2171Substrate By similarity

Experimental info

Mutagenesis2171S → A: Loss of activity. Ref.1
Mutagenesis2181S → A: Lowers activity by at least 98%. Ref.1
Mutagenesis2371D → E or N: Loss of activity. Ref.1
Mutagenesis2411S → A: Loss of activity. Ref.1
Mutagenesis2491C → A: Loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9TUI8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0600F2FDC9879D7C

FASTA57962,857
        10         20         30         40         50         60 
MVQEELWAAF SGPSGVALAC CLVAAALALR WSSRRMARGA AARARQRQQA ALETMDKAAQ 

        70         80         90        100        110        120 
RFRLQNPDLD SEMLLALPLP QLVQKVRSGE LSPEAVLFSY LQKAWEVNRG TNCVTTYLAD 

       130        140        150        160        170        180 
CEAQLCQAPG QGLLYGVPVS LKECFSCKGH DSTLGLSRNQ GTPAECDCVV VQVLKLQGAV 

       190        200        210        220        230        240 
PFVHTNVPQS MFSYDCSNPL FGQTTNPWMS SKSPGGSSGG EGALIAAGGS PLGLGTDIGG 

       250        260        270        280        290        300 
SIRFPSAFCG ICGIKPTGNR ISKSGLKGSV YGQVAVQLSV GPMARDVESL ALCLRALLCE 

       310        320        330        340        350        360 
DMFRLDPTVP PLPFNEEVYA SSRPLRVGYY ETDNYTMPTP AMRRALLETK RSLEAAGHTL 

       370        380        390        400        410        420 
IPFLPANIPH ALEALSTGGL FSDGGKRLLQ NFEGDYVDSC LGDLISILRL PKWLKGLLAF 

       430        440        450        460        470        480 
MLRPLLPRLA GFLSSLRPRS AGKLWELQHE IEMYRHSVIA QWRALDLDVV LTPMLSPALD 

       490        500        510        520        530        540 
LNAPGKATGA VSYTLLYNCL DFPAGVVPVT TVTAEDEAQM EHYKGYFGDI WDKVVQKAMK 

       550        560        570 
RSVGLPVAVQ CVALPWQEEL CLRFMREVER LMAPGRQPS

« Hide

References

[1]"Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis."
Goparaju S.K., Kurahashi Y., Suzuki H., Ueda N., Yamamoto S.
Biochim. Biophys. Acta 1441:77-84(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS OF SER-217; SER-218; ASP-237; SER-241 AND CYS-249.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB027132 mRNA. Translation: BAA86917.1.
RefSeqNP_999079.1. NM_213914.1.
UniGeneSsc.2698.

3D structure databases

ProteinModelPortalQ9TUI8.
SMRQ9TUI8. Positions 37-572.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000004216.

Proteomic databases

PaxDbQ9TUI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396949.
KEGGssc:396949.

Organism-specific databases

CTD2166.

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000016500.
HOVERGENHBG005632.
KOK15528.
OrthoDBEOG4PRSQP.

Family and domain databases

Gene3D3.90.1300.10. 1 hit.
InterProIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun.
[Graphical view]
PANTHERPTHR11895. PTHR11895. 1 hit.
PTHR11895:SF4. PTHR11895:SF4. 1 hit.
PfamPF01425. Amidase. 1 hit.
[Graphical view]
PIRSFPIRSF001221. Amidase_fungi. 1 hit.
SUPFAMSSF75304. Amidase_sig_enz. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFAAH1_PIG
AccessionPrimary (citable) accession number: Q9TUI8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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