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O08914 (FAAH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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 1

EC=3.5.1.99
Alternative name(s):
Anandamide amidohydrolase 1
Oleamide hydrolase 1
Gene names
Name:Faah
Synonyms:Faah1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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_0000105265

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

Sequence conflict721E → Q in AAH06863. Ref.4
Sequence conflict2301S → P in AK004985. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O08914 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 11B2DF6CBC110015

FASTA57963,221
        10         20         30         40         50         60 
MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA GLETMDKAVQ 

        70         80         90        100        110        120 
RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY LGKAWEVNKG TNCVTSYLTD 

       130        140        150        160        170        180 
CETQLSQAPR QGLLYGVPVS LKECFSYKGH ASTLGLSLNE GVTSESDCVV VQVLKLQGAV 

       190        200        210        220        230        240 
PFVHTNVPQS MLSYDCSNPL FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG 

       250        260        270        280        290        300 
SIRFPSAFCG ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE 

       310        320        330        340        350        360 
DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK QSLEAAGHTL 

       370        380        390        400        410        420 
VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC LGDLVLVLKL PRWFKKLLSF 

       430        440        450        460        470        480 
LLKPLFPRLA AFLNSMCPRS AEKLWELQHE IEMYRQSVIA QWKAMNLDVV LTPMLGPALD 

       490        500        510        520        530        540 
LNTPGRATGA ISYTVLYNCL DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK 

       550        560        570 
KGIGLPVAVQ CVALPWQEEL CLRFMREVER LMTPEKRPS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of human and mouse fatty acid amide hydrolases."
Giang D.K., Cravatt B.F.
Proc. Natl. Acad. Sci. U.S.A. 94:2238-2242(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Conserved chromosomal location and genomic structure of human and mouse fatty-acid amide hydrolase genes and evaluation of clasper as a candidate neurological mutation."
Wan M., Cravatt B.F., Ring H.Z., Zhang X., Francke U.
Genomics 54:408-414(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82536 mRNA. Translation: AAB58506.1.
AF098009 expand/collapse EMBL AC list , AF097997, AF097998, AF097999, AF098000, AF098001, AF098002, AF098003, AF098004, AF098005, AF098006, AF098007, AF098008 Genomic DNA. Translation: AAD11788.1.
AK004985 mRNA. No translation available.
BC006863 mRNA. Translation: AAH06863.1.
BC052321 mRNA. Translation: AAH52321.1.
CCDSCCDS18501.1.
RefSeqNP_034303.3. NM_010173.4.
UniGeneMm.256025.

3D structure databases

ProteinModelPortalO08914.
SMRO08914. Positions 35-575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1838003.

Chemistry

BindingDBO08914.
ChEMBLCHEMBL3455.

PTM databases

PhosphoSiteO08914.

Proteomic databases

MaxQBO08914.
PaxDbO08914.
PRIDEO08914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171.
GeneID14073.
KEGGmmu:14073.
UCSCuc008ufs.2. mouse.

Organism-specific databases

CTD2166.
MGIMGI:109609. Faah.

Phylogenomic databases

eggNOGCOG0154.
GeneTreeENSGT00550000074673.
HOGENOMHOG000016500.
HOVERGENHBG005632.
KOK15528.
OMACCFVAAA.
OrthoDBEOG72JWG0.
PhylomeDBO08914.
TreeFamTF314455.

Gene expression databases

ArrayExpressO08914.
BgeeO08914.
CleanExMM_FAAH.
GenevestigatorO08914.

Family and domain databases

Gene3D3.90.1300.10. 1 hit.
InterProIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun_type.
[Graphical view]
PANTHERPTHR11895. PTHR11895. 1 hit.
PfamPF01425. Amidase. 1 hit.
[Graphical view]
PIRSFPIRSF001221. Amidase_fungi. 1 hit.
SUPFAMSSF75304. SSF75304. 1 hit.
PROSITEPS00571. AMIDASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285074.
PROO08914.
SOURCESearch...

Entry information

Entry nameFAAH1_MOUSE
AccessionPrimary (citable) accession number: O08914
Secondary accession number(s): Q922S0, Q9DBF5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 112 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot