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Protein

Fatty-acid amide hydrolase 1

Gene

Faah

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Anandamide + H2O = arachidonic acid + ethanolamine.
Oleamide + H2O = oleic acid + NH3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei142 – 1421Charge relay systemBy similarity
Binding sitei191 – 1911Substrate; via carbonyl oxygenBy similarity
Active sitei217 – 2171Charge relay systemBy similarity
Binding sitei217 – 2171SubstrateBy similarity
Active sitei241 – 2411Acyl-ester intermediateBy similarity

GO - Molecular functioni

  1. acylglycerol lipase activity Source: MGI
  2. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
  3. fatty acid amide hydrolase activity Source: UniProtKB

GO - Biological processi

  1. fatty acid catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.4. 3474.
3.5.1.99. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty-acid amide hydrolase 1 (EC:3.5.1.99)
Alternative name(s):
Anandamide amidohydrolase 1
Oleamide hydrolase 1
Gene namesi
Name:Faah
Synonyms:Faah1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:109609. Faah.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 403374CytoplasmicBy similarityAdd
BLAST
Intramembranei404 – 43330By similarityAdd
BLAST
Topological domaini434 – 579146CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. organelle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Fatty-acid amide hydrolase 1PRO_0000105265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei241 – 2411PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO08914.
PaxDbiO08914.
PRIDEiO08914.

PTM databases

PhosphoSiteiO08914.

Expressioni

Gene expression databases

BgeeiO08914.
CleanExiMM_FAAH.
ExpressionAtlasiO08914. baseline and differential.
GenevestigatoriO08914.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-1838003.

Structurei

3D structure databases

ProteinModelPortaliO08914.
SMRiO08914. Positions 35-575.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2414Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the amidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiO08914.
KOiK15528.
OMAiLKECFTY.
OrthoDBiEOG72JWG0.
PhylomeDBiO08914.
TreeFamiTF314455.

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.

O08914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA
60 70 80 90 100
GLETMDKAVQ RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY
110 120 130 140 150
LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH
160 170 180 190 200
ASTLGLSLNE GVTSESDCVV VQVLKLQGAV PFVHTNVPQS MLSYDCSNPL
210 220 230 240 250
FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG
260 270 280 290 300
ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE
310 320 330 340 350
DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK
360 370 380 390 400
QSLEAAGHTL VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC
410 420 430 440 450
LGDLVLVLKL PRWFKKLLSF LLKPLFPRLA AFLNSMCPRS AEKLWELQHE
460 470 480 490 500
IEMYRQSVIA QWKAMNLDVV LTPMLGPALD LNTPGRATGA ISYTVLYNCL
510 520 530 540 550
DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK KGIGLPVAVQ
560 570
CVALPWQEEL CLRFMREVER LMTPEKRPS
Length:579
Mass (Da):63,221
Last modified:June 30, 1997 - v1
Checksum:i11B2DF6CBC110015
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721E → Q in AAH06863 (PubMed:15489334).Curated
Sequence conflicti230 – 2301S → P in AK004985 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82536 mRNA. Translation: AAB58506.1.
AF098009
, 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.
CCDSiCCDS18501.1.
RefSeqiNP_034303.3. NM_010173.4.
UniGeneiMm.256025.

Genome annotation databases

EnsembliENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171.
GeneIDi14073.
KEGGimmu:14073.
UCSCiuc008ufs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82536 mRNA. Translation: AAB58506.1.
AF098009
, 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.
CCDSiCCDS18501.1.
RefSeqiNP_034303.3. NM_010173.4.
UniGeneiMm.256025.

3D structure databases

ProteinModelPortaliO08914.
SMRiO08914. Positions 35-575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1838003.

Chemistry

BindingDBiO08914.
ChEMBLiCHEMBL3455.

PTM databases

PhosphoSiteiO08914.

Proteomic databases

MaxQBiO08914.
PaxDbiO08914.
PRIDEiO08914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171.
GeneIDi14073.
KEGGimmu:14073.
UCSCiuc008ufs.2. mouse.

Organism-specific databases

CTDi2166.
MGIiMGI:109609. Faah.

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
InParanoidiO08914.
KOiK15528.
OMAiLKECFTY.
OrthoDBiEOG72JWG0.
PhylomeDBiO08914.
TreeFamiTF314455.

Enzyme and pathway databases

BRENDAi3.5.1.4. 3474.
3.5.1.99. 3474.

Miscellaneous databases

NextBioi285074.
PROiO08914.
SOURCEiSearch...

Gene expression databases

BgeeiO08914.
CleanExiMM_FAAH.
ExpressionAtlasiO08914. baseline and differential.
GenevestigatoriO08914.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(1997) [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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary gland.

Entry informationi

Entry nameiFAAH1_MOUSE
AccessioniPrimary (citable) accession number: O08914
Secondary accession number(s): Q922S0, Q9DBF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: June 30, 1997
Last modified: March 31, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.