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O08914

- FAAH1_MOUSE

UniProt

O08914 - FAAH1_MOUSE

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Protein
Fatty-acid amide hydrolase 1
Gene
Faah, Faah1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei142 – 1421Charge relay system By similarity
Binding sitei191 – 1911Substrate; via carbonyl oxygen By similarity
Active sitei217 – 2171Charge relay system By similarity
Binding sitei217 – 2171Substrate By similarity
Active sitei241 – 2411Acyl-ester intermediate By 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
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

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: 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 – 2921Helical; Reviewed prediction
Add
BLAST
Topological domaini30 – 403374Cytoplasmic By similarity
Add
BLAST
Intramembranei404 – 43330 By similarity
Add
BLAST
Topological domaini434 – 579146Cytoplasmic By similarity
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. endoplasmic reticulum 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 1
PRO_0000105265Add
BLAST

Proteomic databases

MaxQBiO08914.
PaxDbiO08914.
PRIDEiO08914.

PTM databases

PhosphoSiteiO08914.

Expressioni

Gene expression databases

ArrayExpressiO08914.
BgeeiO08914.
CleanExiMM_FAAH.
GenevestigatoriO08914.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

MINTiMINT-1838003.

Structurei

3D structure databases

ProteinModelPortaliO08914.
SMRiO08914. Positions 35-575.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the amidase family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000016500.
HOVERGENiHBG005632.
KOiK15528.
OMAiCCFVAAA.
OrthoDBiEOG72JWG0.
PhylomeDBiO08914.
TreeFamiTF314455.

Family and domain databases

Gene3Di3.90.1300.10. 1 hit.
InterProiIPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun_type.
[Graphical view]
PANTHERiPTHR11895. PTHR11895. 1 hit.
PfamiPF01425. Amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001221. Amidase_fungi. 1 hit.
SUPFAMiSSF75304. SSF75304. 1 hit.
PROSITEiPS00571. AMIDASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08914-1 [UniParc]FASTAAdd to Basket

« Hide

MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA    50
GLETMDKAVQ RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY 100
LGKAWEVNKG TNCVTSYLTD CETQLSQAPR QGLLYGVPVS LKECFSYKGH 150
ASTLGLSLNE GVTSESDCVV VQVLKLQGAV PFVHTNVPQS MLSYDCSNPL 200
FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG SIRFPSAFCG 250
ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE 300
DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK 350
QSLEAAGHTL VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC 400
LGDLVLVLKL PRWFKKLLSF LLKPLFPRLA AFLNSMCPRS AEKLWELQHE 450
IEMYRQSVIA QWKAMNLDVV LTPMLGPALD LNTPGRATGA ISYTVLYNCL 500
DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK KGIGLPVAVQ 550
CVALPWQEEL CLRFMREVER LMTPEKRPS 579
Length:579
Mass (Da):63,221
Last modified:July 1, 1997 - v1
Checksum:i11B2DF6CBC110015
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721E → Q in AAH06863. 1 Publication
Sequence conflicti230 – 2301S → P in AK004985. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18501.1.
RefSeqi NP_034303.3. NM_010173.4.
UniGenei Mm.256025.

3D structure databases

ProteinModelPortali O08914.
SMRi O08914. Positions 35-575.
ModBasei Search...

Protein-protein interaction databases

MINTi MINT-1838003.

Chemistry

BindingDBi O08914.
ChEMBLi CHEMBL3455.

PTM databases

PhosphoSitei O08914.

Proteomic databases

MaxQBi O08914.
PaxDbi O08914.
PRIDEi O08914.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049095 ; ENSMUSP00000041543 ; ENSMUSG00000034171 .
GeneIDi 14073.
KEGGi mmu:14073.
UCSCi uc008ufs.2. mouse.

Organism-specific databases

CTDi 2166.
MGIi MGI:109609. Faah.

Phylogenomic databases

eggNOGi COG0154.
GeneTreei ENSGT00550000074673.
HOGENOMi HOG000016500.
HOVERGENi HBG005632.
KOi K15528.
OMAi CCFVAAA.
OrthoDBi EOG72JWG0.
PhylomeDBi O08914.
TreeFami TF314455.

Miscellaneous databases

NextBioi 285074.
PROi O08914.
SOURCEi Search...

Gene expression databases

ArrayExpressi O08914.
Bgeei O08914.
CleanExi MM_FAAH.
Genevestigatori O08914.

Family and domain databases

Gene3Di 3.90.1300.10. 1 hit.
InterProi IPR000120. Amidase.
IPR020556. Amidase_CS.
IPR023631. Amidase_dom.
IPR015830. Amidase_fun_type.
[Graphical view ]
PANTHERi PTHR11895. PTHR11895. 1 hit.
Pfami PF01425. Amidase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001221. Amidase_fungi. 1 hit.
SUPFAMi SSF75304. SSF75304. 1 hit.
PROSITEi PS00571. AMIDASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.

Entry informationi

Entry nameiFAAH1_MOUSE
AccessioniPrimary (citable) accession number: O08914
Secondary accession number(s): Q922S0, Q9DBF5
Entry historyi
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 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