Reviewed, UniProtKB/Swiss-Prot O08914 (FAAH1_MOUSE)

Names and origin

Protein names

Recommended name:
    Fatty-acid amide hydrolase 1
    EC=3.5.1.n2
Alternative name(s):
    Oleamide hydrolase 1
    Anandamide amidohydrolase 1

Gene names

Name:	Faah
Synonyms:	Faah1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell organelle membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro fatty acid amide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 579	579	Fatty-acid amide hydrolase 1		PRO_0000105265
Regions
	Transmembrane	9 – 29	21	Potential
	Topological domain	30 – 403	374	Cytoplasmic By similarity
	Topological domain	434 – 579	146	Cytoplasmic By similarity
	Region	238 – 241	4	Substrate binding By similarity
	Region	404 – 433	30	In membrane By similarity
Sites
	Active site	142	1	Charge relay system By similarity
	Active site	217	1	Charge relay system By similarity
	Active site	241	1	Acyl-ester intermediate By similarity
	Binding site	191	1	Substrate; via carbonyl oxygen By similarity
	Binding site	217	1	Substrate By similarity
Amino acid modifications
	Modified residue	329	1	Phosphotyrosine By similarity
	Modified residue	335	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	72	1	E → Q in AAH06863. Ref.4
	Sequence conflict	230	1	S → P Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O08914-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 11B2DF6CBC110015	FASTA	579	63,221
	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

References

	« Hide 'large scale' referencesShow '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: 9122178] [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: 9878243] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00117176.
RefSeq	NP_034303.3.
UniGene	Mm.256025
3D structure databases
HSSP	HSSP built from PDB template 1MT5 based on UniProtKB P97612.
SMR	O08914. Positions 37-573.
ModBase	Search...
Protein-protein interaction databases
STRING	O08914.
PTM databases
PhosphoSite	O08914.
Proteomic databases
PRIDE	O08914.
Genome annotation databases
Ensembl	ENSMUST00000049095; ENSMUSP00000041543; ENSMUSG00000034171; Mus musculus. [Genome view] ENSMUST00000051237; ENSMUSP00000051700; ENSMUSG00000034171; Mus musculus. [Genome view]
GeneID	14073.
KEGG	mmu:14073.
UCSC	uc008ufs.1. mouse.
Organism-specific databases
CTD	14073.
MGI	MGI:109609. Faah.
Phylogenomic databases
HOVERGEN	O08914.
Gene expression databases
ArrayExpress	O08914.
Bgee	O08914.
CleanEx	MM_FAAH.
Genevestigator	O08914.
GermOnline	ENSMUSG00000034171. Mus musculus.
Family and domain databases
InterPro	IPR000120. Amidase. IPR020556. Amidase_CS. IPR015830. Amidase_fun. [Graphical view]
Gene3D	G3DSA:3.90.1300.10. Amidase_sig_enz. 1 hit.
PANTHER	PTHR11895. Amidase. 1 hit.
Pfam	PF01425. Amidase. 1 hit. [Graphical view]
PIRSF	PIRSF001221. Amidase_fungi. 1 hit.
PROSITE	PS00571. AMIDASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

FAAH1_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)