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Q6GMR7 (FAAH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 2

EC=3.5.1.99
Alternative name(s):
Amidase domain-containing protein
Anandamide amidohydrolase 2
Oleamide hydrolase 2
Gene names
Name:FAAH2
Synonyms:AMDD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 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 monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates. Ref.4

Catalytic activity

Anandamide + H2O = arachidonic acid + ethanolamine.

Oleamide + H2O = oleic acid + NH3.

Enzyme regulation

Inhibited by O-aryl carbamates and alpha-keto heterocytes. Ref.4

Subunit structure

Homodimer By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential Ref.4.

Tissue specificity

Highly expressed in the brain, small intestine and testis. Also expressed in the heart, kidney, liver, lung and prostate. Ref.4

Sequence similarities

Belongs to the amidase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 532532Fatty-acid amide hydrolase 2
PRO_0000291993

Regions

Transmembrane11 – 3121Helical; Potential
Compositional bias48 – 514Poly-Leu

Sites

Active site1311Charge relay system By similarity
Active site2061Charge relay system By similarity
Active site2301Acyl-ester intermediate By similarity

Experimental info

Sequence conflict981K → R in BAB71007. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6GMR7 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 1D83E34BFF186E5E

FASTA53258,304
        10         20         30         40         50         60 
MAPSFTARIQ LFLLRALGFL IGLVGRAALV LGGPKFASKT PRPVTEPLLL LSGMQLAKLI 

        70         80         90        100        110        120 
RQRKVKCIDV VQAYINRIKD VNPMINGIVK YRFEEAMKEA HAVDQKLAEK QEDEATLENK 

       130        140        150        160        170        180 
WPFLGVPLTV KEAFQLQGMP NSSGLMNRRD AIAKTDATVV ALLKGAGAIP LGITNCSELC 

       190        200        210        220        230        240 
MWYESSNKIY GRSNNPYDLQ HIVGGSSGGE GCTLAAACSV IGVGSDIGGS IRMPAFFNGI 

       250        260        270        280        290        300 
FGHKPSPGVV PNKGQFPLAV GAQELFLCTG PMCRYAEDLA PMLKVMAGPG IKRLKLDTKV 

       310        320        330        340        350        360 
HLKDLKFYWM EHDGGSFLMS KVDQDLIMTQ KKVVVHLETI LGASVQHVKL KKMKYSFQLW 

       370        380        390        400        410        420 
IAMMSAKGHD GKEPVKFVDL LGDHGKHVSP LWELIKWCLG LSVYTIPSIG LALLEEKLRY 

       430        440        450        460        470        480 
SNEKYQKFKA VEESLRKELV DMLGDDGVFL YPSHPTVAPK HHVPLTRPFN FAYTGVFSAL 

       490        500        510        520        530 
GLPVTQCPLG LNAKGLPLGI QVVAGPFNDH LTLAVAQYLE KTFGGWVCPG KF 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Colon.
[4]"A second fatty acid amide hydrolase with variable distribution among placental mammals."
Wei B.Q., Mikkelsen T.S., McKinney M.K., Lander E.S., Cravatt B.F.
J. Biol. Chem. 281:36569-36578(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK055766 mRNA. Translation: BAB71007.1.
AL928898 expand/collapse EMBL AC list , AL590394, AL606754, Z83745 Genomic DNA. Translation: CAH71179.1.
AL590394 expand/collapse EMBL AC list , AL606754, AL928898, Z83745 Genomic DNA. Translation: CAI40731.1.
AL606754 expand/collapse EMBL AC list , AL590394, AL928898, Z83745 Genomic DNA. Translation: CAI40852.1.
Z83745 expand/collapse EMBL AC list , AL590394, AL606754, AL928898 Genomic DNA. Translation: CAI42802.1.
BC048279 mRNA. Translation: AAH48279.1.
BC073922 mRNA. Translation: AAH73922.1.
RefSeqNP_777572.2. NM_174912.3.
UniGeneHs.496205.
Hs.745495.

3D structure databases

ProteinModelPortalQ6GMR7.
SMRQ6GMR7. Positions 56-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127693. 1 interaction.
STRING9606.ENSP00000364035.

Chemistry

ChEMBLCHEMBL1628475.
GuidetoPHARMACOLOGY1401.

PTM databases

PhosphoSiteQ6GMR7.

Polymorphism databases

DMDM74757585.

Proteomic databases

PaxDbQ6GMR7.
PRIDEQ6GMR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374900; ENSP00000364035; ENSG00000165591.
GeneID158584.
KEGGhsa:158584.
UCSCuc004dvc.3. human.

Organism-specific databases

CTD158584.
GeneCardsGC0XP057330.
H-InvDBHIX0021688.
HGNCHGNC:26440. FAAH2.
HPAHPA027534.
MIM300654. gene.
neXtProtNX_Q6GMR7.
PharmGKBPA162385543.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0154.
HOGENOMHOG000116697.
HOVERGENHBG101001.
InParanoidQ6GMR7.
OMACPLGLNA.
OrthoDBEOG7PZRX7.
PhylomeDBQ6GMR7.
TreeFamTF313781.

Gene expression databases

ArrayExpressQ6GMR7.
BgeeQ6GMR7.
CleanExHS_FAAH2.
GenevestigatorQ6GMR7.

Family and domain databases

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

Other

ChiTaRSFAAH2. human.
GenomeRNAi158584.
NextBio87770.
PROQ6GMR7.
SOURCESearch...

Entry information

Entry nameFAAH2_HUMAN
AccessionPrimary (citable) accession number: Q6GMR7
Secondary accession number(s): Q86VT2, Q96N98
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM