Q6GMR7 (FAAH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fatty-acid amide hydrolase 2
EC=3.5.1.99

Alternative name(s):
Oleamide hydrolase 2
Anandamide amidohydrolase 2
Amidase domain-containing protein

Gene names

Name:	FAAH2
Synonyms:	AMDD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
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 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

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor Inferred from electronic annotation. Source: InterPro hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 532	532	Fatty-acid amide hydrolase 2		PRO_0000291993
Regions
	Transmembrane	11 – 31	21	Helical; Potential
	Compositional bias	48 – 51	4	Poly-Leu
Sites
	Active site	131	1	Charge relay system By similarity
	Active site	206	1	Charge relay system By similarity
	Active site	230	1	Acyl-ester intermediate By similarity
Experimental info
	Sequence conflict	98	1	K → R in BAB71007. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6GMR7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 1D83E34BFF186E5E	FASTA	532	58,304
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [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. , 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: 15772651] [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: 15489334] [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: 17015445] [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 , AL590394, AL606754, Z83745 Genomic DNA. Translation: CAH71179.1. AL590394 , AL606754, AL928898, Z83745 Genomic DNA. Translation: CAI40731.1. AL606754 , AL590394, AL928898, Z83745 Genomic DNA. Translation: CAI40852.1. Z83745 , AL590394, AL606754, AL928898 Genomic DNA. Translation: CAI42802.1. BC048279 mRNA. Translation: AAH48279.1. BC073922 mRNA. Translation: AAH73922.1.
IPI	IPI00043550.
RefSeq	NP_777572.2.
UniGene	Hs.496205. Hs.724714.
3D structure databases
ProteinModelPortal	Q6GMR7.
SMR	Q6GMR7. Positions 51-524.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GMR7.
Proteomic databases
PRIDE	Q6GMR7.
Genome annotation databases
Ensembl	ENST00000374900; ENSP00000364035; ENSG00000165591; Homo sapiens. [Genome view]
GeneID	158584.
KEGG	hsa:158584.
Organism-specific databases
CTD	158584.
GeneCards	GC0XP057330.
H-InvDB	HIX0021688.
HGNC	HGNC:26440. FAAH2.
HPA	HPA027534.
MIM	300654. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08686.
HOGENOM	HBG481888.
HOVERGEN	HBG101001.
InParanoid	Q6GMR7.
OMA	MEHDGGS.
OrthoDB	EOG9PZMS9.
PhylomeDB	Q6GMR7.
Gene expression databases
ArrayExpress	Q6GMR7.
Bgee	Q6GMR7.
CleanEx	HS_FAAH2.
Genevestigator	Q6GMR7.
Family and domain databases
InterPro	IPR000120. Amidase. IPR020556. Amidase_CS. [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]
SUPFAM	SSF75304. Amidase_sig_enz. 1 hit.
PROSITE	PS00571. AMIDASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	87770.
SOURCE	Search...

Entry information

Entry name

FAAH2_HUMAN

Accession

Primary (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:	August 10, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.