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Protein

Fatty-acid amide hydrolase 2

Gene

FAAH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 monounsaturated substrate anandamide preferentially as compared to polyunsaturated substrates.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by O-aryl carbamates and alpha-keto heterocytes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Charge relay systemBy similarity
Active sitei206 – 2061Charge relay systemBy similarity
Active sitei230 – 2301Acyl-ester intermediateBy similarity

GO - Molecular functioni

  1. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
  2. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.4. 2681.
3.5.1.99. 2681.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FAAH2
Synonyms:AMDD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:26440. FAAH2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385543.

Polymorphism and mutation databases

BioMutaiFAAH2.
DMDMi74757585.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Fatty-acid amide hydrolase 2PRO_0000291993Add
BLAST

Proteomic databases

MaxQBiQ6GMR7.
PaxDbiQ6GMR7.
PRIDEiQ6GMR7.

PTM databases

PhosphoSiteiQ6GMR7.

Expressioni

Tissue specificityi

Highly expressed in the brain, small intestine and testis. Also expressed in the heart, kidney, liver, lung and prostate.1 Publication

Gene expression databases

BgeeiQ6GMR7.
CleanExiHS_FAAH2.
ExpressionAtlasiQ6GMR7. baseline and differential.
GenevestigatoriQ6GMR7.

Organism-specific databases

HPAiHPA027534.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi127693. 1 interaction.
STRINGi9606.ENSP00000364035.

Structurei

3D structure databases

ProteinModelPortaliQ6GMR7.
SMRiQ6GMR7. Positions 56-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 514Poly-Leu

Sequence similaritiesi

Belongs to the amidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000116697.
HOVERGENiHBG101001.
InParanoidiQ6GMR7.
OMAiMMSAKGH.
OrthoDBiEOG7PZRX7.
PhylomeDBiQ6GMR7.
TreeFamiTF313781.

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.

Q6GMR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSFTARIQ LFLLRALGFL IGLVGRAALV LGGPKFASKT PRPVTEPLLL
60 70 80 90 100
LSGMQLAKLI RQRKVKCIDV VQAYINRIKD VNPMINGIVK YRFEEAMKEA
110 120 130 140 150
HAVDQKLAEK QEDEATLENK WPFLGVPLTV KEAFQLQGMP NSSGLMNRRD
160 170 180 190 200
AIAKTDATVV ALLKGAGAIP LGITNCSELC MWYESSNKIY GRSNNPYDLQ
210 220 230 240 250
HIVGGSSGGE GCTLAAACSV IGVGSDIGGS IRMPAFFNGI FGHKPSPGVV
260 270 280 290 300
PNKGQFPLAV GAQELFLCTG PMCRYAEDLA PMLKVMAGPG IKRLKLDTKV
310 320 330 340 350
HLKDLKFYWM EHDGGSFLMS KVDQDLIMTQ KKVVVHLETI LGASVQHVKL
360 370 380 390 400
KKMKYSFQLW IAMMSAKGHD GKEPVKFVDL LGDHGKHVSP LWELIKWCLG
410 420 430 440 450
LSVYTIPSIG LALLEEKLRY SNEKYQKFKA VEESLRKELV DMLGDDGVFL
460 470 480 490 500
YPSHPTVAPK HHVPLTRPFN FAYTGVFSAL GLPVTQCPLG LNAKGLPLGI
510 520 530
QVVAGPFNDH LTLAVAQYLE KTFGGWVCPG KF
Length:532
Mass (Da):58,304
Last modified:July 19, 2004 - v1
Checksum:i1D83E34BFF186E5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981K → R in BAB71007 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14375.1.
RefSeqiNP_777572.2. NM_174912.3.
UniGeneiHs.496205.
Hs.745495.

Genome annotation databases

EnsembliENST00000374900; ENSP00000364035; ENSG00000165591.
GeneIDi158584.
KEGGihsa:158584.
UCSCiuc004dvc.3. human.

Polymorphism and mutation databases

BioMutaiFAAH2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14375.1.
RefSeqiNP_777572.2. NM_174912.3.
UniGeneiHs.496205.
Hs.745495.

3D structure databases

ProteinModelPortaliQ6GMR7.
SMRiQ6GMR7. Positions 56-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127693. 1 interaction.
STRINGi9606.ENSP00000364035.

Chemistry

BindingDBiQ6GMR7.
ChEMBLiCHEMBL1628475.
GuidetoPHARMACOLOGYi1401.

PTM databases

PhosphoSiteiQ6GMR7.

Polymorphism and mutation databases

BioMutaiFAAH2.
DMDMi74757585.

Proteomic databases

MaxQBiQ6GMR7.
PaxDbiQ6GMR7.
PRIDEiQ6GMR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374900; ENSP00000364035; ENSG00000165591.
GeneIDi158584.
KEGGihsa:158584.
UCSCiuc004dvc.3. human.

Organism-specific databases

CTDi158584.
GeneCardsiGC0XP057330.
H-InvDBHIX0021688.
HGNCiHGNC:26440. FAAH2.
HPAiHPA027534.
MIMi300654. gene.
neXtProtiNX_Q6GMR7.
PharmGKBiPA162385543.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0154.
GeneTreeiENSGT00550000074673.
HOGENOMiHOG000116697.
HOVERGENiHBG101001.
InParanoidiQ6GMR7.
OMAiMMSAKGH.
OrthoDBiEOG7PZRX7.
PhylomeDBiQ6GMR7.
TreeFamiTF313781.

Enzyme and pathway databases

BRENDAi3.5.1.4. 2681.
3.5.1.99. 2681.

Miscellaneous databases

ChiTaRSiFAAH2. human.
GenomeRNAii158584.
NextBioi87770.
PROiQ6GMR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6GMR7.
CleanExiHS_FAAH2.
ExpressionAtlasiQ6GMR7. baseline and differential.
GenevestigatoriQ6GMR7.

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. "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] [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.
    , 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.

Entry informationi

Entry nameiFAAH2_HUMAN
AccessioniPrimary (citable) accession number: Q6GMR7
Secondary accession number(s): Q86VT2, Q96N98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 19, 2004
Last modified: April 29, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.