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Q6GMR7

- FAAH2_HUMAN

UniProt

Q6GMR7 - FAAH2_HUMAN

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Protein

Fatty-acid amide hydrolase 2

Gene
FAAH2, AMDD
Organism
Homo sapiens (Human)
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 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 system By similarity
Active sitei206 – 2061Charge relay system By similarity
Active sitei230 – 2301Acyl-ester intermediate By 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

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: Chromosome X

Organism-specific databases

HGNCiHGNC:26440. FAAH2.

Subcellular locationi

Membrane; Single-pass membrane protein Reviewed prediction 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Reviewed predictionAdd
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.

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

ArrayExpressiQ6GMR7.
BgeeiQ6GMR7.
CleanExiHS_FAAH2.
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.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the amidase family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0154.
HOGENOMiHOG000116697.
HOVERGENiHBG101001.
InParanoidiQ6GMR7.
OMAiEKTFGGW.
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

MAPSFTARIQ LFLLRALGFL IGLVGRAALV LGGPKFASKT PRPVTEPLLL    50
LSGMQLAKLI RQRKVKCIDV VQAYINRIKD VNPMINGIVK YRFEEAMKEA 100
HAVDQKLAEK QEDEATLENK WPFLGVPLTV KEAFQLQGMP NSSGLMNRRD 150
AIAKTDATVV ALLKGAGAIP LGITNCSELC MWYESSNKIY GRSNNPYDLQ 200
HIVGGSSGGE GCTLAAACSV IGVGSDIGGS IRMPAFFNGI FGHKPSPGVV 250
PNKGQFPLAV GAQELFLCTG PMCRYAEDLA PMLKVMAGPG IKRLKLDTKV 300
HLKDLKFYWM EHDGGSFLMS KVDQDLIMTQ KKVVVHLETI LGASVQHVKL 350
KKMKYSFQLW IAMMSAKGHD GKEPVKFVDL LGDHGKHVSP LWELIKWCLG 400
LSVYTIPSIG LALLEEKLRY SNEKYQKFKA VEESLRKELV DMLGDDGVFL 450
YPSHPTVAPK HHVPLTRPFN FAYTGVFSAL GLPVTQCPLG LNAKGLPLGI 500
QVVAGPFNDH LTLAVAQYLE KTFGGWVCPG KF 532
Length:532
Mass (Da):58,304
Last modified:July 19, 2004 - v1
Checksum:i1D83E34BFF186E5E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981K → R in BAB71007. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi74757585.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14375.1.
RefSeqi NP_777572.2. NM_174912.3.
UniGenei Hs.496205.
Hs.745495.

3D structure databases

ProteinModelPortali Q6GMR7.
SMRi Q6GMR7. Positions 56-524.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127693. 1 interaction.
STRINGi 9606.ENSP00000364035.

Chemistry

ChEMBLi CHEMBL1628475.
GuidetoPHARMACOLOGYi 1401.

PTM databases

PhosphoSitei Q6GMR7.

Polymorphism databases

DMDMi 74757585.

Proteomic databases

MaxQBi Q6GMR7.
PaxDbi Q6GMR7.
PRIDEi Q6GMR7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374900 ; ENSP00000364035 ; ENSG00000165591 .
GeneIDi 158584.
KEGGi hsa:158584.
UCSCi uc004dvc.3. human.

Organism-specific databases

CTDi 158584.
GeneCardsi GC0XP057330.
H-InvDB HIX0021688.
HGNCi HGNC:26440. FAAH2.
HPAi HPA027534.
MIMi 300654. gene.
neXtProti NX_Q6GMR7.
PharmGKBi PA162385543.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0154.
HOGENOMi HOG000116697.
HOVERGENi HBG101001.
InParanoidi Q6GMR7.
OMAi EKTFGGW.
OrthoDBi EOG7PZRX7.
PhylomeDBi Q6GMR7.
TreeFami TF313781.

Miscellaneous databases

ChiTaRSi FAAH2. human.
GenomeRNAii 158584.
NextBioi 87770.
PROi Q6GMR7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6GMR7.
Bgeei Q6GMR7.
CleanExi HS_FAAH2.
Genevestigatori Q6GMR7.

Family and domain databases

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

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: July 9, 2014
This is version 96 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

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