| Tag | Content |
|---|
| CPLM ID | CPLM-000192 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Fatty-acid amide hydrolase 1 |
Protein Synonyms/Alias | Anandamide amidohydrolase 1; Oleamide hydrolase 1 |
Gene Name | Faah |
Gene Synonyms/Alias | Faah1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 57 | AGLETMDKAVQRFRL | ubiquitination | [1] | | 142 | YGVPVSLKECFSYKG | ubiquitination | [1] | | 255 | FCGICGLKPTGNRLS | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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). |
Sequence Annotation | REGION 238 241 Substrate binding (By similarity).
ACT_SITE 142 142 Charge relay system (By similarity).
ACT_SITE 217 217 Charge relay system (By similarity).
ACT_SITE 241 241 Acyl-ester intermediate (By similarity).
BINDING 191 191 Substrate; via carbonyl oxygen (By
BINDING 217 217 Substrate (By similarity). |
Keyword | Complete proteome; Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane; Reference proteome; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 579 AA |
Protein Sequence | MVLSEVWTAL SGLSGVCLAC SLLSAAVVLR WTRSQTARGA VTRARQKQRA GLETMDKAVQ 60
RFRLQNPDLD SEALLALPLL QLVQKLQSGE LSPEAVLFTY LGKAWEVNKG TNCVTSYLTD 120
CETQLSQAPR QGLLYGVPVS LKECFSYKGH ASTLGLSLNE GVTSESDCVV VQVLKLQGAV 180
PFVHTNVPQS MLSYDCSNPL FGQTMNPWKP SKSPGGSSGG EGALIGSGGS PLGLGTDIGG 240
SIRFPSAFCG ICGLKPTGNR LSKSGLKSCV YGQTAVQLSV GPMARDVDSL ALCMKALLCE 300
DLFRLDSTIP PLPFREEIYR SSRPLRVGYY ETDNYTMPTP AMRRAVMETK QSLEAAGHTL 360
VPFLPNNIPY ALEVLSAGGL FSDGGCSFLQ NFKGDFVDPC LGDLVLVLKL PRWFKKLLSF 420
LLKPLFPRLA AFLNSMCPRS AEKLWELQHE IEMYRQSVIA QWKAMNLDVV LTPMLGPALD 480
LNTPGRATGA ISYTVLYNCL DFPAGVVPVT TVTAEDDAQM EHYKGYFGDM WDNILKKGMK 540
KGIGLPVAVQ CVALPWQEEL CLRFMREVER LMTPEKRPS 579 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0031090; C:organelle membrane; ISS:UniProtKB. GO:0047372; F:acylglycerol lipase activity; IMP:MGI. GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro. GO:0017064; F:fatty acid amide hydrolase activity; ISS:UniProtKB. GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |