GenomeNet

Database: UniProt
Entry: A0A2Y9NPR7_DELLE
LinkDB: A0A2Y9NPR7_DELLE
Original site: A0A2Y9NPR7_DELLE 
ID   A0A2Y9NPR7_DELLE        Unreviewed;       655 AA.
AC   A0A2Y9NPR7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=fatty acid amide hydrolase {ECO:0000256|ARBA:ARBA00012112};
DE            EC=3.5.1.99 {ECO:0000256|ARBA:ARBA00012112};
GN   Name=FAAH {ECO:0000313|RefSeq:XP_022431318.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022431318.1};
RN   [1] {ECO:0000313|RefSeq:XP_022431318.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022431318.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenamide + H2O = (9Z)-octadecenoate + NH4(+);
CC         Xref=Rhea:RHEA:26506, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:116314; EC=3.5.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000208};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507;
CC         Evidence={ECO:0000256|ARBA:ARBA00000208};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine;
CC         Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000231};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137;
CC         Evidence={ECO:0000256|ARBA:ARBA00000231};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl) ethanolamine = (9Z)-octadecenoate +
CC         ethanolamine; Xref=Rhea:RHEA:45060, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57603, ChEBI:CHEBI:71466;
CC         Evidence={ECO:0000256|ARBA:ARBA00000890};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45061;
CC         Evidence={ECO:0000256|ARBA:ARBA00000890};
CC   -!- SIMILARITY: Belongs to the amidase family.
CC       {ECO:0000256|ARBA:ARBA00009199}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_022431318.1; XM_022575610.2.
DR   AlphaFoldDB; A0A2Y9NPR7; -.
DR   STRING; 9749.A0A2Y9NPR7; -.
DR   KEGG; dle:111175768; -.
DR   InParanoid; A0A2Y9NPR7; -.
DR   OrthoDB; 731186at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 2.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR45847; FATTY ACID AMIDE HYDROLASE; 1.
DR   PANTHER; PTHR45847:SF3; FATTY-ACID AMIDE HYDROLASE 1; 1.
DR   Pfam; PF01425; Amidase; 2.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 2.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801,
KW   ECO:0000313|RefSeq:XP_022431318.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          96..269
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   DOMAIN          348..638
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   655 AA;  70274 MW;  93C663FA37456598 CRC64;
     MVLEELWAAL SGSSGATLAC CLVAAALALR WSSHRTARGA AARARQRQQA ALETMDKAAQ
     RFRLQNPDLD SEALLALPLP QLVQKLHSGE LSPEAVLFTY LGKAWEVNKG TNCVTAYLAD
     CEAQLCQAPR QGLLYGVPVS LKECFSYKGQ DSTLGLSLHE GAPAERDSVV VQVLKRQGAL
     PFVYTNVPQS MFSYDCGNPL FGQTVNPWKS SKSPGGSSGG EGALIAAGGS PLGLGTDIGG
     SIRFPSAFCG ICGLKPTGNR ISKSGLKGCV YGQVAGEVCG SLYALEEGGL PDLPLPLPLL
     GAVLGPQATL GLSSCALSLF TLRATAQSLL GPGPRAPWGW VISLSSPPCP TVQLSVGPMA
     RDVESLALCL RALLCEDMFH LDPSVPPLPF REEVYTSSQP LRVGYYETDN YTMPTPAMTR
     ALLETKKRLE AAGHTLVPFL PSNIPHALET LSTGGLFSDG GKSFLQNFKG DFVDPCLGNL
     ISALRLPSWL KGLLAFMLRP LLPRLSAFLN SMKSRSAGKL WELHHEIEVY RHSVIAQWRA
     VELDVLLTPM LGPALDLNGP GKATGAISYT LLYNCLDFPA GVVPVTTVTA EDEAQLEHYK
     GCFGDIWDKA LQKAVKKSVG LPVAVQCVAL PWQEELCLRF MREVERLMTP ERQPC
//
DBGET integrated database retrieval system