FAH2B_DANRE
ID FAH2B_DANRE Reviewed; 526 AA.
AC Q05AM4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Fatty-acid amide hydrolase 2-B;
DE EC=3.5.1.99;
GN Name=faah2b; ORFNames=zgc:153568;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION AS FAAH2B.
RX PubMed=17256142; DOI=10.1007/s00438-007-0207-3;
RA McPartland J.M., Glass M., Matias I., Norris R.W., Kilpatrick C.W.;
RT "A shifted repertoire of endocannabinoid genes in the zebrafish (Danio
RT rerio).";
RL Mol. Genet. Genomics 277:555-570(2007).
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 -!- 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; BC124392; AAI24393.1; -; mRNA.
DR RefSeq; NP_001070930.1; NM_001077462.1.
DR AlphaFoldDB; Q05AM4; -.
DR SMR; Q05AM4; -.
DR STRING; 7955.ENSDARP00000071507; -.
DR PaxDb; Q05AM4; -.
DR GeneID; 768298; -.
DR KEGG; dre:768298; -.
DR CTD; 768298; -.
DR ZFIN; ZDB-GENE-061027-358; faah2b.
DR eggNOG; KOG1212; Eukaryota.
DR InParanoid; Q05AM4; -.
DR OrthoDB; 852596at2759; -.
DR PhylomeDB; Q05AM4; -.
DR Reactome; R-DRE-2142753; Arachidonic acid metabolism.
DR PRO; PR:Q05AM4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0103073; F:anandamide amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102077; F:oleamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Fatty-acid amide hydrolase 2-B"
FT /id="PRO_0000291995"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 227
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 526 AA; 57026 MW; 271E1756BABDDA86 CRC64;
MGLTLGERVQ HCLLVLVSGL FLALFRLLSP GTKRPKHLPP ITNPLLTLSA VQLAEKIRRG
EVSSVEVVQA YIDRIQEVNP LLNALIKDRF SAALLEAARA DKLIKEENGG EEVLRNQFPL
LGVPMSVKES FGLQGMPNSG GLKSRGKVLA SVDAPPVALL KRAGAIPLGV TNTSELCMWM
ESNNHLYGIT SNPYNLERIC GGSSGGEGSI IGGGASVFGI GSDIGGSIRM PCFFNGIFGH
KPSRGVVSND NQFPRCSGLQ NEYTGSGPMC RYAEDLLPLL KIMAGPTADK LTLSKAVDLK
KLRFFTIVDD GGSPLTSPVD RQLVEVQKRV AARLEADLGV TVQEVNFPQL KYSYQIWDTF
LALPDKDGKP PEAFVELMAD GGSVWPVWEL IKRIFGRSEH TVAAIGLALM ESSHSSKSSE
FILKQKEDLQ REMEDLLGTD GVLLYPSHPL LAPKHHHPLF MPFNFSYTGI LNILGLPVTQ
CPLGLSKERL PLGVQVVAGL CQDHLTLAMA LYLEKAFGGW VDPGVV