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   27-MAR-2024, entry version 85.
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}.
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   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; 7955-ENSDARP00000071507; -.
DR   GeneID; 768298; -.
DR   KEGG; dre:768298; -.
DR   AGR; ZFIN:ZDB-GENE-061027-358; -.
DR   CTD; 768298; -.
DR   ZFIN; ZDB-GENE-061027-358; faah2b.
DR   eggNOG; KOG1212; Eukaryota.
DR   InParanoid; Q05AM4; -.
DR   OrthoDB; 146362at2759; -.
DR   PhylomeDB; Q05AM4; -.
DR   PRO; PR:Q05AM4; -.
DR   Proteomes; UP000000437; Alternate scaffold 7.
DR   Proteomes; UP000000437; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR43372; FATTY-ACID AMIDE HYDROLASE; 1.
DR   PANTHER; PTHR43372:SF4; FATTY-ACID AMIDE HYDROLASE 2; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   PIRSF; PIRSF001221; Amidase_fungi; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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
//