ID   FAH2A_DANRE             Reviewed;         532 AA.
AC   Q6DH69;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Fatty-acid amide hydrolase 2-A;
DE            EC=3.5.1.99;
GN   Name=faah2a; ORFNames=zgc:92625;
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   STRAIN=AB; TISSUE=Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION AS FAAH2A.
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; BC076113; AAH76113.1; -; mRNA.
DR   RefSeq; NP_001002700.1; NM_001002700.2.
DR   AlphaFoldDB; Q6DH69; -.
DR   SMR; Q6DH69; -.
DR   STRING; 7955.ENSDARP00000037509; -.
DR   PaxDb; Q6DH69; -.
DR   Ensembl; ENSDART00000037553; ENSDARP00000037509; ENSDARG00000008457.
DR   Ensembl; ENSDART00000185873; ENSDARP00000146345; ENSDARG00000112163.
DR   GeneID; 436973; -.
DR   KEGG; dre:436973; -.
DR   CTD; 436973; -.
DR   ZFIN; ZDB-GENE-040718-453; faah2a.
DR   eggNOG; KOG1212; Eukaryota.
DR   GeneTree; ENSGT00940000162502; -.
DR   HOGENOM; CLU_009600_16_1_1; -.
DR   InParanoid; Q6DH69; -.
DR   OMA; VCMWVES; -.
DR   OrthoDB; 852596at2759; -.
DR   PhylomeDB; Q6DH69; -.
DR   TreeFam; TF313781; -.
DR   PRO; PR:Q6DH69; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000008457; Expressed in liver and 19 other tissues.
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..532
FT                   /note="Fatty-acid amide hydrolase 2-A"
FT                   /id="PRO_0000291994"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  58093 MW;  D986716F9702E59E CRC64;
     MALTRFERFL GRLLRAVVWI LFAAFKLFAP QQRHGVSRLP PITNPLLLLS AMQLARKIRR
     KEVTSVEVVQ AYIDRIQEVN PLINAMVKDR FSAALQEAAQ VDKLIEEETG GEDVLEDRLP
     LLGVPITVKE AFALQGMPNS TGLLTRRDLV SGADAPSVAL LKRAGAIPLG VTNCSELCMW
     LESHNHLYGI TNNPYDFERI VGGSSGGEGS ILGAGSSVIG IGSDIGGSIR IPCFFNGIFG
     HKPSVGIVNN EGQYPPASGQ QMGFLCTGPM CRYAEDLIPM LSIMGGPNAE KLSLFTEVDL
     KKLRFFSVPH NGGSHLVSPV EPQLLHAQKM VVKRLEADLG VKVQELLIPQ LKYSFQIWGT
     MMASPGKDGK PPTTFAELMS EGGKKVWPAW ELFKWFLGFS SHTLAAIGLA LVELFQSSHP
     SPFIMQQKES LQQELEELLG TDGVLLYPSH PLIAQKHHHP IFTPFNFSYT GIFNILGLPV
     TQCPLGLSAE GLPLGVQIVA GKLQDRLSLA TALYLEKAFG GWREPGKTTI KP