LOCUS       NM_174912               1980 bp    mRNA    linear   PRI 10-JUN-2024
DEFINITION  Homo sapiens fatty acid amide hydrolase 2 (FAAH2), transcript
            variant 1, mRNA.
ACCESSION   NM_174912
VERSION     NM_174912.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1980)
  AUTHORS   Sirrs,S., van Karnebeek,C.D., Peng,X., Shyr,C., Tarailo-Graovac,M.,
            Mandal,R., Testa,D., Dubin,D., Carbonetti,G., Glynn,S.E.,
            Sayson,B., Robinson,W.P., Han,B., Wishart,D., Ross,C.J.,
            Wasserman,W.W., Hurwitz,T.A., Sinclair,G. and Kaczocha,M.
  TITLE     Defects in fatty acid amide hydrolase 2 in a male with neurologic
            and psychiatric symptoms
  JOURNAL   Orphanet J Rare Dis 10, 38 (2015)
   PUBMED   25885783
  REMARK    GeneRIF: A male patient with neuropsychiatric disorders attributed
            to a FAAH2 missense mutation is described.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1980)
  AUTHORS   Kaczocha,M., Glaser,S.T., Chae,J., Brown,D.A. and Deutsch,D.G.
  TITLE     Lipid droplets are novel sites of N-acylethanolamine inactivation
            by fatty acid amide hydrolase-2
  JOURNAL   J Biol Chem 285 (4), 2796-2806 (2010)
   PUBMED   19926788
  REMARK    GeneRIF: results establish FAAH-2 as a bone fide
            N-acylethanolamine-catabolizing enzyme and suggest that
            inactivation is spatially separated in cells of higher mammals
REFERENCE   3  (bases 1 to 1980)
  AUTHORS   Karbarz,M.J., Luo,L., Chang,L., Tham,C.S., Palmer,J.A.,
            Wilson,S.J., Wennerholm,M.L., Brown,S.M., Scott,B.P., Apodaca,R.L.,
            Keith,J.M., Wu,J., Breitenbucher,J.G., Chaplan,S.R. and Webb,M.
  TITLE     Biochemical and biological properties of 4-(3-phenyl-[1,2,4]
            thiadiazol-5-yl)-piperazine-1-carboxylic acid phenylamide, a
            mechanism-based inhibitor of fatty acid amide hydrolase
  JOURNAL   Anesth Analg 108 (1), 316-329 (2009)
   PUBMED   19095868
  REMARK    GeneRIF: Biochemical and biological properties of
            4-(3-phenyl-[1,2,4] thiadiazol-5-yl)-piperazine-1-carboxylic acid
            phenylamide, a mechanism-based inhibitor of fatty acid amide
            hydrolase.
REFERENCE   4  (bases 1 to 1980)
  AUTHORS   Wei,B.Q., Mikkelsen,T.S., McKinney,M.K., Lander,E.S. and
            Cravatt,B.F.
  TITLE     A second fatty acid amide hydrolase with variable distribution
            among placental mammals
  JOURNAL   J Biol Chem 281 (48), 36569-36578 (2006)
   PUBMED   17015445
  REMARK    GeneRIF: FAAH2 is the second membrane-associated AS enzyme in
            humans that displays FAAH activity
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83745.1, AL590394.7,
            AL928898.6 and AL606754.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 29, 2020 this sequence version replaced NM_174912.3.
            
            Summary: This gene encodes a fatty acid amide hydrolase that shares
            a conserved protein motif with the amidase signature family of
            enzymes. The encoded enzyme is able to catalyze the hydrolysis of a
            broad range of bioactive lipids, including those from the three
            main classes of fatty acid amides; N-acylethanolamines, fatty acid
            primary amides and N-acyl amino acids. This enzyme has a preference
            for monounsaturated acyl chains as a substrate. Alternate splicing
            results in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055766.1, BC073922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374900.5/ ENSP00000364035.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-312               Z83745.1           125072-125383
            313-375             Z83745.1           130864-130926
            376-395             AL590394.7         2001-2020
            396-532             AL590394.7         20033-20169
            533-742             AL590394.7         41038-41247
            743-862             AL590394.7         50711-50830
            863-998             AL928898.6         27896-28031
            999-1116            AL928898.6         30157-30274
            1117-1236           AL928898.6         81163-81282
            1237-1348           AL606754.6         9404-9515
            1349-1543           AL606754.6         11000-11194
            1544-1980           AL606754.6         51233-51669
FEATURES             Location/Qualifiers
     source          1..1980
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     gene            1..1980
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /note="fatty acid amide hydrolase 2"
                     /db_xref="GeneID:158584"
                     /db_xref="HGNC:HGNC:26440"
                     /db_xref="MIM:300654"
     exon            1..312
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     CDS             121..1719
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /EC_number="3.5.1.99"
                     /note="isoform 1 is encoded by transcript variant 1;
                     amidase domain containing; anandamide amidohydrolase 2;
                     oleamide hydrolase 2; amidase domain-containing protein"
                     /codon_start=1
                     /product="fatty-acid amide hydrolase 2 isoform 1"
                     /protein_id="NP_777572.2"
                     /db_xref="CCDS:CCDS14375.1"
                     /db_xref="GeneID:158584"
                     /db_xref="HGNC:HGNC:26440"
                     /db_xref="MIM:300654"
                     /translation="MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPV
                     TEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHA
                     VDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVV
                     ALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAAC
                     SVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYA
                     EDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVV
                     VHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLW
                     ELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFL
                     YPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFN
                     DHLTLAVAQYLEKTFGGWVCPGKF"
     exon            313..395
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            396..532
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            533..742
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            743..862
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            863..998
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            999..1116
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            1117..1236
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            1237..1348
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            1349..1543
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     exon            1544..1980
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1960..1965
                     /regulatory_class="polyA_signal_sequence"
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /note="hexamer: AATAAA"
     polyA_site      1980
                     /gene="FAAH2"
                     /gene_synonym="AMDD"
                     /note="major polyA site"
ORIGIN      
        1 agacactgga cttgtaaacg aaaagcttca taagtccctc tttgcttagt acttttctcg
       61 tcctttcccc agggtgcacg taaccctcaa gcactaggac cgtgcggaat ccaggctgcg
      121 atggcacctt catttaccgc ccgcattcag ttgttcctct tgcgggcgct aggctttctc
      181 ataggcttag taggccgagc agctttagtc ttagggggtc caaagtttgc ctcaaagacc
      241 cctcggccgg tgactgaacc attgcttctg ctttcgggga tgcagctggc caagctgatc
      301 cgacagagaa aggtgaaatg tatagatgtt gttcaggctt atatcaacag aatcaaggac
      361 gtgaacccaa tgatcaatgg aattgtcaag tacaggtttg aggaagcgat gaaggaggct
      421 catgctgtag atcaaaagct tgcagagaag caggaagatg aagccaccct ggaaaataaa
      481 tggcccttcc ttggggttcc tttgacagtc aaggaagctt tccagctaca aggaatgccc
      541 aattcttctg gactcatgaa ccgtcgtgat gccattgcca aaacagatgc cactgtggtg
      601 gcattactga agggagctgg tgccattcct cttggcataa ccaactgtag tgagttgtgt
      661 atgtggtatg aatccagtaa caagatctat ggccgatcaa acaacccata tgatttacag
      721 catattgtag gtggaagttc tggtggtgag ggctgcacac tggcagctgc ctgctcagtt
      781 attggtgtgg gctctgatat tggtggtagc attcgaatgc ctgctttctt caatggtata
      841 tttggacaca agccttctcc aggtgtggtt cccaacaaag gtcagtttcc cttggctgtg
      901 ggagcccagg agttgtttct gtgcactggt cctatgtgcc gttatgctga agacctggcc
      961 cccatgttga aggtcatggc aggacctggg atcaaaaggt taaaactaga cacaaaggta
     1021 catttaaaag acttaaaatt ttactggatg gaacatgatg gaggctcatt tttaatgtcc
     1081 aaagtggacc aagatctcat tatgactcag aaaaaggttg tggttcacct tgaaactatt
     1141 ctaggagcct cagttcaaca tgttaaactg aagaaaatga agtactcttt tcagttgtgg
     1201 atcgcaatga tgtcagcaaa gggacatgat gggaaggaac ctgtgaaatt tgtagatttg
     1261 cttggtgacc atgggaaaca tgtcagtcct ctgtgggagt tgatcaaatg gtgcctgggt
     1321 ctgtcagtgt acaccatccc ttccattgga ctggctttgt tggaagaaaa gctcagatat
     1381 agcaatgaga aataccaaaa gtttaaggca gtggaagaaa gcctgcgtaa agagctggtg
     1441 gatatgctag gtgatgatgg tgtgttctta tatccctcac atcccacagt ggcacctaag
     1501 catcatgtcc ctctaacacg gcctttcaac tttgcttaca caggtgtctt cagtgccctg
     1561 ggtttgcctg tgacccaatg cccactggga ctgaatgcca aaggactccc tttaggcatc
     1621 caggttgtgg ctggaccctt taatgatcat ctgaccctgg ctgtggccca gtacttggag
     1681 aaaacttttg ggggctgggt ctgtccagga aagttttagg aggaccttct gcaaggttaa
     1741 tgtgtgtgtg tgtttgtgtt cgtgtggtgg tgtttctatt aattgggtga aatcaagcac
     1801 cagcagacaa gcagagaaac aactggggaa tttattgact catttagtta ttctttctac
     1861 ttttatttcc ttctctaact gttggtctta ctaaaatggt aatatttgct tcttgctttt
     1921 atgttactgg aaaattagga catgtaaatg gataagtgca ataaagtttc ctaaatgctg
//
