LOCUS       NM_001302479            1316 bp    mRNA    linear   ROD 30-APR-2024
DEFINITION  Mus musculus aminoacylase 3 (Acy3), transcript variant 1, mRNA.
ACCESSION   NM_001302479
VERSION     NM_001302479.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (bases 1 to 1316)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (bases 1 to 1316)
  AUTHORS   Tsirulnikov,K., Abuladze,N., Vahi,R., Hasnain,H., Phillips,M.,
            Ryan,C.M., Atanasov,I., Faull,K.F., Kurtz,I. and Pushkin,A.
  TITLE     Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis
            C virus core protein
  JOURNAL   FEBS Lett 586 (21), 3799-3804 (2012)
   PUBMED   23010594
  REMARK    GeneRIF: Aminoacylase 3 binds to and cleaves the N-terminus of the
            hepatitis C virus that may by implicated in HCV pathogenesis.
REFERENCE   3  (bases 1 to 1316)
  AUTHORS   Hsieh,J.M., Tsirulnikov,K., Sawaya,M.R., Magilnick,N., Abuladze,N.,
            Kurtz,I., Abramson,J. and Pushkin,A.
  TITLE     Structures of aminoacylase 3 in complex with acetylated substrates
  JOURNAL   Proc Natl Acad Sci U S A 107 (42), 17962-17967 (2010)
   PUBMED   20921362
  REMARK    GeneRIF: structures, in conjunction with biochemical data,
            indicated that AA3 mediates substrate specificity through van der
            Waals interactions providing a dynamic interaction interface, which
            facilitates a diverse range of substrates
REFERENCE   4  (bases 1 to 1316)
  AUTHORS   Tsirulnikov,K., Abuladze,N., Newman,D., Ryazantsev,S., Wolak,T.,
            Magilnick,N., Koag,M.C., Kurtz,I. and Pushkin,A.
  TITLE     Mouse aminoacylase 3: a metalloenzyme activated by cobalt and
            nickel
  JOURNAL   Biochim Biophys Acta 1794 (7), 1049-1057 (2009)
   PUBMED   19362172
REFERENCE   5  (bases 1 to 1316)
  AUTHORS   Ryazantsev,S., Abuladze,N., Newman,D., Bondar,G., Kurtz,I. and
            Pushkin,A.
  TITLE     Structural characterization of dimeric murine aminoacylase III
  JOURNAL   FEBS Lett 581 (9), 1898-1902 (2007)
   PUBMED   17434493
  REMARK    GeneRIF: A 16A resolution model of the AAIII dimer.
REFERENCE   6  (bases 1 to 1316)
  AUTHORS   Newman,D., Abuladze,N., Scholz,K., Dekant,W., Tsuprun,V.,
            Ryazantsev,S., Bondar,G., Sassani,P., Kurtz,I. and Pushkin,A.
  TITLE     Specificity of aminoacylase III-mediated deacetylation of
            mercapturic acids
  JOURNAL   Drug Metab Dispos 35 (1), 43-50 (2007)
   PUBMED   17012540
REFERENCE   7  (bases 1 to 1316)
  AUTHORS   Pushkin,A., Carpenito,G., Abuladze,N., Newman,D., Tsuprun,V.,
            Ryazantsev,S., Motemoturu,S., Sassani,P., Solovieva,N.,
            Dukkipati,R. and Kurtz,I.
  TITLE     Structural characterization, tissue distribution, and functional
            expression of murine aminoacylase III
  JOURNAL   Am J Physiol Cell Physiol 286 (4), C848-C856 (2004)
   PUBMED   14656720
  REMARK    GeneRIF: data suggest that in kidney proximal tubules, aminoacylase
            III plays an important role in deacetylating mercapturic acids
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK143782.1 and AA110692.1.
            
            Summary: This gene encodes a member of the aminoacylase family of
            enzymes. This enzyme specifically deacetylates N-acetyl aromatic
            amino acids and mercapturic acids. Action of this enzyme on
            metabolites of the environmental contaminant trichloroethylene
            leads to the generation of toxic products that may lead to kidney
            failure. This protein has been found to bind to the hepatitis C
            virus core protein. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1282              AK143782.1         2-1283
            1283-1316           AA110692.1         256-289
FEATURES             Location/Qualifiers
     source          1..1316
                     /organism="Mus musculus"
                     /mol_type="mRNA"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 3.7 cM"
     gene            1..1316
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /note="aminoacylase 3"
                     /db_xref="GeneID:71670"
                     /db_xref="MGI:MGI:1918920"
     exon            1..42
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            43..171
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            172..426
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     CDS             191..1147
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /EC_number="3.5.1.114"
                     /note="isoform 1 is encoded by transcript variant 1;
                     aspartoacylase-2; acylase III; hepatitis C virus
                     core-binding protein 1; aminoacylase III;
                     N-acyl-aromatic-L-amino acid amidohydrolase
                     (carboxylate-forming); aspartoacylase (aminoacylase) 3"
                     /codon_start=1
                     /product="N-acyl-aromatic-L-amino acid amidohydrolase
                     (carboxylate-forming) isoform 1"
                     /protein_id="NP_001289408.1"
                     /db_xref="CCDS:CCDS29406.1"
                     /db_xref="GeneID:71670"
                     /db_xref="MGI:MGI:1918920"
                     /translation="MSSLPGSREPLLRVAVTGGTHGNEMCGVYLARYWLQNPGELQRP
                     SFSAMPVLANPAATAACCRYLDRDLNRSCTLTFLGSTATPDDPYEVKRARELNQLLGP
                     KGTGQAFDFTLDLHNTTANTGVCLISESNISFNLHLCHYLQRQNPGMPCRLFLYEPAG
                     TETFSVESISKNGICLEMGPQPQGVLRADLFSRMRALVASILDFIELFNQGMDLPAFE
                     MDIYRNLGSVDFPRTADGDLAGTVHPQLQDHDFEPLRPGEPIFKLFSGEDVLYEGDSI
                     VYPVFINEAAYYEKHVAFLKSEKIRVTVPALLRLTPRSTQTP"
     exon            427..619
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            620..713
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            714..821
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            822..931
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     exon            932..1286
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1268..1273
                     /regulatory_class="polyA_signal_sequence"
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /note="hexamer: AATAGA"
     polyA_site      1286
                     /gene="Acy3"
                     /gene_synonym="0610006H10Rik; AA3; AAIII; Acy-3; HCBP1"
                     /note="major polyA site"
ORIGIN      
        1 attaggcctg tggcctaggg aagcccaggc tcgtaccagc agcttaggtc ctcagagaga
       61 aaagtgggga gagcgacact caccctcaga acattccaga agagggactg aggttgcaag
      121 ggggaacaaa aatttggctg ctggtgtctt gaacttggct tctgggtaca gttcttcccc
      181 acactgggag atgtcctccc tacctgggtc ccgggagccc ctgctccgtg tggctgtgac
      241 tggaggcacc cacgggaatg agatgtgtgg tgtctacctg gcccggtact ggctacagaa
      301 cccaggggag ctgcagagac ccagcttctc agccatgccg gttctggcca acccagcagc
      361 cacagctgcc tgttgccgtt acctggaccg tgatctcaac cgctcctgca ccctcacctt
      421 ccttggttcc accgctaccc ctgatgaccc ctatgaagtg aaaagagccc gagagttgaa
      481 ccagctgctg ggtcccaagg gcacaggcca ggcttttgac tttaccctag acctgcacaa
      541 caccacagca aacactggag tctgcctcat ctctgaatcc aacatctcct tcaacttgca
      601 cctgtgccac tacctacagc ggcagaaccc ggggatgccc tgccgcctct ttctgtatga
      661 gccagctggg acggagacct tcagcgtgga atctatatcc aagaatggaa tctgtctgga
      721 gatgggccca cagcctcagg gcgtgctgcg ggccgacctg ttctcccgga tgcgagctct
      781 ggtggcatcc attctggact tcatcgagct cttcaaccaa ggcatggact tacccgcctt
      841 tgagatggat atctacagga acttgggcag tgtggacttc ccacgcactg cagatggtga
      901 cctggctggc actgtgcacc ctcaactgca ggaccatgac tttgagccac tgaggcctgg
      961 tgaacccatc ttcaagcttt tcagcggaga agacgtactg tatgaggggg actccattgt
     1021 gtaccctgtg ttcattaatg aggctgccta ttatgagaag cacgtggcat tcctgaagtc
     1081 tgagaagatc agggtcacag tgcctgccct gctgaggttg accccccgct ccacccagac
     1141 tccctaaccc aaatcatacc tggcctgatc tcagttttcc tatctgaaca atgggtccca
     1201 agcccagggt cccctatctc actctggaca ccatatccct ttccagacaa ctgatctcat
     1261 tatataaaat agactgtgcc ccaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaa
//
