LOCUS       NP_076106               1335 aa            linear   ROD 02-JUN-2024
DEFINITION  aldehyde oxidase 3 [Mus musculus].
ACCESSION   NP_076106
VERSION     NP_076106.2
DBSOURCE    REFSEQ: accession NM_023617.2
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  (residues 1 to 1335)
  AUTHORS   Jing,J., Feng,J., Yuan,Y., Guo,T., Lei,J., Pei,F., Ho,T.V. and
            Chai,Y.
  TITLE     Spatiotemporal single-cell regulatory atlas reveals neural crest
            lineage diversification and cellular function during tooth
            morphogenesis
  JOURNAL   Nat Commun 13 (1), 4803 (2022)
   PUBMED   35974052
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1335)
  AUTHORS   Cerqueira,N.M., Coelho,C., Bras,N.F., Fernandes,P.A., Garattini,E.,
            Terao,M., Romao,M.J. and Ramos,M.J.
  TITLE     Insights into the structural determinants of substrate specificity
            and activity in mouse aldehyde oxidases
  JOURNAL   J Biol Inorg Chem 20 (2), 209-217 (2015)
   PUBMED   25287365
  REMARK    GeneRIF: Although mAOX2 and mAOX3 are very similar to each other,
            we propose the following pairs of overlapping substrate
            specificities: mAOX2/mAOX4 and mAOX3/mAXO1.
REFERENCE   3  (residues 1 to 1335)
  AUTHORS   Mahro,M., Bras,N.F., Cerqueira,N.M., Teutloff,C., Coelho,C.,
            Romao,M.J. and Leimkuhler,S.
  TITLE     Identification of crucial amino acids in mouse aldehyde oxidase 3
            that determine substrate specificity
  JOURNAL   PLoS One 8 (12), e82285 (2013)
   PUBMED   24358164
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1335)
  AUTHORS   Kurosaki,M., Bolis,M., Fratelli,M., Barzago,M.M., Pattini,L.,
            Perretta,G., Terao,M. and Garattini,E.
  TITLE     Structure and evolution of vertebrate aldehyde oxidases: from gene
            duplication to gene suppression
  JOURNAL   Cell Mol Life Sci 70 (10), 1807-1830 (2013)
   PUBMED   23263164
REFERENCE   5  (residues 1 to 1335)
  AUTHORS   Coelho,C., Mahro,M., Trincao,J., Carvalho,A.T., Ramos,M.J.,
            Terao,M., Garattini,E., Leimkuhler,S. and Romao,M.J.
  TITLE     The first mammalian aldehyde oxidase crystal structure: insights
            into substrate specificity
  JOURNAL   J Biol Chem 287 (48), 40690-40702 (2012)
   PUBMED   23019336
  REMARK    GeneRIF: AOX3 forms a homodimer and each monomer comprises three
            major domains involved in binding to the cofactors.
REFERENCE   6  (residues 1 to 1335)
  AUTHORS   Reynolds,S.D., Zemke,A.C., Giangreco,A., Brockway,B.L.,
            Teisanu,R.M., Drake,J.A., Mariani,T., Di,P.Y., Taketo,M.M. and
            Stripp,B.R.
  TITLE     Conditional stabilization of beta-catenin expands the pool of lung
            stem cells
  JOURNAL   Stem Cells 26 (5), 1337-1346 (2008)
   PUBMED   18356571
REFERENCE   7  (residues 1 to 1335)
  AUTHORS   Kurosaki,M., Terao,M., Barzago,M.M., Bastone,A., Bernardinello,D.,
            Salmona,M. and Garattini,E.
  TITLE     The aldehyde oxidase gene cluster in mice and rats. Aldehyde
            oxidase homologue 3, a novel member of the molybdo-flavoenzyme
            family with selective expression in the olfactory mucosa
  JOURNAL   J Biol Chem 279 (48), 50482-50498 (2004)
   PUBMED   15383531
REFERENCE   8  (residues 1 to 1335)
  AUTHORS   Vila,R., Kurosaki,M., Barzago,M.M., Kolek,M., Bastone,A.,
            Colombo,L., Salmona,M., Terao,M. and Garattini,E.
  TITLE     Regulation and biochemistry of mouse molybdo-flavoenzymes. The
            DBA/2 mouse is selectively deficient in the expression of aldehyde
            oxidase homologues 1 and 2 and represents a unique source for the
            purification and characterization of aldehyde oxidase
  JOURNAL   J Biol Chem 279 (10), 8668-8683 (2004)
   PUBMED   14665639
REFERENCE   9  (residues 1 to 1335)
  AUTHORS   Terao,M., Kurosaki,M., Marini,M., Vanoni,M.A., Saltini,G.,
            Bonetto,V., Bastone,A., Federico,C., Saccone,S., Fanelli,R.,
            Salmona,M. and Garattini,E.
  TITLE     Purification of the aldehyde oxidase homolog 1 (AOH1) protein and
            cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes.
            Identification of a novel molybdo-flavoprotein gene cluster on
            mouse chromosome 1
  JOURNAL   J Biol Chem 276 (49), 46347-46363 (2001)
   PUBMED   11562361
REFERENCE   10 (residues 1 to 1335)
  AUTHORS   Terao,M., Kurosaki,M., Saltini,G., Demontis,S., Marini,M.,
            Salmona,M. and Garattini,E.
  TITLE     Cloning of the cDNAs coding for two novel molybdo-flavoproteins
            showing high similarity with aldehyde oxidase and xanthine
            oxidoreductase
  JOURNAL   J Biol Chem 275 (39), 30690-30700 (2000)
   PUBMED   10893244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025116.14, AK054065.1, BX633666.1, BB616838.1, AK004700.1 and
            AV275739.1.
            
            On Sep 8, 2006 this sequence version replaced NP_076106.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF172276.2, AK149434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849382, SAMN00849384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1335
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 28.96 cM"
     Protein         1..1335
                     /product="aldehyde oxidase 3"
                     /EC_number="1.2.3.1"
                     /note="aldehyde oxidase 1; aldehyde oxidase structural
                     homolog 2; aldehyde oxidase homolog 1; azaheterocycle
                     hydroxylase 3"
                     /calculated_mol_wt=146772
     Region          9..1334
                     /region_name="mam_aldehyde_ox"
                     /note="aldehyde oxidase; TIGR02969"
                     /db_xref="CDD:132014"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5QE80; propagated from
                     UniProtKB/Swiss-Prot (G3X982.1)"
     CDS             1..1335
                     /gene="Aox3"
                     /gene_synonym="1200011D03Rik; Aoh1; Aoh2"
                     /coded_by="NM_023617.2:124..4131"
                     /db_xref="CCDS:CCDS14969.1"
                     /db_xref="GeneID:71724"
                     /db_xref="MGI:MGI:1918974"
ORIGIN      
        1 mspskesdel iffvngkkvt ernadpevnl lfylrkvirl tgtkygcggg dcgactvmis
       61 rydpiskris hfsataclvp icslhgaavt tvegigstkt rihpvqeria kghgtqcgfc
      121 tpgmvmsiyt llrnhpepst eqimetlggn lcrctgyrpi vesaksfcps stccqmngeg
      181 kccldeekne perknsvctk lyekkefqpl dptqelifpp elmrmaeesq ntvltfrger
      241 ttwiapgtln dllelkmkhp saplvignty lglhmkftdv sypiiispar ilelfvvtnt
      301 kqgltlgagl sltqvknvls dvvsrlpkek tqiycallkq lktlagqqir nvaslgghii
      361 srlptsdlnp ilgignciln vastegiqqi plndhflagv pdailkpeqv lisvfvprss
      421 kwefvsafrq aprqqnafat vnagmkvvfk edtntitdlg ilyggigatv isadkscrql
      481 igrcwdeeml ddagkmicee vsllmaapgg meeyrktlai sflfmfyldv lkqlktrdph
      541 kypdisqkll hiledfpltm pygmqsfqdv dfqqplqdpi grpimhqsgi khatgeavfc
      601 ddmsvlpgel flavvtssks hakiisldas ealaslgvvd vvtardvpgd ngreeeslya
      661 qdevicvgqi vcavaadsya haqqaakkvk ivyqdiepmi vtvqdalqye sfigperkle
      721 qgnveeafqc adqilegevh lggqehfyme tqsvrvvpkg edkemdiyvs sqdaaftqem
      781 vartlgipkn rinchvkrvg gafggkaskp gllasvaava aqktgrpirf ilerrddmli
      841 tggrhpllgk ykigfmnngk ikaadiqlyi nggctpddse lvieyallkl enaykipnlr
      901 vrgrvcktnl psntafrgfg fpqgafvtet cmsavaakcr lppekvreln myrtidrtih
      961 nqefdptnll qcweacvens syynrkkavd efnqqrfwkk rgiaiipmkf svgfpktfyy
     1021 qaaalvqiyt dgsvlvahgg velgqgintk miqvasrelk ipmsyihlde mstvtvpntv
     1081 ttgastgadv ngravqnacq ilmkrlepii kqnpsgtwee wvkeafvqsi slsatgyfrg
     1141 yqadmdwekg egdifpyfvf gaacseveid cltgahknir tdivmdgsfs inpavdigqi
     1201 egafvqglgl ytleelkysp egvlytrgph qykiasvtdi peefhvsllt ptpnpkaiys
     1261 skglgeagtf lgcsvffaia aavaaareer glspiwains pataevirma cedqftnlvp
     1321 qtdskcckpw sipva
//
