LOCUS       NP_665713                681 aa            linear   ROD 03-APR-2024
DEFINITION  peroxisomal acyl-coenzyme A oxidase 2 [Rattus norvegicus].
ACCESSION   NP_665713
VERSION     NP_665713.2
DBSOURCE    REFSEQ: accession NM_145770.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Monte,M.J., Alonso-Pena,M., Briz,O., Herraez,E., Berasain,C.,
            Argemi,J., Prieto,J. and Marin,J.J.G.
  TITLE     ACOX2 deficiency: An inborn error of bile acid synthesis identified
            in an adolescent with persistent hypertransaminasemia
  JOURNAL   J Hepatol 66 (3), 581-588 (2017)
   PUBMED   27884763
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Tokuoka,K., Nakajima,Y., Hirotsu,K., Miyahara,I., Nishina,Y.,
            Shiga,K., Tamaoki,H., Setoyama,C., Tojo,H. and Miura,R.
  TITLE     Three-dimensional structure of rat-liver acyl-CoA oxidase in
            complex with a fatty acid: insights into substrate-recognition and
            reactivity toward molecular oxygen
  JOURNAL   J Biochem 139 (4), 789-795 (2006)
   PUBMED   16672280
  REMARK    GeneRIF: The overall dimeric structure and the folding pattern of
            each subunit are essentially superimposable on those of uncomplexed
            acyl-CoA oxidase-II structure.
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Baumgart,E., Vanhooren,J.C., Fransen,M., Marynen,P., Puype,M.,
            Vandekerckhove,J., Leunissen,J.A., Fahimi,H.D., Mannaerts,G.P. and
            van Veldhoven,P.P.
  TITLE     Molecular characterization of the human peroxisomal branched-chain
            acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue
            distribution, and evidence for the absence of the protein in
            Zellweger syndrome
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 13748-13753 (1996)
   PUBMED   8943006
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Baumgart,E., Vanhooren,J.C., Fransen,M., Van Leuven,F.,
            Fahimi,H.D., Van Veldhoven,P.P. and Mannaerts,G.P.
  TITLE     Molecular cloning and further characterization of rat peroxisomal
            trihydroxycoprostanoyl-CoA oxidase
  JOURNAL   Biochem J 320 (Pt 1) (Pt 1), 115-121 (1996)
   PUBMED   8947475
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Van Veldhoven,P.P., Croes,K., Asselberghs,S., Herdewijn,P. and
            Mannaerts,G.P.
  TITLE     Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters:
            stereospecific recognition of the 2S-methyl compounds by
            trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase
  JOURNAL   FEBS Lett 388 (1), 80-84 (1996)
   PUBMED   8654595
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Van Veldhoven,P.P., Vanhove,G., Assselberghs,S., Eyssen,H.J. and
            Mannaerts,G.P.
  TITLE     Substrate specificities of rat liver peroxisomal acyl-CoA oxidases:
            palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA
            oxidase (non-inducible acyl-CoA oxidase), and
            trihydroxycoprostanoyl-CoA oxidase
  JOURNAL   J Biol Chem 267 (28), 20065-20074 (1992)
   PUBMED   1400324
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Casteels,M., Schepers,L., Van Veldhoven,P.P., Eyssen,H.J. and
            Mannaerts,G.P.
  TITLE     Separate peroxisomal oxidases for fatty acyl-CoAs and
            trihydroxycoprostanoyl-CoA in human liver
  JOURNAL   J Lipid Res 31 (10), 1865-1872 (1990)
   PUBMED   2079609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Sep 13, 2012 this sequence version replaced NP_665713.1.
            
            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 :: X95189.1, SRR26643286.39670.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [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..681
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..681
                     /product="peroxisomal acyl-coenzyme A oxidase 2"
                     /EC_number="1.17.99.3"
                     /note="acyl-Coenzyme A oxidase 2, branched chain; THCA-CoA
                     oxidase; trihydroxycoprostanoyl-CoA oxidase;
                     3-alpha,7-alpha,
                     12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase;
                     acyl-CoA oxidase 2, branched chain;
                     3-alpha,7-alpha,
                     12-alpha-trihydroxy-5-beta-cholestanoyl-CoA
                     24-hydroxylase"
                     /calculated_mol_wt=76616
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499; propagated from
                     UniProtKB/Swiss-Prot (P97562.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99424; propagated from
                     UniProtKB/Swiss-Prot (P97562.1)"
     Region          20..655
                     /region_name="AXO"
                     /note="Peroxisomal acyl-CoA oxidase; cd01150"
                     /db_xref="CDD:173839"
     Site            order(73..74,78,82,156..161,163,190..191,197..198,225,
                     239..244,246..247,323,325,334,339..341,346,406,409,
                     414..415,417,419,427..428,431,441,529,533..534,536..537,
                     646,652..653)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:173839"
     Site            order(121,151..154,191..193,247,296,301,417,436..437)
                     /site_type="active"
                     /db_xref="CDD:173839"
     Site            437
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:173839"
     Site            453
                     /site_type="active"
                     /note="end of homology with other ACAD's [active]"
                     /db_xref="CDD:173839"
     Region          679..681
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97562.1)"
     CDS             1..681
                     /gene="Acox2"
                     /gene_synonym="THCCox"
                     /coded_by="NM_145770.4:199..2244"
                     /db_xref="GeneID:252898"
                     /db_xref="RGD:628684"
ORIGIN      
        1 mgspmhrvsl gdtwswqvhp didserhsps fsverltnil dgglpntvlr rkvesiiqsd
       61 pvfnlkklyf mtreelyeda iqkrfhlekl awslgwsedg periyanrvl dgnvnlslhg
      121 vamnairslg sdeqiakwgq lcknfqiitt yaqtelghgt ylqgleteat ydearqefvi
      181 hsptmtstkw wpgdlgwsvt havvlaqltc lgvrhgmhaf ivpirsledh tplpgitvgd
      241 igpkmglehi dngflqlnhv rvprenmlsr faevlpdgty qrlgtpqsny lgmlvtrvql
      301 lckgilpslq kaciiatrys virhqsrlrp sdpeakiley qtqqqkllpq lavsyafhft
      361 atslseffhs sysailkrdf sllpelhals tgmkatfadf caqgaeicrr acgghgyskl
      421 sglptlvara tasctyegen tvlylqvarf lmksylqaqa spgatpqkpl pqsvmyiatq
      481 rparcsaqta adfrcpdvyt tawayvstrl irdaahrtqt lmksgvdqhd awnqttvihl
      541 qaakaycyfi tvknfkeave kldkepeiqr vlqrlcdlya lhgvltnsgd flhdgflsga
      601 qvdmareafl dllplirkda illtdafdfs dhclnsalgc ydghvyerlf ewaqkspant
      661 qenpaykkyi rplmlgwrhk m
//
