ACOX2_RABIT
ID ACOX2_RABIT Reviewed; 681 AA.
AC O02767;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 2 {ECO:0000250|UniProtKB:Q99424};
DE EC=1.17.99.3 {ECO:0000269|PubMed:9218493};
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase;
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase {ECO:0000303|PubMed:9218493};
DE AltName: Full=Trihydroxycoprostanoyl-CoA oxidase {ECO:0000250|UniProtKB:P97562};
DE Short=THCA-CoA oxidase {ECO:0000303|PubMed:9218493};
DE Short=THCCox;
GN Name=ACOX2 {ECO:0000250|UniProtKB:Q99424};
GN Synonyms=THCA {ECO:0000312|EMBL:CAA73728.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=9218493; DOI=10.1074/jbc.272.29.18481;
RA Pedersen J.J., Eggertsen G., Hellman U., Andersson U., Bjoerkhem I.;
RT "Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-
RT trihydroxy-5beta-cholestanoyl-CoA oxidase from rabbit liver.";
RL J. Biol. Chem. 272:18481-18489(1997).
CC -!- FUNCTION: Oxidizes the CoA esters of the bile acid intermediates
CC di- and tri-hydroxycholestanoic acids (PubMed:9218493). Capable of
CC oxidizing short as well as long chain 2-methyl branched fatty acids (By
CC similarity). {ECO:0000250|UniProtKB:P07872,
CC ECO:0000269|PubMed:9218493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA + A + H2O = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-
CC 5beta-cholestan-26-oyl-CoA + AH2; Xref=Rhea:RHEA:15733,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58677, ChEBI:CHEBI:59807; EC=1.17.99.3;
CC Evidence={ECO:0000269|PubMed:9218493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15734;
CC Evidence={ECO:0000305|PubMed:9218493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-
CC CoA + O2 = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-
CC en-26-oyl-CoA + H2O2; Xref=Rhea:RHEA:46728, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:59879, ChEBI:CHEBI:77251;
CC Evidence={ECO:0000269|PubMed:9218493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46729;
CC Evidence={ECO:0000305|PubMed:9218493};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07872}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q99424}.
CC -!- TISSUE SPECIFICITY: Liver and kidney. {ECO:0000269|PubMed:9218493}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; Y13279; CAA73728.1; -; mRNA.
DR RefSeq; NP_001076232.1; NM_001082763.1.
DR AlphaFoldDB; O02767; -.
DR SMR; O02767; -.
DR STRING; 9986.ENSOCUP00000003596; -.
DR SwissLipids; SLP:000001293; -.
DR GeneID; 100009549; -.
DR KEGG; ocu:100009549; -.
DR CTD; 8309; -.
DR eggNOG; KOG0136; Eukaryota.
DR InParanoid; O02767; -.
DR OrthoDB; 416859at2759; -.
DR BRENDA; 1.17.99.3; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
DR GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Fatty acid metabolism; Flavoprotein;
KW Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..681
FT /note="Peroxisomal acyl-coenzyme A oxidase 2"
FT /id="PRO_0000204683"
FT MOTIF 679..681
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99424"
FT MOD_RES 66
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 137
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 453
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 561
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
FT MOD_RES 667
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXD1"
SQ SEQUENCE 681 AA; 76199 MW; 7BF3550F353FB2E3 CRC64;
MGIPVHRVSL GDAWSSRMHP DMESERCAQS FSVERLTNIL DGGAQHTALR RKVESIIHGN
PQFSSKDNYF MSQNELYEAA TRKRYHLQKI AQRMGWTEEG RELEYAHRAL SADLNLNLQG
IFLKALRSLG SEEQIAKWEP LGKTFQIIST YAQTELGHGT YLQGLETEAT YDAATQEFVI
HSPTVTATKW WPGDLGRSAT HALILAQLIC SGARRGMHAF IVPVRSLQDH TPLPGITIGD
IGPKMGLQHI DNGFLKMDHV RVPRENMLSR FAQVLPDGAY IKLGTAQSNY LGMLVTRVHL
LLGAILSPLQ KACVIATRYS VIRHQCRLRP SDPEVKILEH QTQQQKLFPQ LAMCYAFHFL
ATGLLEFFQQ AYKNILDRDF TLLPELHALS TGTKAMMSDF CTQGAEQCRR ACGGHGYSKL
SGLPSLVTSV TASCTYEGEN TVLYLQVARF LVKSCLQAQG FPGSTSQRSL PRSVSYLALP
DLARCPAQTA ADFFCPALYT AAWAHVAARL TKDSVHHLQA LRQSGADEHE AWNQTTIIHL
QAAKAHCYYI SVKSFKEALE KLENEPAIQQ VLKRLCDLHA LHGILTNSGD FLHDGFLSGA
QVDMARTAYM DLLPLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF EWAQRSPTNT
QENPAYKKYI QPLLQSWRSN L
