ACOX2_RAT
ID ACOX2_RAT Reviewed; 681 AA.
AC P97562;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 2 {ECO:0000250|UniProtKB:Q99424};
DE EC=1.17.99.3 {ECO:0000269|PubMed:1400324, ECO:0000269|PubMed:8947475};
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:0000250|UniProtKB:O02767};
DE AltName: Full=Trihydroxycoprostanoyl-CoA oxidase {ECO:0000303|PubMed:1400324, ECO:0000303|PubMed:8947475};
DE Short=THCA-CoA oxidase {ECO:0000250|UniProtKB:O02767};
DE Short=THCCox;
GN Name=Acox2 {ECO:0000312|RGD:628684};
GN Synonyms=Thcox {ECO:0000312|EMBL:CAA64488.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-33; 74-83; 128-137;
RP 265-270; 328-336; 454-464 AND 656-667, FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8947475; DOI=10.1042/bj3200115;
RA Baumgart E., Vanhooren J.C.T., Fransen M., Van Leuven F., Fahimi H.D.,
RA Van Veldhoven P.P., Mannaerts G.P.;
RT "Molecular cloning and further characterization of rat peroxisomal
RT trihydroxycoprostanoyl-CoA oxidase.";
RL Biochem. J. 320:115-121(1996).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1400324; DOI=10.1016/s0021-9258(19)88666-0;
RA Van Veldhoven P.P., Vanhove G., Assselberghs S., Eyssen H.J.,
RA Mannaerts G.P.;
RT "Substrate specificities of rat liver peroxisomal acyl-CoA oxidases:
RT palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase
RT (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase.";
RL J. Biol. Chem. 267:20065-20074(1992).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
CC -!- FUNCTION: Oxidizes the CoA esters of the bile acid intermediates
CC di- and tri-hydroxycoprostanic acids (PubMed:8947475, PubMed:1400324).
CC Capable of oxidizing short as well as long chain 2-methyl branched
CC fatty acids (PubMed:1400324). {ECO:0000269|PubMed:1400324,
CC ECO:0000269|PubMed:8947475}.
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:1400324, ECO:0000269|PubMed:8947475};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15734;
CC Evidence={ECO:0000305|PubMed:1400324, ECO:0000305|PubMed:8947475};
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:0000250|UniProtKB:O02767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46729;
CC Evidence={ECO:0000250|UniProtKB:O02767};
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:0000269|PubMed:8947475}.
CC -!- TISSUE SPECIFICITY: Most abundant in liver. Also expressed in kidney.
CC Not present in any other tissues tested. {ECO:0000269|PubMed:8947475}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; X95189; CAA64488.1; -; mRNA.
DR AlphaFoldDB; P97562; -.
DR SMR; P97562; -.
DR STRING; 10116.ENSRNOP00000010260; -.
DR CarbonylDB; P97562; -.
DR iPTMnet; P97562; -.
DR PhosphoSitePlus; P97562; -.
DR PaxDb; P97562; -.
DR PRIDE; P97562; -.
DR RGD; 628684; Acox2.
DR eggNOG; KOG0136; Eukaryota.
DR InParanoid; P97562; -.
DR PhylomeDB; P97562; -.
DR BioCyc; MetaCyc:MON-14328; -.
DR BRENDA; 1.17.99.3; 5301.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR PRO; PR:P97562; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IDA:RGD.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:RGD.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEP:RGD.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
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 GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
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_0000204684"
FT MOTIF 679..681
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499"
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 303
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; 76799 MW; 3599D71365D38932 CRC64;
MGSPMHRVSL GDHWSWQVHP DIDSERHSPS FSVERLTNIL DGGLPNTVLR RKVESIIQSD
PVFNLKKLYF MTREELYEDA IQKRFHLEKL AWSLGWSEDG PERIYANRVL DGNVNLSLHG
VAMNAIRSLG SDEQIAKWGQ LCKNFQIITT YAQTELGHGT YLQGLETEAT YDEARQELVI
HSPTMTSTKW WPGDLGWSVT HAVVLAQLTC LGVRHGMHAF IVPIRSLEDH TPLPGITVGD
IGPKMGLEHI DNGFLQLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL
LCKGILPSLQ KACIIATRYS VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ LAVSYAFHFT
ATSLSEFFHS SYSAILKRDF SLLPELHALS TGMKATFADF CAQGAEICRR ACGGHGYSKL
SGLPTLVARA TASCTYEGEN TVLYLQVARF LMKSYLQAQA SPGATPQKPL PQSVMYIATQ
RPARCSAQTA ADFRCPDVYT TAWAYVSTRL IRDAAHRTQT LMKSGVDQHD AWNQTTVIHL
QAAKAHCYFI TVKNFKEAVE KLDKEPEIQR VLQRLCDLYA LHGVLTNSGD FLHDGFLSGA
QVDMAREAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYERLF EWAQKYPANT
QENPAYKKYI RPLMLGWRHK M
