ACOX3_MOUSE
ID ACOX3_MOUSE Reviewed; 700 AA.
AC Q9EPL9; Q7TPP6; Q80UQ0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3;
DE EC=1.3.3.6 {ECO:0000250|UniProtKB:Q63448};
DE AltName: Full=Branched-chain acyl-CoA oxidase;
DE Short=BRCACox;
DE AltName: Full=Pristanoyl-CoA oxidase {ECO:0000250|UniProtKB:Q63448};
GN Name=Acox3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P., Ghys K.;
RT "Cloning of the mouse pristanoyl-CoA oxidase.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids.
CC {ECO:0000250|UniProtKB:Q63448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-pristanoyl-CoA + O2 = (2E)-pristenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40459, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77099, ChEBI:CHEBI:77293;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40460;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77075, ChEBI:CHEBI:77085;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278430; CAC20692.1; -; mRNA.
DR EMBL; BC044725; AAH44725.1; -; mRNA.
DR EMBL; BC055019; AAH55019.1; -; mRNA.
DR CCDS; CCDS19232.1; -.
DR RefSeq; NP_109646.2; NM_030721.2.
DR RefSeq; XP_006504261.1; XM_006504198.3.
DR RefSeq; XP_017176670.1; XM_017321181.1.
DR AlphaFoldDB; Q9EPL9; -.
DR SMR; Q9EPL9; -.
DR STRING; 10090.ENSMUSP00000063412; -.
DR iPTMnet; Q9EPL9; -.
DR PhosphoSitePlus; Q9EPL9; -.
DR SwissPalm; Q9EPL9; -.
DR EPD; Q9EPL9; -.
DR jPOST; Q9EPL9; -.
DR MaxQB; Q9EPL9; -.
DR PaxDb; Q9EPL9; -.
DR PeptideAtlas; Q9EPL9; -.
DR PRIDE; Q9EPL9; -.
DR ProteomicsDB; 285939; -.
DR Antibodypedia; 52278; 116 antibodies from 23 providers.
DR DNASU; 80911; -.
DR Ensembl; ENSMUST00000068947; ENSMUSP00000063412; ENSMUSG00000029098.
DR Ensembl; ENSMUST00000114237; ENSMUSP00000109875; ENSMUSG00000029098.
DR GeneID; 80911; -.
DR KEGG; mmu:80911; -.
DR UCSC; uc008xdx.1; mouse.
DR CTD; 8310; -.
DR MGI; MGI:1933156; Acox3.
DR VEuPathDB; HostDB:ENSMUSG00000029098; -.
DR eggNOG; KOG0135; Eukaryota.
DR GeneTree; ENSGT00940000159423; -.
DR InParanoid; Q9EPL9; -.
DR OMA; VMPNIQI; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; Q9EPL9; -.
DR TreeFam; TF314226; -.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 80911; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Acox3; mouse.
DR PRO; PR:Q9EPL9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9EPL9; protein.
DR Bgee; ENSMUSG00000029098; Expressed in right kidney and 128 other tissues.
DR ExpressionAtlas; Q9EPL9; baseline and differential.
DR Genevisible; Q9EPL9; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0016402; F:pristanoyl-CoA oxidase activity; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:MGI.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
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; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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 FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..700
FT /note="Peroxisomal acyl-coenzyme A oxidase 3"
FT /id="PRO_0000204686"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q63448"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63448"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15254"
FT MOD_RES 505
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 177..178
FT /note="DP -> ES (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="Y -> H (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..409
FT /note="KP -> NR (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="C -> V (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="H -> Y (in Ref. 2; AAH44725)"
FT /evidence="ECO:0000305"
FT CONFLICT 593..594
FT /note="TL -> SV (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="L -> S (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="A -> R (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="A -> R (in Ref. 1; CAC20692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 78404 MW; 85C448E38A4A0C67 CRC64;
MGSLPEEKDS ALWSDTPKGP LSAYRARASF NSGELLLFWD GQDVIHFKKT IFSTLENDPL
FARSYGADLP LEKLRELNFL RCKRVFEYGF FKVEELLKNP LKILVLINCL GMYDWSLANK
CVLHMLVFGT TVFVSGSEKH FKYLEKIYSL EIFGCFALTE LSHGSNTKAM RTTAHYDPDT
QEFILHSPDF EAAKFWVGNL GKTATHAVVF AQLYMPDGQC HGLHSFLVQI RDTKTLLPMT
GVMVGDIGKK LGQNGLDNGF AMFNKVRIPR QNLLDRTGNI TSEGTYNSPF KDVRQRLGAS
LGSLSSGRIS IISMSVVNLK LAVSIAIRFS ATRCQFGPTD KEEIPVLEYP LQQWRILPYL
AAAYALDHFS KTIFMDLIEV QSARLRGDHS DQQAELGREI HALASAGKPL ASWTAQRGIQ
ECREACGGHG YLAMNRFGDL RNDNDPNCTY EGDNNVLLQQ TSNYLLSLLE PPLQDGAHFT
SPLKTVDFLE AYPGILGQKF LGSSKADWMD SAAPLAAYRW LVCYLLQESH RRYCQEKKSR
GSDFEARNNS QVYGCRPLAL AFMELTVMQR FHEHIHSSGL SPSLRTVLGR LSTLYGLWCL
SQHMALLYRG GYISGEQTGR AMEDAILTLC EQLKDDAVAL VDVIAPSDFV LNSPIAKADG
ELYKNLWAAV LQQNGVLERA AWWPEFSANK SVADRLKSQL
