ID Q3TAW3_MOUSE Unreviewed; 673 AA.
AC Q3TAW3;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=Acox3 {ECO:0000313|Ensembl:ENSMUSP00000144499.2,
GN ECO:0000313|MGI:MGI:1933156};
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 {ECO:0000313|EMBL:BAE42553.1};
RN [1] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAE42553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42553.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [9] {ECO:0000313|Ensembl:ENSMUSP00000144499.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144499.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [10] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [12] {ECO:0000313|Ensembl:ENSMUSP00000144499.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144499.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036229};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000256|ARBA:ARBA00036229};
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:0000256|ARBA:ARBA00036397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000256|ARBA:ARBA00036397};
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:0000256|ARBA:ARBA00036704};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000256|ARBA:ARBA00036704};
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:0000256|ARBA:ARBA00036893};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000256|ARBA:ARBA00036893};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR EMBL; AK171598; BAE42553.1; -; mRNA.
DR RefSeq; XP_006504262.1; XM_006504199.3.
DR ProteomicsDB; 334716; -.
DR Antibodypedia; 52278; 128 antibodies from 23 providers.
DR DNASU; 80911; -.
DR Ensembl; ENSMUST00000202266.4; ENSMUSP00000144499.2; ENSMUSG00000029098.18.
DR GeneID; 80911; -.
DR AGR; MGI:1933156; -.
DR CTD; 8310; -.
DR MGI; MGI:1933156; Acox3.
DR VEuPathDB; HostDB:ENSMUSG00000029098; -.
DR GeneTree; ENSGT00940000159423; -.
DR HOGENOM; CLU_014629_4_2_1; -.
DR OrthoDB; 5777at2759; -.
DR BioGRID-ORCS; 80911; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Acox3; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000029098; Expressed in right kidney and 131 other cell types or tissues.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:InterPro.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 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; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 1: Evidence at protein level;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|EPD:Q3TAW3,
KW ECO:0007829|MaxQB:Q3TAW3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 155..265
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 301..460
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 512..662
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 673 AA; 75360 MW; CA21289EC9DE23E2 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
EVLSTQEKLE KRK
//
