ACOX1_MOUSE
ID ACOX1_MOUSE Reviewed; 661 AA.
AC Q9R0H0; A2A850; O35616; Q3TDG0; Q8BYC3;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1;
DE Short=AOX;
DE EC=1.3.3.6 {ECO:0000305|PubMed:11855929, ECO:0000305|PubMed:20195242};
DE AltName: Full=Palmitoyl-CoA oxidase {ECO:0000250|UniProtKB:Q15067};
DE AltName: Full=Peroxisomal fatty acyl-CoA oxidase;
DE AltName: Full=Straight-chain acyl-CoA oxidase;
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, A chain {ECO:0000250|UniProtKB:P07872};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, B chain {ECO:0000250|UniProtKB:P07872};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, C chain {ECO:0000250|UniProtKB:P07872};
GN Name=Acox1 {ECO:0000312|MGI:MGI:1330812}; Synonyms=Acox, Paox;
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] (ISOFORM 1).
RX PubMed=10672038; DOI=10.1046/j.1432-1327.2000.01128.x;
RA Nohammer C., El-Shabrawi Y., Schauer S., Hiden M., Berger J.,
RA Forss-Petter S., Winter E., Eferl R., Zechner R., Hoefler G.;
RT "cDNA cloning and analysis of tissue-specific expression of mouse
RT peroxisomal straight-chain acyl-CoA oxidase.";
RL Eur. J. Biochem. 267:1254-1260(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Saibara T., Adachi K.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=11855929; DOI=10.1006/mgme.2001.3279;
RA Infante J.P., Tschanz C.L., Shaw N., Michaud A.L., Lawrence P.,
RA Brenna J.T.;
RT "Straight-chain acyl-CoA oxidase knockout mouse accumulates extremely long
RT chain fatty acids from alpha-linolenic acid: evidence for runaway carousel-
RT type enzyme kinetics in peroxisomal beta-oxidation diseases.";
RL Mol. Genet. Metab. 75:108-119(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [10]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, FUNCTION, AND
RP PATHWAY.
RX PubMed=20195242; DOI=10.1038/labinvest.2010.46;
RA Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K., Kulik W.,
RA Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I., Rao M.S.,
RA Wanders R.J., Reddy J.K., Cherkaoui-Malki M.;
RT "Reversal of mouse Acyl-CoA oxidase 1 (ACOX1) null phenotype by human
RT ACOX1b isoform.";
RL Lab. Invest. 90:696-708(2010).
RN [11]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-90; LYS-159; LYS-241;
RP LYS-349; LYS-437; LYS-446; LYS-512; LYS-542; LYS-637; LYS-643 AND LYS-655,
RP AND IDENTIFICATION BY MASS 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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-216; LYS-267; LYS-272;
RP LYS-437; LYS-446; LYS-512; LYS-637 AND LYS-652, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Involved in the initial and rate-limiting step of peroxisomal
CC beta-oxidation of straight-chain saturated and unsaturated very-long-
CC chain fatty acids. Catalyzes the desaturation of fatty acyl-CoAs such
CC as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-
CC CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to
CC molecular oxygen (O(2)), thereby producing hydrogen peroxide
CC (H(2)O(2)). {ECO:0000305|PubMed:11855929, ECO:0000305|PubMed:20195242}.
CC -!- FUNCTION: [Isoform 1]: Shows highest activity against medium-chain
CC fatty acyl-CoAs. Shows optimum activity with a chain length of 10
CC carbons (decanoyl-CoA) in vitro. {ECO:0000250|UniProtKB:Q15067}.
CC -!- FUNCTION: [Isoform 2]: Is active against a much broader range of
CC substrates and shows activity towards long-chain acyl-CoAs.
CC {ECO:0000250|UniProtKB:Q15067}.
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:0000305|PubMed:11855929, ECO:0000305|PubMed:20195242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:11855929, ECO:0000305|PubMed:20195242};
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:0000305|PubMed:20195242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:20195242};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57330, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + octanoyl-CoA = (2E)-octenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40175, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40179, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:61405;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57353, ChEBI:CHEBI:57378;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38971, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + O2 =
CC (2E,5Z,8Z,11Z,14Z,17Z)-icosahexaenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:69643, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:73862, ChEBI:CHEBI:187901;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + O2 =
CC (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:39119, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:74086, ChEBI:CHEBI:76360;
CC Evidence={ECO:0000305|PubMed:11855929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39120;
CC Evidence={ECO:0000305|PubMed:11855929};
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 {ECO:0000269|PubMed:11855929, ECO:0000269|PubMed:20195242}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with LONP2 (By
CC similarity). {ECO:0000250|UniProtKB:P07872,
CC ECO:0000250|UniProtKB:Q15067}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P07872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R0H0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0H0-2; Sequence=VSP_042477;
CC -!- TISSUE SPECIFICITY: Highest levels of isoform 1 are found in liver and
CC kidney while highest levels of isoform 2 are found in white adipose
CC tissue. Isoform 1 is expressed at higher levels than isoform 2 in liver
CC and kidney while isoform 2 is expressed at higher levels in brain,
CC heart, lung, muscle, white adipose tissue and testis.
CC {ECO:0000269|PubMed:20195242}.
CC -!- DISRUPTION PHENOTYPE: Severe microvesicular hepatic steatosis,
CC sustained activation of Ppara, spontaneous massive peroxisome
CC proliferation and eventual development of hepatocellular carcinomas
CC (PubMed:20195242). Null mice have strikingly increased levels of both
CC n-3 and n-6 very long chain polyunsaturated fatty acids (over twenty-
CC four (24) carbons long) (PubMed:11855929).
CC {ECO:0000269|PubMed:11855929, ECO:0000269|PubMed:20195242}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE41642.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF006688; AAB62926.1; -; mRNA.
DR EMBL; AB034914; BAA86870.1; -; mRNA.
DR EMBL; AK040566; BAC30628.1; -; mRNA.
DR EMBL; AK170217; BAE41642.1; ALT_INIT; mRNA.
DR EMBL; AL607108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34562.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34563.1; -; Genomic_DNA.
DR EMBL; BC056448; AAH56448.1; -; mRNA.
DR CCDS; CCDS25660.1; -. [Q9R0H0-2]
DR CCDS; CCDS70354.1; -. [Q9R0H0-1]
DR RefSeq; NP_001258827.1; NM_001271898.1. [Q9R0H0-1]
DR RefSeq; NP_056544.2; NM_015729.3. [Q9R0H0-2]
DR AlphaFoldDB; Q9R0H0; -.
DR SMR; Q9R0H0; -.
DR BioGRID; 197926; 21.
DR STRING; 10090.ENSMUSP00000063325; -.
DR iPTMnet; Q9R0H0; -.
DR PhosphoSitePlus; Q9R0H0; -.
DR SwissPalm; Q9R0H0; -.
DR EPD; Q9R0H0; -.
DR jPOST; Q9R0H0; -.
DR MaxQB; Q9R0H0; -.
DR PaxDb; Q9R0H0; -.
DR PeptideAtlas; Q9R0H0; -.
DR PRIDE; Q9R0H0; -.
DR ProteomicsDB; 285937; -. [Q9R0H0-1]
DR ProteomicsDB; 285938; -. [Q9R0H0-2]
DR Antibodypedia; 19646; 393 antibodies from 31 providers.
DR DNASU; 11430; -.
DR Ensembl; ENSMUST00000066587; ENSMUSP00000063325; ENSMUSG00000020777. [Q9R0H0-2]
DR Ensembl; ENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777. [Q9R0H0-1]
DR GeneID; 11430; -.
DR KEGG; mmu:11430; -.
DR UCSC; uc007mkj.2; mouse. [Q9R0H0-1]
DR UCSC; uc007mkl.2; mouse. [Q9R0H0-2]
DR CTD; 51; -.
DR MGI; MGI:1330812; Acox1.
DR VEuPathDB; HostDB:ENSMUSG00000020777; -.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000157287; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q9R0H0; -.
DR OMA; GRRFFTM; -.
DR OrthoDB; 416859at2759; -.
DR TreeFam; TF300672; -.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 11430; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Acox1; mouse.
DR PRO; PR:Q9R0H0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9R0H0; protein.
DR Bgee; ENSMUSG00000020777; Expressed in left lobe of liver and 276 other tissues.
DR ExpressionAtlas; Q9R0H0; baseline and differential.
DR Genevisible; Q9R0H0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; ISO:MGI.
DR GO; GO:0071949; F:FAD binding; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; 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:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; IMP:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:MGI.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR GO; GO:0016559; P:peroxisome fission; ISO:MGI.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0140493; P:very long-chain fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
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 Acetylation; Alternative splicing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..661
FT /note="Peroxisomal acyl-CoA oxidase 1, A chain"
FT /id="PRO_0000204678"
FT CHAIN 1..438
FT /note="Peroxisomal acyl-CoA oxidase 1, B chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447502"
FT CHAIN 439..661
FT /note="Peroxisomal acyl-CoA oxidase 1, C chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447503"
FT MOTIF 659..661
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT SITE 468..469
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 89
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 241
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 349
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 437
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 446
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 446
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 512
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 512
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 542
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 637
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 637
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 643
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 652
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 655
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 90..133
FT /note="KLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQII -> NSVH
FT RGHPEPLDLHLGMFLPTLLHQATEEQQERFFMPAWNLEIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042477"
FT CONFLICT 22
FT /note="I -> V (in Ref. 1; AAB62926)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="G -> D (in Ref. 3; BAE41642)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="W -> R (in Ref. 3; BAE41642)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="L -> I (in Ref. 3; BAE41642)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="E -> Q (in Ref. 1; AAB62926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 74649 MW; 4140DB77A4CE7BE6 CRC64;
MNPDLRKERA AATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY
EVAVKKSATM VKKMREFGIA DPEEIMWFKK LHMVNFVEPV GLNYSMFIPT LLNQGTTAQQ
EKWMHPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL
GKTSNHAIVL AQLITRGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL
KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGSAA QSLSKACTIA
IRYSAVRRQS EIKRSEPEPQ ILDFQTQQYK LFPLLATAYA FHFLGRYIKE TYMRINESIG
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF
EGENTVMMLQ TARFLMKIYD QVQSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTLVDINSL
DSLTEAYKLR AARLVEIAAK NLQAQVSHRK SKEVAWNLTS VDLVRASEAH CHYVTVKVFA
DKLPKIQDRA VQAVLRNLCL LYSLYGISQK GGDFLEGNII TGAQMSQVNS RILELLTVTR
PNAVALVDAF DFKDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY YKHLKPLQSK
L
