ACOX1_HUMAN
ID ACOX1_HUMAN Reviewed; 660 AA.
AC Q15067; A8K6X8; A8KAA0; B4DK61; F5GYQ8; Q12863; Q15068; Q15101; Q16131;
AC Q7Z3W5; Q9UD31;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000303|PubMed:8117268};
DE Short=AOX {ECO:0000303|PubMed:8117268};
DE EC=1.3.3.6 {ECO:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242, ECO:0000269|PubMed:7876265, ECO:0000305|PubMed:33234382};
DE AltName: Full=Palmitoyl-CoA oxidase {ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:7876265};
DE AltName: Full=Peroxisomal fatty acyl-CoA oxidase;
DE AltName: Full=Straight-chain acyl-CoA oxidase {ECO:0000303|PubMed:15060085};
DE Short=SCOX {ECO:0000303|PubMed:15060085};
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|HGNC:HGNC:119}; Synonyms=ACOX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=8159712; DOI=10.1073/pnas.91.8.3107;
RA Varanasi U., Chu R., Chu S., Espinosa R., Lebeau M.M., Reddy J.K.;
RT "Isolation of the human peroxisomal acyl-CoA oxidase gene: organization,
RT promoter analysis, and chromosomal localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3107-3111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY
RP (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=7876265; DOI=10.1074/jbc.270.9.4908;
RA Chu R., Varanasi U., Chu S., Lin Y., Usuda N., Rao M.S., Reddy J.K.;
RT "Overexpression and characterization of the human peroxisomal acyl-CoA
RT oxidase in insect cells.";
RL J. Biol. Chem. 270:4908-4915(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-312, AND INVOLVEMENT IN
RP PSEUDO-NALD.
RC TISSUE=Liver;
RX PubMed=8040306; DOI=10.1172/jci117365;
RA Fourner B., Saudubray J.-M., Benichou B., Lyonnet S., Munnich A.,
RA Clevers H., Poll-The B.T.;
RT "Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal
RT adrenoleukodystrophy.";
RL J. Clin. Invest. 94:526-531(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-312.
RC TISSUE=Liver;
RX PubMed=8117268; DOI=10.1006/bbrc.1994.1158;
RA Aoyama T., Tsushima K., Souri M., Kamijo T., Suzuki Y., Shimozawa N.,
RA Orii T., Hashimoto T.;
RT "Molecular cloning and functional expression of a human peroxisomal acyl-
RT coenzyme A oxidase.";
RL Biochem. Biophys. Res. Commun. 198:1113-1118(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP MET-312.
RC TISSUE=Placenta, Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-312.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ILE-153
RP AND MET-312.
RC TISSUE=Colon, and Eye;
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 [10]
RP FUNCTION.
RX PubMed=15060085; DOI=10.1194/jlr.m300512-jlr200;
RA Ferdinandusse S., Denis S., Van Roermund C.W., Wanders R.J., Dacremont G.;
RT "Identification of the peroxisomal beta-oxidation enzymes involved in the
RT degradation of long-chain dicarboxylic acids.";
RL J. Lipid Res. 45:1104-1111(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP FUNCTION (ISOFORMS 1 AND 2), COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES
RP (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, CATALYTIC ACTIVITY (ISOFORMS 1 AND
RP 2), AND PATHWAY.
RX PubMed=17603022; DOI=10.1016/j.bbrc.2007.06.059;
RA Oaxaca-Castillo D., Andreoletti P., Vluggens A., Yu S., van Veldhoven P.P.,
RA Reddy J.K., Cherkaoui-Malki M.;
RT "Biochemical characterization of two functional human liver acyl-CoA
RT oxidase isoforms 1a and 1b encoded by a single gene.";
RL Biochem. Biophys. Res. Commun. 360:314-319(2007).
RN [13]
RP INTERACTION WITH LONP2.
RX PubMed=18281296; DOI=10.1093/jb/mvn020;
RA Omi S., Nakata R., Okamura-Ikeda K., Konishi H., Taniguchi H.;
RT "Contribution of peroxisome-specific isoform of Lon protease in sorting
RT PTS1 proteins to peroxisomes.";
RL J. Biochem. 143:649-660(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-267; LYS-437; LYS-500
RP AND LYS-504, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP TISSUE SPECIFICITY, CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), AND REVERSAL OF
RP ACOX1 NULL PHENOTYPE IN MOUSE.
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 [17]
RP ERRATUM OF PUBMED:20195242.
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.;
RL Lab. Invest. 90:808-808(2010).
RN [18]
RP CATALYTIC ACTIVITY, VARIANT PSEUDO-NALD SER-420, AND FUNCTION.
RX PubMed=33234382; DOI=10.1016/j.braindev.2020.10.011;
RA Morita A., Enokizono T., Ohto T., Tanaka M., Watanabe S., Takada Y.,
RA Iwama K., Mizuguchi T., Matsumoto N., Morita M., Takashima S.,
RA Shimozawa N., Takada H.;
RT "Novel ACOX1 mutations in two siblings with peroxisomal acyl-CoA oxidase
RT deficiency.";
RL Brain Dev. 43:475-481(2021).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
RX PubMed=11815777; DOI=10.1067/mpd.2002.120511;
RA Suzuki Y., Iai M., Kamei A., Tanabe Y., Chida S., Yamaguchi S., Zhang Z.,
RA Takemoto Y., Shimozawa N., Kondo N.;
RT "Peroxisomal acyl-CoA oxidase deficiency.";
RL J. Pediatr. 140:128-130(2002).
RN [24]
RP VARIANTS PSEUDO-NALD VAL-64 DEL; CYS-178; LEU-184; VAL-231; VAL-278;
RP ARG-309 AND PRO-310, AND FUNCTION.
RX PubMed=17458872; DOI=10.1002/humu.20535;
RA Ferdinandusse S., Denis S., Hogenhout E.M., Koster J., van Roermund C.W.,
RA Ijlst L., Moser A.B., Wanders R.J., Waterham H.R.;
RT "Clinical, biochemical, and mutational spectrum of peroxisomal acyl-
RT coenzyme A oxidase deficiency.";
RL Hum. Mutat. 28:904-912(2007).
RN [25]
RP INVOLVEMENT IN MITCH, VARIANT MITCH SER-237, CHARACTERIZATION OF VARIANT
RP MITCH SER-237, SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RX PubMed=32169171; DOI=10.1016/j.neuron.2020.02.021;
RG Members of Undiagnosed Diseases Network;
RA Chung H.L., Wangler M.F., Marcogliese P.C., Jo J., Ravenscroft T.A.,
RA Zuo Z., Duraine L., Sadeghzadeh S., Li-Kroeger D., Schmidt R.E.,
RA Pestronk A., Rosenfeld J.A., Burrage L., Herndon M.J., Chen S.,
RA Shillington A., Vawter-Lee M., Hopkin R., Rodriguez-Smith J.,
RA Henrickson M., Lee B., Moser A.B., Jones R.O., Watkins P., Yoo T., Mar S.,
RA Choi M., Bucelli R.C., Yamamoto S., Lee H.K., Prada C.E., Chae J.H.,
RA Vogel T.P., Bellen H.J.;
RT "Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Loss via
RT Different Mechanisms.";
RL Neuron 106:589.e6-606.e6(2020).
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 (PubMed:7876265, PubMed:15060085, PubMed:17458872,
CC PubMed:17603022, PubMed:32169171, PubMed:33234382). Catalyzes the
CC desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-
CC CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-
CC CoA, and donates electrons directly to molecular oxygen (O(2)), thereby
CC producing hydrogen peroxide (H(2)O(2)) (PubMed:7876265,
CC PubMed:17458872, PubMed:17603022). {ECO:0000269|PubMed:15060085,
CC ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:17603022,
CC ECO:0000269|PubMed:32169171, ECO:0000269|PubMed:33234382,
CC ECO:0000269|PubMed:7876265}.
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:0000269|PubMed:17603022}.
CC -!- FUNCTION: [Isoform 2]: Is active against a much broader range of
CC substrates and shows activity towards long-chain fatty acyl-CoAs.
CC {ECO:0000269|PubMed:17603022}.
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:33234382};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:33234382};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242,
CC ECO:0000269|PubMed:7876265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:17603022, ECO:0000305|PubMed:20195242,
CC ECO:0000305|PubMed:7876265};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:17603022, ECO:0000305|PubMed:20195242};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242,
CC ECO:0000269|PubMed:7876265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:17603022, ECO:0000305|PubMed:20195242,
CC ECO:0000305|PubMed:7876265};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:17603022, ECO:0000305|PubMed:20195242};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644;
CC Evidence={ECO:0000305|PubMed:17603022};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:17603022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644;
CC Evidence={ECO:0000305|PubMed:17603022};
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:0000305|PubMed:33234382};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000305|PubMed:33234382};
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=(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:0000250|UniProtKB:Q9R0H0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39120;
CC Evidence={ECO:0000250|UniProtKB:Q9R0H0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17603022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=73 uM for hexadecanoyl-CoA (palmitoyl-CoA)
CC {ECO:0000269|PubMed:17603022};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17603022};
CC Temperature dependence:
CC Optimum temperature at pH 7.5 is 40 degrees Celsius with no activity
CC at 50 degrees Celsius. {ECO:0000269|PubMed:17603022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=90 uM for hexadecanoyl-CoA (palmitoyl-CoA)
CC {ECO:0000269|PubMed:17603022};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:17603022};
CC Temperature dependence:
CC Optimum temperature at pH 7.5 is 47.5 degrees Celsius with 57%
CC activity retained at 50 degrees Celsius.
CC {ECO:0000269|PubMed:17603022};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:17603022}.
CC -!- SUBUNIT: Homodimer (PubMed:32169171). Interacts with LONP2
CC (PubMed:18281296). {ECO:0000269|PubMed:18281296,
CC ECO:0000269|PubMed:32169171}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:32169171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ACOX1a, SCOX-exon 3I;
CC IsoId=Q15067-1; Sequence=Displayed;
CC Name=2; Synonyms=ACOX1b, SCOX-exon 3II;
CC IsoId=Q15067-2; Sequence=VSP_000146;
CC Name=3;
CC IsoId=Q15067-3; Sequence=VSP_046129, VSP_000146;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels of isoform 1
CC and isoform 2 detected in testis. Isoform 1 is expressed at higher
CC levels than isoform 2 in liver and kidney while isoform 2 levels are
CC higher in brain, lung, muscle, white adipose tissue and testis. Levels
CC are almost equal in heart. {ECO:0000269|PubMed:17603022,
CC ECO:0000269|PubMed:20195242}.
CC -!- DISEASE: Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD)
CC [MIM:264470]: A peroxisomal single-enzyme disorder of fatty acid beta-
CC oxidation, resulting in clinical manifestations that remind neonatal
CC adrenoleukodystrophy. Clinical features include intellectual
CC disability, leukodystrophy, seizures, mild hepatomegaly, hearing
CC deficit. Pseudo-NALD is characterized by increased plasma levels of
CC very-long chain fatty acids, due to decreased or absent peroxisome
CC acyl-CoA oxidase activity. Peroxisomes are intact and functioning.
CC {ECO:0000269|PubMed:11815777, ECO:0000269|PubMed:17458872,
CC ECO:0000269|PubMed:33234382, ECO:0000269|PubMed:8040306}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Mitchell syndrome (MITCH) [MIM:618960]: A disorder
CC characterized by episodic demyelination, sensorimotor polyneuropathy,
CC and sensorineural hearing loss. {ECO:0000269|PubMed:32169171}. Note=The
CC gene represented in this entry is involved in disease pathogenesis.
CC -!- MISCELLANEOUS: Isoform 1 and isoform 2 can reverse the Acox1 null
CC phenotype in mouse which is characterized by severe microvesicular
CC hepatic steatosis, sustained activation of PPARA, spontaneous massive
CC peroxisome proliferation and eventual development of hepatocellular
CC carcinomas. Isoform 2 is more effective in reversal of the phenotype
CC than isoform 1 (PubMed:20195242). {ECO:0000305|PubMed:20195242}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97622.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U03268; AAA19113.1; -; Genomic_DNA.
DR EMBL; U03254; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03255; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03256; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03258; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03259; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03260; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03261; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03263; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03264; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03265; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03266; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03267; AAA19113.1; JOINED; Genomic_DNA.
DR EMBL; U03268; AAA19114.1; -; Genomic_DNA.
DR EMBL; U03254; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03255; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03257; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03258; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03259; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03260; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03261; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03263; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03264; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03265; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03266; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U03267; AAA19114.1; JOINED; Genomic_DNA.
DR EMBL; U07866; AAA18595.1; -; mRNA.
DR EMBL; X71440; CAA50574.1; -; mRNA.
DR EMBL; S69189; AAB30019.2; -; mRNA.
DR EMBL; AK291793; BAF84482.1; -; mRNA.
DR EMBL; AK292965; BAF85654.1; -; mRNA.
DR EMBL; AK296409; BAG59073.1; -; mRNA.
DR EMBL; BX537380; CAD97622.1; ALT_INIT; mRNA.
DR EMBL; AC040980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89351.1; -; Genomic_DNA.
DR EMBL; BC008767; AAH08767.1; -; mRNA.
DR EMBL; BC010425; AAH10425.1; -; mRNA.
DR CCDS; CCDS11734.1; -. [Q15067-2]
DR CCDS; CCDS11735.1; -. [Q15067-1]
DR PIR; A54942; A54942.
DR PIR; B54942; B54942.
DR PIR; I38095; I38095.
DR RefSeq; NP_001171968.1; NM_001185039.1. [Q15067-3]
DR RefSeq; NP_004026.2; NM_004035.6. [Q15067-2]
DR RefSeq; NP_009223.2; NM_007292.5. [Q15067-1]
DR AlphaFoldDB; Q15067; -.
DR SMR; Q15067; -.
DR BioGRID; 106567; 103.
DR IntAct; Q15067; 30.
DR STRING; 9606.ENSP00000293217; -.
DR ChEMBL; CHEMBL4105748; -.
DR DrugBank; DB07930; (3R)-3-HYDROXYDODECANOIC ACID.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB09328; Vayarin.
DR SwissLipids; SLP:000000536; -. [Q15067-1]
DR SwissLipids; SLP:000000537; -. [Q15067-2]
DR GlyGen; Q15067; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15067; -.
DR PhosphoSitePlus; Q15067; -.
DR SwissPalm; Q15067; -.
DR BioMuta; ACOX1; -.
DR DMDM; 126302511; -.
DR EPD; Q15067; -.
DR jPOST; Q15067; -.
DR MassIVE; Q15067; -.
DR MaxQB; Q15067; -.
DR PaxDb; Q15067; -.
DR PeptideAtlas; Q15067; -.
DR PRIDE; Q15067; -.
DR ProteomicsDB; 24812; -.
DR ProteomicsDB; 60421; -. [Q15067-1]
DR ProteomicsDB; 60422; -. [Q15067-2]
DR TopDownProteomics; Q15067-1; -. [Q15067-1]
DR Antibodypedia; 19646; 393 antibodies from 31 providers.
DR DNASU; 51; -.
DR Ensembl; ENST00000293217.10; ENSP00000293217.4; ENSG00000161533.12. [Q15067-2]
DR Ensembl; ENST00000301608.8; ENSP00000301608.4; ENSG00000161533.12. [Q15067-1]
DR GeneID; 51; -.
DR KEGG; hsa:51; -.
DR MANE-Select; ENST00000293217.10; ENSP00000293217.4; NM_004035.7; NP_004026.2. [Q15067-2]
DR UCSC; uc002jqe.5; human. [Q15067-1]
DR CTD; 51; -.
DR DisGeNET; 51; -.
DR GeneCards; ACOX1; -.
DR HGNC; HGNC:119; ACOX1.
DR HPA; ENSG00000161533; Tissue enhanced (liver).
DR MalaCards; ACOX1; -.
DR MIM; 264470; phenotype.
DR MIM; 609751; gene.
DR MIM; 618960; phenotype.
DR neXtProt; NX_Q15067; -.
DR OpenTargets; ENSG00000161533; -.
DR Orphanet; 2971; Peroxisomal acyl-CoA oxidase deficiency.
DR PharmGKB; PA21; -.
DR VEuPathDB; HostDB:ENSG00000161533; -.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000157287; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q15067; -.
DR OMA; GRRFFTM; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; Q15067; -.
DR TreeFam; TF300672; -.
DR BioCyc; MetaCyc:HS08589-MON; -.
DR BRENDA; 1.3.3.6; 2681.
DR PathwayCommons; Q15067; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression. [Q15067-1]
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism. [Q15067-2]
DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids. [Q15067-2]
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins.
DR SABIO-RK; Q15067; -.
DR SignaLink; Q15067; -.
DR SIGNOR; Q15067; -.
DR UniPathway; UPA00661; -.
DR BioGRID-ORCS; 51; 59 hits in 1084 CRISPR screens.
DR ChiTaRS; ACOX1; human.
DR GeneWiki; ACOX1; -.
DR GenomeRNAi; 51; -.
DR Pharos; Q15067; Tchem.
DR PRO; PR:Q15067; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q15067; protein.
DR Bgee; ENSG00000161533; Expressed in jejunal mucosa and 202 other tissues.
DR ExpressionAtlas; Q15067; baseline and differential.
DR Genevisible; Q15067; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IGI:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IMP:BHF-UCL.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; IMP:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0016559; P:peroxisome fission; IGI:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0140493; P:very long-chain fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:BHF-UCL.
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; Deafness; Disease variant; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Neuropathy;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..660
FT /note="Peroxisomal acyl-CoA oxidase 1, A chain"
FT /id="PRO_0000204677"
FT CHAIN 1..468
FT /note="Peroxisomal acyl-CoA oxidase 1, B chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447500"
FT CHAIN 469..660
FT /note="Peroxisomal acyl-CoA oxidase 1, C chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447501"
FT MOTIF 658..660
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:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 241
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 349
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 437
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 446
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 446
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 504
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 512
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 512
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 542
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 637
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 637
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 643
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 651
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 654
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046129"
FT VAR_SEQ 90..131
FT /note="KLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQ -> NFVHRG
FT RPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLE (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:8040306"
FT /id="VSP_000146"
FT VARIANT 64
FT /note="Missing (in pseudo-NALD)"
FT /evidence="ECO:0000269|PubMed:17458872"
FT /id="VAR_067040"
FT VARIANT 101
FT /note="G -> S (in dbSNP:rs3744032)"
FT /id="VAR_048182"
FT VARIANT 153
FT /note="T -> I (in dbSNP:rs17855420)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030619"
FT VARIANT 178
FT /note="G -> C (in pseudo-NALD; dbSNP:rs118204091)"
FT /evidence="ECO:0000269|PubMed:11815777,
FT ECO:0000269|PubMed:17458872"
FT /id="VAR_025789"
FT VARIANT 184
FT /note="S -> L (in pseudo-NALD; dbSNP:rs780887410)"
FT /evidence="ECO:0000269|PubMed:17458872"
FT /id="VAR_067041"
FT VARIANT 231
FT /note="G -> V (in pseudo-NALD)"
FT /evidence="ECO:0000269|PubMed:17458872"
FT /id="VAR_067042"
FT VARIANT 237
FT /note="N -> S (in MITCH; gain-of-function; increased
FT dimerization; increased protein levels and peroxisomal
FT acyl-coenzyme A oxidase function; increased levels of
FT reactive oxygen species; no effect on VLCFA levels; no
FT effect on peroxisome location; causes Schwann cell death
FT and myelination defects; dbSNP:rs1567876984)"
FT /evidence="ECO:0000269|PubMed:32169171"
FT /id="VAR_083893"
FT VARIANT 278
FT /note="M -> V (in pseudo-NALD; dbSNP:rs118204090)"
FT /evidence="ECO:0000269|PubMed:11815777,
FT ECO:0000269|PubMed:17458872"
FT /id="VAR_025790"
FT VARIANT 309
FT /note="Q -> R (in pseudo-NALD; dbSNP:rs118204092)"
FT /evidence="ECO:0000269|PubMed:17458872"
FT /id="VAR_067043"
FT VARIANT 310
FT /note="S -> P (in pseudo-NALD; dbSNP:rs758962364)"
FT /evidence="ECO:0000269|PubMed:17458872"
FT /id="VAR_067044"
FT VARIANT 312
FT /note="I -> M (in dbSNP:rs1135640)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:8040306, ECO:0000269|PubMed:8117268"
FT /id="VAR_021529"
FT VARIANT 420
FT /note="F -> S (in Pseudo-NALD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33234382"
FT /id="VAR_085887"
FT CONFLICT 27
FT /note="P -> L (in Ref. 3; CAA50574)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="A -> R (in Ref. 3; CAA50574)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> D (in Ref. 6; CAD97622)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="Q -> E (in Ref. 4; AAB30019)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Y -> H (in Ref. 2; AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..213
FT /note="IG -> NR (in Ref. 1; AAA19113/AAA19114 and 2;
FT AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="T -> P (in Ref. 1; AAA19113/AAA19114 and 2;
FT AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="F -> L (in Ref. 2; AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="C -> R (in Ref. 2; AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="R -> L (in Ref. 5; BAF85654)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="C -> L (in Ref. 1; AAA19113/AAA19114 and 2;
FT AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 534..535
FT /note="VV -> GL (in Ref. 1; AAA19113/AAA19114 and 2;
FT AAA18595)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="V -> A (in Ref. 3; CAA50574)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="Y -> YH (in Ref. 4; AAB30019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 74424 MW; D713768A47374EA1 CRC64;
MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY
EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQK
EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL
GKTSNHAIVL AQLITKGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL
KMDNHRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA
IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE TYHRINEGIG
QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG YSHCSGLPNI YVNFTPSCTF
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP
ESLTEAYKLR AARLVEIAAK NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS
EKLLKIQDKA IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR
SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY KHLKSLQSKL
