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Peroxisomal acyl-coenzyme A oxidase 1 (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) (Straight-chain acyl-CoA oxidase) (SCOX)

 ACOX1_HUMAN             Reviewed;         660 AA.
Q15067; A8K6X8; A8KAA0; B4DK61; F5GYQ8; Q12863; Q15068; Q15101;
Q16131; Q7Z3W5; Q9UD31;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 3.
25-OCT-2017, entry version 181.
RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000303|PubMed:8117268};
Short=AOX {ECO:0000303|PubMed:8117268};
EC=1.3.3.6 {ECO:0000250|UniProtKB:P07872};
AltName: Full=Palmitoyl-CoA oxidase {ECO:0000303|PubMed:14702039};
AltName: Full=Straight-chain acyl-CoA oxidase;
Short=SCOX;
Name=ACOX1 {ECO:0000312|HGNC:HGNC:119}; Synonyms=ACOX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=8159712; DOI=10.1073/pnas.91.8.3107;
Varanasi U., Chu R., Chu S., Espinosa R., Lebeau M.M., Reddy J.K.;
"Isolation of the human peroxisomal acyl-CoA oxidase gene:
organization, promoter analysis, and chromosomal localization.";
Proc. Natl. Acad. Sci. U.S.A. 91:3107-3111(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7876265; DOI=10.1074/jbc.270.9.4908;
Chu R., Varanasi U., Chu S., Lin Y., Usuda N., Rao M.S., Reddy J.K.;
"Overexpression and characterization of the human peroxisomal acyl-CoA
oxidase in insect cells.";
J. Biol. Chem. 270:4908-4915(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-312, AND
INVOLVEMENT IN PSEUDO-NALD.
TISSUE=Liver;
PubMed=8040306; DOI=10.1172/JCI117365;
Fourner B., Saudubray J.-M., Benichou B., Lyonnet S., Munnich A.,
Clevers H., Poll-The B.T.;
"Large deletion of the peroxisomal acyl-CoA oxidase gene in
pseudoneonatal adrenoleukodystrophy.";
J. Clin. Invest. 94:526-531(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-312.
TISSUE=Liver;
PubMed=8117268; DOI=10.1006/bbrc.1994.1158;
Aoyama T., Tsushima K., Souri M., Kamijo T., Suzuki Y., Shimozawa N.,
Orii T., Hashimoto T.;
"Molecular cloning and functional expression of a human peroxisomal
acyl-coenzyme A oxidase.";
Biochem. Biophys. Res. Commun. 198:1113-1118(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANT MET-312.
TISSUE=Placenta, Thalamus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
MET-312.
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
ILE-153 AND MET-312.
TISSUE=Colon, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
SPECIFICITY.
PubMed=17603022; DOI=10.1016/j.bbrc.2007.06.059;
Oaxaca-Castillo D., Andreoletti P., Vluggens A., Yu S.,
van Veldhoven P.P., Reddy J.K., Cherkaoui-Malki M.;
"Biochemical characterization of two functional human liver acyl-CoA
oxidase isoforms 1a and 1b encoded by a single gene.";
Biochem. Biophys. Res. Commun. 360:314-319(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-255; LYS-267; LYS-437;
LYS-500 AND LYS-504, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
TISSUE SPECIFICITY, AND REVERSAL OF ACOX1 NULL PHENOTYPE IN MOUSE.
PubMed=20195242; DOI=10.1038/labinvest.2010.46;
Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K.,
Kulik W., Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I.,
Rao M.S., Wanders R.J., Reddy J.K., Cherkaoui-Malki M.;
"Reversal of mouse Acyl-CoA oxidase 1 (ACOX1) null phenotype by human
ACOX1b isoform.";
Lab. Invest. 90:696-708(2010).
[15]
ERRATUM.
Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K.,
Kulik W., Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I.,
Rao M.S., Wanders R.J., Reddy J.K., Cherkaoui-Malki M.;
Lab. Invest. 90:808-808(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
PubMed=11815777; DOI=10.1067/mpd.2002.120511;
Suzuki Y., Iai M., Kamei A., Tanabe Y., Chida S., Yamaguchi S.,
Zhang Z., Takemoto Y., Shimozawa N., Kondo N.;
"Peroxisomal acyl-CoA oxidase deficiency.";
J. Pediatr. 140:128-130(2002).
[21]
VARIANTS PSEUDO-NALD VAL-64 DEL; CYS-178; LEU-184; VAL-231; VAL-278;
ARG-309 AND PRO-310, AND FUNCTION.
PubMed=17458872; DOI=10.1002/humu.20535;
Ferdinandusse S., Denis S., Hogenhout E.M., Koster J.,
van Roermund C.W., Ijlst L., Moser A.B., Wanders R.J., Waterham H.R.;
"Clinical, biochemical, and mutational spectrum of peroxisomal acyl-
coenzyme A oxidase deficiency.";
Hum. Mutat. 28:904-912(2007).
-!- FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-
enoyl-CoAs. Isoform 1 shows highest activity against medium-chain
fatty acyl-CoAs and activity decreases with increasing chain
length. Isoform 2 is active against a much broader range of
substrates and shows activity towards very long-chain acyl-CoAs.
Isoform 2 is twice as active as isoform 1 against 16-hydroxy-
palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-
CoA. {ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:17603022}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA +
H(2)O(2). {ECO:0000250|UniProtKB:P07872}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17603022};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=73 uM for palmitoyl-CoA (isoform 1)
{ECO:0000269|PubMed:17603022};
KM=90 uM for palmitoyl-CoA (isoform 2)
{ECO:0000269|PubMed:17603022};
pH dependence:
Optimum pH is 8.5 for isoform 1 and 7.5-8.5 for isoform 2.
{ECO:0000269|PubMed:17603022};
Temperature dependence:
Optimum temperature for isoform 1 at pH 7.5 is 40 degrees
Celsius with no activity at 50 degrees Celsius. Optimum
temperature for isoform 2 at pH 7.5 is 47.5 degrees Celsius with
57% activity retained at 50 degrees Celsius.
{ECO:0000269|PubMed:17603022};
-!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07872}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P07872}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ACOX1a, SCOX-exon 3I;
IsoId=Q15067-1; Sequence=Displayed;
Name=2; Synonyms=ACOX1b, SCOX-exon 3II;
IsoId=Q15067-2; Sequence=VSP_000146;
Name=3;
IsoId=Q15067-3; Sequence=VSP_046129, VSP_000146;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels of
isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed
at higher levels than isoform 2 in liver and kidney while isoform
2 levels are higher in brain, lung, muscle, white adipose tissue
and testis. Levels are almost equal in heart.
{ECO:0000269|PubMed:17603022, ECO:0000269|PubMed:20195242}.
-!- DISEASE: Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD)
[MIM:264470]: A peroxisomal single-enzyme disorder of fatty acid
beta-oxidation, resulting in clinical manifestations that remind
neonatal adrenoleukodystrophy. Clinical features include mental
retardation, leukodystrophy, seizures, mild hepatomegaly, hearing
deficit. Pseudo-NALD is characterized by increased plasma levels
of very-long chain fatty acids, due to decreased or absent
peroxisome acyl-CoA oxidase activity. Peroxisomes are intact and
functioning. {ECO:0000269|PubMed:11815777,
ECO:0000269|PubMed:17458872, ECO:0000269|PubMed:8040306}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Isoform 1 and isoform 2 can reverse the Acox1 null
phenotype in mouse which is characterized by severe microvesicular
hepatic steatosis, sustained activation of Ppara, spontaneous
massive peroxisome proliferation and eventual development of
hepatocellular carcinomas. Isoform 2 is more effective in reversal
of the phenotype than isoform 1 (PubMed:20195242).
{ECO:0000305|PubMed:20195242}.
-!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD97622.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U03268; AAA19113.1; -; Genomic_DNA.
EMBL; U03254; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03255; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03256; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03258; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03259; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03260; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03261; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03263; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03264; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03265; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03266; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03267; AAA19113.1; JOINED; Genomic_DNA.
EMBL; U03268; AAA19114.1; -; Genomic_DNA.
EMBL; U03254; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03255; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03257; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03258; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03259; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03260; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03261; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03263; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03264; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03265; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03266; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U03267; AAA19114.1; JOINED; Genomic_DNA.
EMBL; U07866; AAA18595.1; -; mRNA.
EMBL; X71440; CAA50574.1; -; mRNA.
EMBL; S69189; AAB30019.2; -; mRNA.
EMBL; AK291793; BAF84482.1; -; mRNA.
EMBL; AK292965; BAF85654.1; -; mRNA.
EMBL; AK296409; BAG59073.1; -; mRNA.
EMBL; BX537380; CAD97622.1; ALT_INIT; mRNA.
EMBL; AC040980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89351.1; -; Genomic_DNA.
EMBL; BC008767; AAH08767.1; -; mRNA.
EMBL; BC010425; AAH10425.1; -; mRNA.
CCDS; CCDS11734.1; -. [Q15067-2]
CCDS; CCDS11735.1; -. [Q15067-1]
PIR; A54942; A54942.
PIR; B54942; B54942.
PIR; I38095; I38095.
RefSeq; NP_001171968.1; NM_001185039.1. [Q15067-3]
RefSeq; NP_004026.2; NM_004035.6. [Q15067-2]
RefSeq; NP_009223.2; NM_007292.5. [Q15067-1]
UniGene; Hs.464137; -.
ProteinModelPortal; Q15067; -.
SMR; Q15067; -.
BioGrid; 106567; 44.
IntAct; Q15067; 9.
MINT; MINT-4717708; -.
STRING; 9606.ENSP00000293217; -.
DrugBank; DB07930; (3R)-3-HYDROXYDODECANOIC ACID.
DrugBank; DB03147; Flavin adenine dinucleotide.
SwissLipids; SLP:000000536; -. [Q15067-1]
SwissLipids; SLP:000000537; -. [Q15067-2]
iPTMnet; Q15067; -.
PhosphoSitePlus; Q15067; -.
SwissPalm; Q15067; -.
BioMuta; ACOX1; -.
DMDM; 126302511; -.
EPD; Q15067; -.
MaxQB; Q15067; -.
PaxDb; Q15067; -.
PeptideAtlas; Q15067; -.
PRIDE; Q15067; -.
TopDownProteomics; Q15067-1; -. [Q15067-1]
DNASU; 51; -.
Ensembl; ENST00000293217; ENSP00000293217; ENSG00000161533. [Q15067-2]
Ensembl; ENST00000301608; ENSP00000301608; ENSG00000161533. [Q15067-1]
GeneID; 51; -.
KEGG; hsa:51; -.
UCSC; uc002jqe.5; human. [Q15067-1]
CTD; 51; -.
DisGeNET; 51; -.
EuPathDB; HostDB:ENSG00000161533.11; -.
GeneCards; ACOX1; -.
HGNC; HGNC:119; ACOX1.
HPA; CAB021094; -.
HPA; HPA021192; -.
HPA; HPA021195; -.
HPA; HPA028759; -.
MalaCards; ACOX1; -.
MIM; 264470; phenotype.
MIM; 609751; gene.
neXtProt; NX_Q15067; -.
OpenTargets; ENSG00000161533; -.
Orphanet; 2971; Peroxisomal acyl-CoA oxidase deficiency.
PharmGKB; PA21; -.
eggNOG; KOG0136; Eukaryota.
eggNOG; COG1960; LUCA.
GeneTree; ENSGT00530000062919; -.
HOVERGEN; HBG050451; -.
InParanoid; Q15067; -.
KO; K00232; -.
OMA; GRRFFTM; -.
OrthoDB; EOG091G0A1P; -.
PhylomeDB; Q15067; -.
TreeFam; TF300672; -.
BioCyc; MetaCyc:HS08589-MONOMER; -.
BRENDA; 1.3.3.6; 2681.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
SABIO-RK; Q15067; -.
UniPathway; UPA00661; -.
ChiTaRS; ACOX1; human.
GeneWiki; ACOX1; -.
GenomeRNAi; 51; -.
PRO; PR:Q15067; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000161533; -.
CleanEx; HS_ACOX1; -.
ExpressionAtlas; Q15067; baseline and differential.
Genevisible; Q15067; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IMP:BHF-UCL.
GO; GO:0019395; P:fatty acid oxidation; IMP:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
GO; GO:0016559; P:peroxisome fission; IGI:UniProtKB.
GO; GO:2000189; P:positive regulation of cholesterol homeostasis; IGI:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; IMP:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:BHF-UCL.
CDD; cd01150; AXO; 1.
Gene3D; 1.10.540.10; -; 1.
InterPro; IPR034171; ACO.
InterPro; IPR029320; Acyl-CoA_ox_N.
InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
InterPro; IPR012258; Acyl-CoA_oxidase.
InterPro; IPR002655; Acyl-CoA_oxidase_C.
InterPro; IPR036250; AcylCo_DH_C-like.
InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
Pfam; PF01756; ACOX; 1.
Pfam; PF02770; Acyl-CoA_dh_M; 1.
Pfam; PF14749; Acyl-CoA_ox_N; 1.
PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
SUPFAM; SSF47203; SSF47203; 2.
SUPFAM; SSF56645; SSF56645; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Disease mutation; FAD; Fatty acid metabolism; Flavoprotein;
Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 660 Peroxisomal acyl-coenzyme A oxidase 1.
/FTId=PRO_0000204677.
MOTIF 658 660 Microbody targeting signal.
ACT_SITE 421 421 Proton acceptor.
{ECO:0000250|UniProtKB:P07872}.
BINDING 139 139 FAD. {ECO:0000250|UniProtKB:P07872}.
BINDING 178 178 FAD; via amide nitrogen.
{ECO:0000250|UniProtKB:P07872}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 89 89 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 90 90 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 216 216 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 241 241 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 255 255 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 267 267 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 349 349 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 437 437 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 437 437 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 446 446 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 446 446 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 500 500 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 504 504 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 512 512 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 512 512 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 542 542 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 637 637 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 637 637 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 643 643 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 651 651 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
MOD_RES 654 654 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9R0H0}.
VAR_SEQ 1 38 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046129.
VAR_SEQ 90 131 KLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGL
Q -> NFVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFM
PAWNLE (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:8040306}.
/FTId=VSP_000146.
VARIANT 64 64 Missing (in pseudo-NALD).
{ECO:0000269|PubMed:17458872}.
/FTId=VAR_067040.
VARIANT 101 101 G -> S (in dbSNP:rs3744032).
/FTId=VAR_048182.
VARIANT 153 153 T -> I (in dbSNP:rs17855420).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030619.
VARIANT 178 178 G -> C (in pseudo-NALD;
dbSNP:rs118204091).
{ECO:0000269|PubMed:11815777,
ECO:0000269|PubMed:17458872}.
/FTId=VAR_025789.
VARIANT 184 184 S -> L (in pseudo-NALD;
dbSNP:rs780887410).
{ECO:0000269|PubMed:17458872}.
/FTId=VAR_067041.
VARIANT 231 231 G -> V (in pseudo-NALD).
{ECO:0000269|PubMed:17458872}.
/FTId=VAR_067042.
VARIANT 278 278 M -> V (in pseudo-NALD;
dbSNP:rs118204090).
{ECO:0000269|PubMed:11815777,
ECO:0000269|PubMed:17458872}.
/FTId=VAR_025790.
VARIANT 309 309 Q -> R (in pseudo-NALD;
dbSNP:rs118204092).
{ECO:0000269|PubMed:17458872}.
/FTId=VAR_067043.
VARIANT 310 310 S -> P (in pseudo-NALD;
dbSNP:rs758962364).
{ECO:0000269|PubMed:17458872}.
/FTId=VAR_067044.
VARIANT 312 312 I -> M (in dbSNP:rs1135640).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:8040306,
ECO:0000269|PubMed:8117268}.
/FTId=VAR_021529.
CONFLICT 27 27 P -> L (in Ref. 3; CAA50574).
{ECO:0000305}.
CONFLICT 80 80 A -> R (in Ref. 3; CAA50574).
{ECO:0000305}.
CONFLICT 84 84 E -> D (in Ref. 6; CAD97622).
{ECO:0000305}.
CONFLICT 119 119 Q -> E (in Ref. 4; AAB30019).
{ECO:0000305}.
CONFLICT 200 200 Y -> H (in Ref. 2; AAA18595).
{ECO:0000305}.
CONFLICT 212 213 IG -> NR (in Ref. 1; AAA19113/AAA19114
and 2; AAA18595). {ECO:0000305}.
CONFLICT 264 264 T -> P (in Ref. 1; AAA19113/AAA19114 and
2; AAA18595). {ECO:0000305}.
CONFLICT 332 332 F -> L (in Ref. 2; AAA18595).
{ECO:0000305}.
CONFLICT 449 449 C -> R (in Ref. 2; AAA18595).
{ECO:0000305}.
CONFLICT 490 490 R -> L (in Ref. 5; BAF85654).
{ECO:0000305}.
CONFLICT 531 531 C -> L (in Ref. 1; AAA19113/AAA19114 and
2; AAA18595). {ECO:0000305}.
CONFLICT 534 535 VV -> GL (in Ref. 1; AAA19113/AAA19114
and 2; AAA18595). {ECO:0000305}.
CONFLICT 615 615 V -> A (in Ref. 3; CAA50574).
{ECO:0000305}.
CONFLICT 650 650 Y -> YH (in Ref. 4; AAB30019).
{ECO:0000305}.
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


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