[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2). TISSUE=Foreskin; PubMed=8159712 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1074/jbc.270.9.4908; PubMed=7876265 [NCBI, ExPASy, EBI, Israel, Japan] 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 PSEUDONEONATAL ADRENOLEUKODYSTROPHY. TISSUE=Liver; PubMed=8040306 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1006/bbrc.1994.1158; PubMed=8117268 [NCBI, ExPASy, EBI, Israel, Japan] 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] (ISOFORM 2), AND VARIANTS ILE-153 AND MET-312. TISSUE=Colon, and Eye; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	VARIANTS PEROXISOMAL ACYL-COA OXIDASE DEFICIENCY CYS-178 AND VAL-278. DOI=10.1067/mpd.2002.120511; PubMed=11815777 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs.
CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD.
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation .
SUBCELLULAR LOCATION: Peroxisome.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q15067-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q15067-2

Features which should be applied to build the isoform sequence: VSP_000146.
DISEASE: Defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy [MIM:264470]; also known as peroxisomal acyl-CoA oxidase deficiency. Pseudo-NALD is a peroxisomal single-enzyme disorder. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly, hearing deficit. Pseudo-NALD is characterized by increased plasma levels of very-long chain fatty cids, due to decreased or absent peroxisome acyl-CoA oxidase activity. Peroxisomes are intact and functioning.
SIMILARITY: Belongs to the acyl-CoA oxidase family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ACOX1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U03268; AAA19113.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03254; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03255; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03256; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03258; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03259; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03260; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03261; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03263; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03264; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03265; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03266; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03267; AAA19113.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03268; AAA19114.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03254; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03255; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03257; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03258; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03259; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03260; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03261; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03263; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03264; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03265; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03266; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U03267; AAA19114.1; JOINED; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U07866; AAA18595.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X71440; CAA50574.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S69189; AAB30019.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008767; AAH08767.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010425; AAH10425.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A54942; A54942.
B54942; B54942.
I38095; I38095.

RefSeq

NP_004026.2; -.
NP_009223.2; -.

UniGene

Hs.464137

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

Q15067; 1-654.

PTM databases

Q15067; -.

Organism-specific databases

GC17M071453; -.

HIX0021139; -.

HGNC:119; ACOX1.

264470; phenotype. [NCBI / EBI]
609751; gene. [NCBI / EBI]

Orphanet

2971; Pseudoadrenoleukodystrophy.

PharmGKB

PA21; -.

GeneCards

Q15067.

Gene expression databases

ArrayExpress

Q15067; -.

CleanEx

HS_ACOX1; -.

GermOnline

ENSG00000161533; Homo sapiens.

Ontologies

GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997;	Molecular function: acyl-CoA oxidase activity (inferred from direct assay from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0006091;	Biological process: generation of precursor metabolites and energy (inferred from mutant phenotype from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006693;	Biological process: prostaglandin metabolic process (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

Proteomic databases

PeptideAtlas

Q15067; -.

Proteomics databases

PRIDE

Q15067; -.

Genome annotation databases

Ensembl

ENSG00000161533; Homo sapiens. [Contig view]

GeneID

51; -.

KEGG

hsa:51; -.

NMPDR

fig|9606.3.peg.14420; -.

Phylogenomic databases

HOGENOM

Q15067; -.

HOVERGEN

Q15067; -.

Other

199; -.

ACOX1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Alternative splicing; Disease mutation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 660`	`660`	`Peroxisomal acyl-coenzyme A oxidase 1.`	`PRO_0000204677`
`MOTIF`	`658 660`	`3`	`Microbody targeting signal.`
`MOD_RES`	`26 26`		`Phosphoserine.`
`MOD_RES`	`267 267`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`310 310`		`Phosphoserine (By similarity).`
`MOD_RES`	`643 643`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`649 649`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`90 131`		`KLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLS` `SKGLQ -> NFVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFMP` `AWNLE (in isoform 2).`	`VSP_000146`
`VARIANT`	`101 101`	`1`	`G -> S (in dbSNP:rs3744032 [NCBI]).`	`VAR_048182`
`VARIANT`	`153 153`	`1`	`T -> I (in dbSNP:rs17855420 [NCBI]).`	`VAR_030619`
`VARIANT`	`178 178`	`1`	`G -> C (in pseudo-NALD).`	`VAR_025789`
`VARIANT`	`278 278`	`1`	`M -> V (in pseudo-NALD).`	`VAR_025790`
`VARIANT`	`312 312`	`1`	`I -> M (in dbSNP:rs1137582 [NCBI]).`	`VAR_021529`
`CONFLICT`	`27 27`		`P -> L (in Ref. 3; CAA50574).`
`CONFLICT`	`80 80`		`A -> R (in Ref. 3; CAA50574).`
`CONFLICT`	`119 119`		`Q -> E (in Ref. 4; AAB30019).`
`CONFLICT`	`200 200`		`Y -> H (in Ref. 2; AAA18595).`
`CONFLICT`	`212 213`		`IG -> NR (in Ref. 1; AAA19113 and 2; AAA18595).`
`CONFLICT`	`264 264`		`T -> P (in Ref. 1; AAA19113 and 2; AAA18595).`
`CONFLICT`	`332 332`		`F -> L (in Ref. 2; AAA18595).`
`CONFLICT`	`449 449`		`C -> R (in Ref. 2; AAA18595).`
`CONFLICT`	`531 531`		`C -> L (in Ref. 1; AAA19113 and 2; AAA18595).`
`CONFLICT`	`534 535`		`VV -> GL (in Ref. 1; AAA19113 and 2; AAA18595).`
`CONFLICT`	`615 615`		`V -> A (in Ref. 3; CAA50574).`
`CONFLICT`	`650 650`		`Y -> YH (in Ref. 4; AAB30019).`

Sequence information

Length: 660 AA [This is the length of the unprocessed precursor]

Molecular weight: 74424 Da [This is the MW of the unprocessed precursor]

CRC64: D713768A47374EA1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY 

        70         80         90        100        110        120 
EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQK 

       130        140        150        160        170        180 
EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITKGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL 

       250        260        270        280        290        300 
KMDNHRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA 

       310        320        330        340        350        360 
IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE TYHRINEGIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG YSHCSGLPNI YVNFTPSCTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP 

       490        500        510        520        530        540 
ESLTEAYKLR AARLVEIAAK NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS 

       550        560        570        580        590        600 
EKLLKIQDKA IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR 

       610        620        630        640        650        660 
SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY KHLKSLQSKL

Q15067 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools