ACOX2 Protein Overview: Sequence, Structure, Function and Protein Interaction

ACOX2 Protein Overview

ACOX2 reagents

Baumgart et al. (1996) reported the molecular characterization of branched-chain acyl-CoA oxidase. Its composite cDNA sequence, derived from overlapping clones isolated by immunoscreening and hybridization of human liver cDNA expression libraries, consists of 2,225 bp and contains an open reading frame of 2,046 bp, encoding a protein of 681 amino acids with a calculated molecular mass of 76,739 Da. The C-terminal tripeptide of the protein was found to be SKL (ser-lys-leu), a known peroxisome targeting signal. Sequence comparison with the other acyl-CoA oxidases and evolutionary analysis demonstrated that, despite its broader substrate specificity, this branched-chain acyl-CoA oxidase is the human homolog of rat trihydroxycoprostanoyl-CoA oxidase and that separate gene duplication events led to the occurrence in mammals of acyl-CoA oxidases with different substrate specificities. Northern blot analysis demonstrated that, in contrast to the rat gene, the human gene is transcribed also in extra hepatic tissues, such as heart, kidney, skeletal muscle, and pancreas. The highest levels of the 2.6-kb mRNA were found in heart, followed by liver. The enzyme was absent from livers of Zellweger patients, as shown by immunoblot analysis and immunocytochemistry. Palmitoyl-CoA oxidase was also absent, whereas even in autolytic samples of human control livers both acyl-CoA oxidases were present. Baumgart et al. (1996) noted that the deficiency of these enzymes is part of the generalized deficiency in peroxisomal beta-oxidation enzymes in Zellweger syndrome (see 214100). Baumgart et al. (1996) isolated the rat trihydroxycoprostanoyl-CoA oxidase cDNA sequenced by screening rat liver cDNA expression libraries. The gene contains a 2,046-bp open reading frame encoding a protein of 681 amino acids with a calculated molecular mass of 76,711 Da. This sequence shares 45% amino acid identity with rat palmitoyl-CoA oxidase and 22% with rat pristanoyl-CoA oxidase. The C terminus (his-lys-met) of trihydroxycoprostanoyl-CoA oxidase does not appear to interact with the C-terminal peroxisomal targeting signal 1 (PTS1) import receptor (PEX5; 600414), although the tripeptide fits the rule of conserved variants for targeting of proteins to glycosomes of Trypanosomatidea. Northern analysis of multiple rat tissues revealed a 2.6-kb transcript only in liver and kidney.

ACOX2 protein family

Belongs to the acyl-CoA oxidase family.

ACOX2 protein name

Recommended name
Peroxisomal acyl-coenzyme A oxidase 2
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase, branched chain acyl-CoA oxidase, BRCACOX, BRCOX, THCCox, trihydroxycoprostanoyl-CoA oxidase

ACOX2 Protein Molecular Weight & PI

The parameters have been computed for the following feature

FT CHAIN 1-681 Peroxisomal acyl-coenzyme A oxidase 2.

Molecular weight (Da)


Theoretical pI


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