Reviewed,
UniProtKB/Swiss-Prot Q9R0H0 (ACOX1_MOUSE)
Last modified
October 13, 2009.
Version 78.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Peroxisomal acyl-coenzyme A oxidase 1 Short name=AOX EC=1.3.3.6 Alternative name(s): Palmitoyl-CoA oxidase | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 661 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs By similarity. |
| Catalytic activity | Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2. |
| Cofactor | FAD By similarity. |
| Pathway | |
| Subcellular location | Peroxisome By similarity. |
| Sequence similarities | Belongs to the acyl-CoA oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Peroxisome |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | fatty acid beta-oxidation Traceable author statement. Source: MGI oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW spermatogenesisInferred from mutant phenotype. Source: MGI |
| Cellular component | mitochondrion Inferred from direct assay. Source: MGI peroxisomal membraneInferred from direct assay. Source: MGI |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activityInferred from electronic annotation. Source: InterPro acyl-CoA oxidase activityTraceable author statement. Source: MGI electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 661 | 661 | Peroxisomal acyl-coenzyme A oxidase 1 | PRO_0000204678 | |||||
Regions | |||||||||
| Motif | 659 – 661 | 3 | Microbody targeting signal | ||||||
Sites | |||||||||
| Active site | 421 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 139 | 1 | FAD By similarity | ||||||
| Binding site | 178 | 1 | FAD; via amide nitrogen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 26 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 255 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 267 | 1 | N6-acetyllysine Ref.4 | ||||||
| Modified residue | 310 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 437 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 500 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 643 | 1 | N6-acetyllysine Ref.4 | ||||||
| Modified residue | 649 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 652 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 22 | 1 | V → I in BAA86870. Ref.2 | ||||||
| Sequence conflict | 263 | 1 | G → D in BAE41642. Ref.3 | ||||||
| Sequence conflict | 516 | 1 | W → R in BAE41642. Ref.3 | ||||||
| Sequence conflict | 523 | 1 | L → I in BAE41642. Ref.3 | ||||||
| Sequence conflict | 648 | 1 | E → Q in AAB62926. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase." Nohammer C., El-Shabrawi Y., Schauer S., Hiden M., Berger J., Forss-Petter S., Winter E., Eferl R., Zechner R., Hoefler G. Eur. J. Biochem. 267:1254-1260(2000) [PubMed: 10672038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | Saibara T., Adachi K. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Liver. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.  Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-661. Strain: NOD. Tissue: Dendritic cell. |
| [4] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-643, MASS SPECTROMETRY. Tissue: Liver. |
| [5] | "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-649, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF006688 mRNA. Translation: AAB62926.1. AB034914 mRNA. Translation: BAA86870.1. AK170217 mRNA. Translation: BAE41642.1. Different initiation. | |
| IPI | IPI00127558. |
| UniGene | Mm.356689 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IS2 based on UniProtKB P07872. |
| SMR | Q9R0H0. Positions 1-655. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9R0H0. |
PTM databases | |
| PhosphoSite | Q9R0H0. |
Proteomic databases | |
| PRIDE | Q9R0H0. |
Genome annotation databases | |
| Ensembl | ENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777; Mus musculus. [Genome view] |
| UCSC | uc007mkm.1. mouse. |
Organism-specific databases | |
| MGI | MGI:1330812. Acox1. |
Phylogenomic databases | |
| HOVERGEN | Q9R0H0. |
Enzyme and pathway databases | |
| BRENDA | 1.3.3.6. 244. |
Gene expression databases | |
| ArrayExpress | Q9R0H0. |
| Bgee | Q9R0H0. |
| CleanEx | MM_ACOX1. MM_PAOX. |
| Genevestigator | Q9R0H0. |
| GermOnline | ENSMUSG00000020777. Mus musculus. |
Family and domain databases | |
| InterPro | IPR006091. Acyl-CoA_Oxase/DH_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view] |
| Gene3D | G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit. |
| PANTHER | PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit. |
| Pfam | PF01756. ACOX. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view] |
| PIRSF | PIRSF000168. Acyl-CoA_oxidase. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | ACOX1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9R0H0 Secondary accession number(s): O35616, Q3TDG0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
