Skip Header

Contribute Send feedback
Read comments (?) or add your own

P07872 (ACOX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal acyl-coenzyme A oxidase 1
Short name=AOX
EC=1.3.3.6
Alternative name(s):
Palmitoyl-CoA oxidase

Cleaved into the following 3 chains:

  1. Peroxisomal acyl-CoA oxidase 1, A chain
  2. Peroxisomal acyl-CoA oxidase 1, B chain
  3. Peroxisomal acyl-CoA oxidase 1, C chain
Gene names
Name:Acox1
Synonyms:Acox
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subunit structure

Homodimer. The enzyme contains three components A, B and C, the latter two being produced from the first by a proteolytic cleavage. Ref.4 Ref.5

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation using acyl-CoA oxidase

Inferred from direct assay PubMed 1400324. Source: RGD

generation of precursor metabolites and energy

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome fission

Inferred from electronic annotation. Source: Compara

positive regulation of cholesterol homeostasis

Inferred from electronic annotation. Source: Compara

prostaglandin metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Compara

very long-chain fatty acid metabolic process

Inferred from electronic annotation. Source: Compara

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Compara

peroxisomal membrane

Inferred from electronic annotation. Source: Compara

peroxisome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionFAD binding

Inferred from electronic annotation. Source: Compara

acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

fatty acid binding

Inferred from direct assay PubMed 1400324. Source: RGD

palmitoyl-CoA oxidase activity

Inferred from direct assay PubMed 1400324. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07872-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07872-2)

The sequence of this isoform differs from the canonical sequence as follows:
     90-133: KLYLANFVEP...MRPSQELQII → NSVHRGHPEP...FMPAWNLEIT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Peroxisomal acyl-CoA oxidase 1, A chain
PRO_0000000552
Chain1 – 438438Peroxisomal acyl-CoA oxidase 1, B chain
PRO_0000000553
Chain439 – 661223Peroxisomal acyl-CoA oxidase 1, C chain
PRO_0000000554

Regions

Motif659 – 6613Microbody targeting signal

Sites

Active site4211Proton acceptor Ref.4 Ref.5
Binding site1391FAD
Binding site1781FAD; via amide nitrogen

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue2551N6-acetyllysine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue3101Phosphoserine By similarity
Modified residue4371N6-acetyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue6431N6-acetyllysine By similarity
Modified residue6491Phosphoserine By similarity

Natural variations

Alternative sequence90 – 13344KLYLA…ELQII → NSVHRGHPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LEIT in isoform 2.
VSP_000147

Secondary structure

1 ................................................................................................ 661
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 24B1F10DF066C29E

FASTA66174,679
        10         20         30         40         50         60 
MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY 

        70         80         90        100        110        120 
EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV GLNYSMFIPT LLNQGTTAQQ 

       130        140        150        160        170        180 
EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITQGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL 

       250        260        270        280        290        300 
KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA 

       310        320        330        340        350        360 
IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE TYLRINESIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKIYD QVRSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTMVDINSL 

       490        500        510        520        530        540 
EGLTEAYKLR AARLVEIAAK NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS 

       550        560        570        580        590        600 
DKLPKIQDKA VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR 

       610        620        630        640        650        660 
PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKHLKPLQSK 


L

« Hide

Isoform 2 [UniParc].

Checksum: 23EBDE0CDEE70559
Show »

FASTA66174,691

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase."
Miyazawa S., Hayashi H., Hijikata M., Ishii N., Furuta S., Kagamiyama H., Osumi T., Hashimoto T.
J. Biol. Chem. 262:8131-8137(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"Isolation and structural characterization of the rat acyl-CoA oxidase gene."
Osumi T., Ishii N., Miyazawa S., Hashimoto T.
J. Biol. Chem. 262:8138-8143(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
[4]"Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase."
Nakajima Y., Miyahara I., Hirotsu K., Nishina Y., Shiga K., Setoyama C., Tamaoki H., Miura R.
J. Biochem. 131:365-374(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH A C12-FATTY ACID, SUBUNIT, ACTIVE SITE.
[5]"Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with a fatty acid: insights into substrate-recognition and reactivity toward molecular oxygen."
Tokuoka K., Nakajima Y., Hirotsu K., Miyahara I., Nishina Y., Shiga K., Tamaoki H., Setoyama C., Tojo H., Miura R.
J. Biochem. 139:789-795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), SUBUNIT, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02752 mRNA. Translation: AAA40666.1.
BC085743 mRNA. Translation: AAH85743.1.
J02753 Genomic DNA. Translation: AAA40667.1.
IPIIPI00211510.
IPI00231941.
PIROXRTA1. A29328.
OXRTA2. B29328.
RefSeqNP_059036.1. NM_017340.2.
UniGeneRn.31796.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IS2X-ray2.20A/B1-661[»]
2DDHX-ray2.07A1-661[»]
ProteinModelPortalP07872.
SMRP07872. Positions 1-655.
ModBaseSearch...

Protein-protein interaction databases

IntActP07872. 1 interaction.
MINTMINT-1775779.
STRING10116.ENSRNOP00000042132.

PTM databases

PhosphoSiteP07872.

Proteomic databases

PaxDbP07872.
PRIDEP07872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID50681.
KEGGrno:50681.

Organism-specific databases

CTD51.
RGD619757. Acox1.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000181256.
HOVERGENHBG050451.
KOK00232.
OrthoDBEOG4KWJSB.

Enzyme and pathway databases

SABIO-RKP07872.
UniPathwayUPA00661.

Gene expression databases

ArrayExpressP07872.
GenevestigatorP07872.
GermOnlineENSRNOG00000008755. Rattus norvegicus.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]
PANTHERPTHR10909:SF11. PTHR10909:SF11. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNetSearch...

Other

BindingDBP07872.
ChEMBLCHEMBL4632.
EvolutionaryTraceP07872.
NextBio610520.
PMAP-CutDBP07872.

Entry information

Entry nameACOX1_RAT
AccessionPrimary (citable) accession number: P07872
Secondary accession number(s): P11354
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 3, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents