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Reviewed, UniProtKB/Swiss-Prot P07872 (ACOX1_RAT)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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

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Protein attributes

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

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General annotation (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.

Subunit structure

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

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

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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

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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
Binding site1391FAD
Binding site1781FAD; via amide nitrogen

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue3101Phosphoserine 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...

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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

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Isoform 2.

Checksum: 23EBDE0CDEE70559
Show »

FASTA66174,691

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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: 3036800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [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: 3036801] [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: 11872165] [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: 16672280] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), SUBUNIT, ACTIVE SITE.

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Cross-references

Sequence databases

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.
UniGeneRn.31796

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IS2X-ray2.20A/B1-661[»]
2DDHX-ray2.07A1-661[»]
ModBaseSearch...

PTM databases

PhosphoSiteP07872.

Proteomic databases

PRIDEP07872.

Genome annotation databases

EnsemblENSRNOG00000008755. Rattus norvegicus. [Contig view]
GeneID50681.
KEGGrno:50681.

Organism-specific databases

RGD619757. Acox1.

Phylogenomic databases

HOVERGENP07872.

Enzyme and pathway databases

BRENDA1.3.3.6. 248.

Gene expression databases

ArrayExpressP07872.
GermOnlineENSRNOG00000008755. Rattus norvegicus.

Family and domain databases

InterProIPR006091. 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]
Gene3DG3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio610520.
PMAP-CutDBP07872.

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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: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents