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P07872

- ACOX1_RAT

UniProt

P07872 - ACOX1_RAT

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Protein
Peroxisomal acyl-coenzyme A oxidase 1
Gene
Acox1, Acox
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Isoform 1 shows optimum activity with a chain length of 10 carbons while isoform 2 exhibits optimum activity with 14 carbons.1 Publication

Catalytic activityi

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

Cofactori

FAD.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391FAD
Binding sitei178 – 1781FAD; via amide nitrogen
Active sitei421 – 4211Proton acceptor2 Publications

GO - Molecular functioni

  1. FAD binding Source: Ensembl
  2. acyl-CoA dehydrogenase activity Source: InterPro
  3. acyl-CoA oxidase activity Source: UniProtKB
  4. fatty acid binding Source: RGD
  5. palmitoyl-CoA oxidase activity Source: RGD

GO - Biological processi

  1. fatty acid beta-oxidation using acyl-CoA oxidase Source: RGD
  2. fatty acid oxidation Source: UniProtKB
  3. generation of precursor metabolites and energy Source: UniProtKB
  4. lipid homeostasis Source: Ensembl
  5. lipid metabolic process Source: UniProtKB
  6. peroxisome fission Source: Ensembl
  7. positive regulation of cholesterol homeostasis Source: Ensembl
  8. prostaglandin metabolic process Source: UniProtKB
  9. spermatogenesis Source: Ensembl
  10. very long-chain fatty acid metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_196408. PPARA activates gene expression.
REACT_198818. alpha-linolenic acid (ALA) metabolism.
SABIO-RKP07872.
UniPathwayiUPA00661.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal acyl-coenzyme A oxidase 1 (EC:1.3.3.6)
Short name:
AOX
Alternative name(s):
Palmitoyl-CoA oxidase
Cleaved into the following 3 chains:
Gene namesi
Name:Acox1
Synonyms:Acox
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619757. Acox1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
  2. peroxisomal membrane Source: Ensembl
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Peroxisomal acyl-CoA oxidase 1, A chain
PRO_0000000552Add
BLAST
Chaini1 – 438438Peroxisomal acyl-CoA oxidase 1, B chain
PRO_0000000553Add
BLAST
Chaini439 – 661223Peroxisomal acyl-CoA oxidase 1, C chain
PRO_0000000554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine By similarity
Modified residuei65 – 651N6-acetyllysine By similarity
Modified residuei89 – 891N6-succinyllysine By similarity
Modified residuei90 – 901N6-succinyllysine By similarity
Modified residuei159 – 1591N6-succinyllysine By similarity
Modified residuei216 – 2161N6-acetyllysine By similarity
Modified residuei241 – 2411N6-succinyllysine By similarity
Modified residuei255 – 2551N6-acetyllysine By similarity
Modified residuei267 – 2671N6-acetyllysine By similarity
Modified residuei272 – 2721N6-acetyllysine By similarity
Modified residuei349 – 3491N6-succinyllysine By similarity
Modified residuei437 – 4371N6-acetyllysine; alternate By similarity
Modified residuei437 – 4371N6-succinyllysine; alternate By similarity
Modified residuei446 – 4461N6-acetyllysine; alternate By similarity
Modified residuei446 – 4461N6-succinyllysine; alternate By similarity
Modified residuei500 – 5001N6-acetyllysine By similarity
Modified residuei512 – 5121N6-acetyllysine; alternate By similarity
Modified residuei512 – 5121N6-succinyllysine; alternate By similarity
Modified residuei542 – 5421N6-succinyllysine By similarity
Modified residuei637 – 6371N6-acetyllysine; alternate By similarity
Modified residuei637 – 6371N6-succinyllysine; alternate By similarity
Modified residuei643 – 6431N6-succinyllysine By similarity
Modified residuei652 – 6521N6-acetyllysine By similarity
Modified residuei655 – 6551N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07872.
PRIDEiP07872.

PTM databases

PhosphoSiteiP07872.

Miscellaneous databases

PMAP-CutDBP07872.

Expressioni

Gene expression databases

GenevestigatoriP07872.

Interactioni

Subunit structurei

Homodimer. The enzyme contains three components A, B and C, the latter two being produced from the first by a proteolytic cleavage.2 Publications

Protein-protein interaction databases

IntActiP07872. 1 interaction.
MINTiMINT-1775779.
STRINGi10116.ENSRNOP00000042132.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119
Helixi16 – 249
Helixi27 – 4115
Helixi44 – 463
Helixi51 – 533
Helixi56 – 7621
Helixi82 – 9312
Helixi101 – 1055
Helixi107 – 1115
Helixi117 – 12812
Beta strandi134 – 1374
Beta strandi143 – 1453
Helixi147 – 1493
Beta strandi153 – 1575
Turni158 – 1614
Beta strandi162 – 1665
Turni170 – 1723
Beta strandi173 – 1753
Turni178 – 1836
Beta strandi185 – 19511
Beta strandi198 – 20811
Turni212 – 2143
Beta strandi221 – 2255
Beta strandi229 – 2313
Beta strandi238 – 24811
Helixi249 – 2513
Helixi279 – 30628
Helixi321 – 3233
Helixi325 – 35329
Turni360 – 3623
Helixi367 – 39529
Helixi398 – 4014
Helixi403 – 4053
Helixi407 – 4148
Helixi415 – 4184
Beta strandi420 – 4223
Helixi424 – 44421
Helixi450 – 4578
Helixi480 – 50930
Helixi512 – 5187
Helixi520 – 54223
Helixi543 – 5453
Helixi549 – 56921
Helixi571 – 5766
Helixi582 – 59918
Helixi600 – 6023
Helixi603 – 6086
Helixi614 – 6174
Helixi628 – 63811
Helixi640 – 6423
Beta strandi643 – 6464
Helixi648 – 6536

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IS2X-ray2.20A/B1-661[»]
2DDHX-ray2.07A1-661[»]
ProteinModelPortaliP07872.
SMRiP07872. Positions 1-655.

Miscellaneous databases

EvolutionaryTraceiP07872.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi659 – 6613Microbody targeting signal

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
KOiK00232.
PhylomeDBiP07872.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR029320. Acyl-CoA_ox_N.
IPR006091. 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_NM_dom.
[Graphical view]
PfamiPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF14749. Acyl-CoA_ox_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P07872-1) [UniParc]FASTAAdd to Basket

Also known as: ACO-I

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.

« Hide

MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED    50
YNFLTRSQRY EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV 100
GLNYSMFIPT LLNQGTTAQQ EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL 150
ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITQGECY 200
GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE 250
NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA 300
IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE 350
TYLRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG 400
YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVRSGKLVGG 450
MVSYLNDLPS QRIQPQQVAV WPTMVDINSL EGLTEAYKLR AARLVEIAAK 500
NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS DKLPKIQDKA 550
VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR 600
PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY 650
HKHLKPLQSK L 661
Length:661
Mass (Da):74,679
Last modified:August 1, 1988 - v1
Checksum:i24B1F10DF066C29E
GO
Isoform 2 (identifier: P07872-2) [UniParc]FASTAAdd to Basket

Also known as: ACO-II

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

Show »
Length:661
Mass (Da):74,691
Checksum:i23EBDE0CDEE70559
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 13344KLYLA…ELQII → NSVHRGHPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LEIT in isoform 2.
VSP_000147Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02752 mRNA. Translation: AAA40666.1.
BC085743 mRNA. Translation: AAH85743.1.
J02753 Genomic DNA. Translation: AAA40667.1.
PIRiA29328. OXRTA1.
B29328. OXRTA2.
RefSeqiNP_059036.1. NM_017340.2. [P07872-1]
UniGeneiRn.31796.

Genome annotation databases

GeneIDi50681.
KEGGirno:50681.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02752 mRNA. Translation: AAA40666.1 .
BC085743 mRNA. Translation: AAH85743.1 .
J02753 Genomic DNA. Translation: AAA40667.1 .
PIRi A29328. OXRTA1.
B29328. OXRTA2.
RefSeqi NP_059036.1. NM_017340.2. [P07872-1 ]
UniGenei Rn.31796.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IS2 X-ray 2.20 A/B 1-661 [» ]
2DDH X-ray 2.07 A 1-661 [» ]
ProteinModelPortali P07872.
SMRi P07872. Positions 1-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P07872. 1 interaction.
MINTi MINT-1775779.
STRINGi 10116.ENSRNOP00000042132.

Chemistry

BindingDBi P07872.
ChEMBLi CHEMBL4632.

PTM databases

PhosphoSitei P07872.

Proteomic databases

PaxDbi P07872.
PRIDEi P07872.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 50681.
KEGGi rno:50681.

Organism-specific databases

CTDi 51.
RGDi 619757. Acox1.

Phylogenomic databases

eggNOGi COG1960.
HOGENOMi HOG000181256.
HOVERGENi HBG050451.
KOi K00232.
PhylomeDBi P07872.

Enzyme and pathway databases

UniPathwayi UPA00661 .
Reactomei REACT_196408. PPARA activates gene expression.
REACT_198818. alpha-linolenic acid (ALA) metabolism.
SABIO-RK P07872.

Miscellaneous databases

EvolutionaryTracei P07872.
NextBioi 610520.
PMAP-CutDB P07872.

Gene expression databases

Genevestigatori P07872.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR029320. Acyl-CoA_ox_N.
IPR006091. 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_NM_dom.
[Graphical view ]
Pfami PF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF14749. Acyl-CoA_ox_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMi SSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).
    Strain: Brown Norway.
    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. "Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities."
    Setoyama C., Tamaoki H., Nishina Y., Shiga K., Miura R.
    Biochem. Biophys. Res. Commun. 217:482-487(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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.
  6. "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.

Entry informationi

Entry nameiACOX1_RAT
AccessioniPrimary (citable) accession number: P07872
Secondary accession number(s): P11354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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