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P07872

- ACOX1_RAT

UniProt

P07872 - ACOX1_RAT

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Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

Acox1

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

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. acyl-CoA dehydrogenase activity Source: InterPro
  2. acyl-CoA oxidase activity Source: UniProtKB
  3. FAD binding Source: Ensembl
  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.
REACT_256178. Beta-oxidation of very long chain fatty acids.
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 chainPRO_0000000552Add
BLAST
Chaini1 – 438438Peroxisomal acyl-CoA oxidase 1, B chainPRO_0000000553Add
BLAST
Chaini439 – 661223Peroxisomal acyl-CoA oxidase 1, C chainPRO_0000000554Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07872.
PRIDEiP07872.

PTM databases

PhosphoSiteiP07872.

Miscellaneous databases

PMAP-CutDBP07872.

Expressioni

Gene expression databases

ExpressionAtlasiP07872. baseline.
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

1
661
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi16 – 249Combined sources
Helixi27 – 4115Combined sources
Helixi44 – 463Combined sources
Helixi51 – 533Combined sources
Helixi56 – 7621Combined sources
Helixi82 – 9312Combined sources
Helixi101 – 1055Combined sources
Helixi107 – 1115Combined sources
Helixi117 – 12812Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi143 – 1453Combined sources
Helixi147 – 1493Combined sources
Beta strandi153 – 1575Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 1665Combined sources
Turni170 – 1723Combined sources
Beta strandi173 – 1753Combined sources
Turni178 – 1836Combined sources
Beta strandi185 – 19511Combined sources
Beta strandi198 – 20811Combined sources
Turni212 – 2143Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi238 – 24811Combined sources
Helixi249 – 2513Combined sources
Helixi279 – 30628Combined sources
Helixi321 – 3233Combined sources
Helixi325 – 35329Combined sources
Turni360 – 3623Combined sources
Helixi367 – 39529Combined sources
Helixi398 – 4014Combined sources
Helixi403 – 4053Combined sources
Helixi407 – 4148Combined sources
Helixi415 – 4184Combined sources
Beta strandi420 – 4223Combined sources
Helixi424 – 44421Combined sources
Helixi450 – 4578Combined sources
Helixi480 – 50930Combined sources
Helixi512 – 5187Combined sources
Helixi520 – 54223Combined sources
Helixi543 – 5453Combined sources
Helixi549 – 56921Combined sources
Helixi571 – 5766Combined sources
Helixi582 – 59918Combined sources
Helixi600 – 6023Combined sources
Helixi603 – 6086Combined sources
Helixi614 – 6174Combined sources
Helixi628 – 63811Combined sources
Helixi640 – 6423Combined sources
Beta strandi643 – 6464Combined sources
Helixi648 – 6536Combined sources

3D structure databases

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

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.Curated

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiP07872.
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

        10         20         30         40         50
MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED
60 70 80 90 100
YNFLTRSQRY EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV
110 120 130 140 150
GLNYSMFIPT LLNQGTTAQQ EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL
160 170 180 190 200
ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITQGECY
210 220 230 240 250
GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE
260 270 280 290 300
NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA
310 320 330 340 350
IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE
360 370 380 390 400
TYLRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG
410 420 430 440 450
YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVRSGKLVGG
460 470 480 490 500
MVSYLNDLPS QRIQPQQVAV WPTMVDINSL EGLTEAYKLR AARLVEIAAK
510 520 530 540 550
NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS DKLPKIQDKA
560 570 580 590 600
VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR
610 620 630 640 650
PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY
660
HKHLKPLQSK L
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. 1 PublicationVSP_000147Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P07872.
KOi K00232.
PhylomeDBi P07872.

Enzyme and pathway databases

UniPathwayi UPA00661 .
Reactomei REACT_196408. PPARA activates gene expression.
REACT_198818. alpha-linolenic acid (ALA) metabolism.
REACT_256178. Beta-oxidation of very long chain fatty acids.
SABIO-RK P07872.

Miscellaneous databases

EvolutionaryTracei P07872.
NextBioi 610520.
PMAP-CutDB P07872.

Gene expression databases

ExpressionAtlasi P07872. baseline.
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: November 26, 2014
This is version 144 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