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Protein

Peroxisomal acyl-coenzyme A oxidase 3

Gene

Acox3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes the CoA-esters of 2-methyl-branched fatty acids.1 Publication

Catalytic activityi

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

Cofactori

Pathwayi: peroxisomal fatty acid beta-oxidation

This protein is involved in the pathway peroxisomal fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway peroxisomal fatty acid beta-oxidation and in Lipid metabolism.

GO - Molecular functioni

  • acyl-CoA dehydrogenase activity Source: InterPro
  • fatty acid binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • pristanoyl-CoA oxidase activity Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation using acyl-CoA oxidase Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKQ63448.
UniPathwayiUPA00661.

Chemistry

SwissLipidsiSLP:000000545.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal acyl-coenzyme A oxidase 3 (EC:1.3.3.6)
Alternative name(s):
Branched-chain acyl-CoA oxidase
Short name:
BRCACox
Pristanoyl-CoA oxidase
Gene namesi
Name:Acox3
Synonyms:Prcox
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69245. Acox3.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 700699Peroxisomal acyl-coenzyme A oxidase 3PRO_0000204687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei281 – 2811PhosphothreonineBy similarity
Modified residuei505 – 5051N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63448.
PRIDEiQ63448.

PTM databases

iPTMnetiQ63448.
PhosphoSiteiQ63448.

Expressioni

Tissue specificityi

Most abundant in liver, kidney, lung, and testis. Present in all tissues tested.

Interactioni

Protein-protein interaction databases

IntActiQ63448. 1 interaction.
STRINGi10116.ENSRNOP00000042002.

Structurei

3D structure databases

ProteinModelPortaliQ63448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi698 – 7003Microbody targeting signal

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000245077.
HOVERGENiHBG101107.
InParanoidiQ63448.
KOiK00232.
PhylomeDBiQ63448.

Family and domain databases

InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF01756. ACOX. 1 hit.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q63448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSSERRDS VLWSDIPKGP LSAYRARASF NSKELMLFWD GQDVLDFKKT
60 70 80 90 100
IFSTLENDPL FARPFGADLP LEKERELNFL RCKRVFEYGF FNAEDMLKNP
110 120 130 140 150
LKILVLMNCL GMYDWSLANK CVLHMLVFGS TIIGSGSEHH FKYLEKIYNL
160 170 180 190 200
EIFGCFALTE LSHGSNTKAM RTTAHYDPAT QEFILHSPDF EAAKFWVGNL
210 220 230 240 250
GKTATHAVVF AQLYTPDGQC RGLHSFLVQI RDPKTLLPMP GVMVGDMGKK
260 270 280 290 300
LGQNGLDNGF AMFHKVRIPR QNLLDRTGNV TSEGHYHTPF KDVRQRLGAS
310 320 330 340 350
LGSLSSGRIS IISISVVNLK LAVIIAIRFS ATRRQFGPTD KEEIPVLEYP
360 370 380 390 400
LQQWRLLPYL AAAYALDHFS KTIFLDLIEL QRAGKVGTTV TGRQSSGREI
410 420 430 440 450
HALASAGKPL ASWTAQRGIQ ECREVVGGHG YLAMNRFGEL RNDNDPNCTY
460 470 480 490 500
EGDNNVLLQQ TSNYLLSLLE HPLQDGAHFT SPLKTVNFLE AYPGILGQKF
510 520 530 540 550
MASSKADWLD SEAPLAAYRW LVCYLLRESH QRYCQEKKSR GSDFEARNNS
560 570 580 590 600
QVYGCRPLAL AFMELTVMQR FHEHTHSSSV PPSLRTVLGR LSMLYGLWCL
610 620 630 640 650
SQHTALLYRG GYISGEQTGK AMEDAILMLC VQLKDDAVAL VDAIAPSDFV
660 670 680 690 700
LGSPIGRADG ELYKNLWAAV LQQSGVLERA AWWPEFTANK SVANRLKSQL
Length:700
Mass (Da):78,446
Last modified:November 1, 1997 - v1
Checksum:iDE2327CEFA7423DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95188 mRNA. Translation: CAA64487.1.
RefSeqiNP_445791.1. NM_053339.1.
UniGeneiRn.10546.

Genome annotation databases

GeneIDi83522.
KEGGirno:83522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95188 mRNA. Translation: CAA64487.1.
RefSeqiNP_445791.1. NM_053339.1.
UniGeneiRn.10546.

3D structure databases

ProteinModelPortaliQ63448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63448. 1 interaction.
STRINGi10116.ENSRNOP00000042002.

Chemistry

SwissLipidsiSLP:000000545.

PTM databases

iPTMnetiQ63448.
PhosphoSiteiQ63448.

Proteomic databases

PaxDbiQ63448.
PRIDEiQ63448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83522.
KEGGirno:83522.

Organism-specific databases

CTDi8310.
RGDi69245. Acox3.

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000245077.
HOVERGENiHBG101107.
InParanoidiQ63448.
KOiK00232.
PhylomeDBiQ63448.

Enzyme and pathway databases

UniPathwayiUPA00661.
SABIO-RKQ63448.

Miscellaneous databases

NextBioi615999.
PROiQ63448.

Family and domain databases

InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF01756. ACOX. 1 hit.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat pristanoyl-CoA oxidase. cDNA cloning and recognition of its C-terminal (SQL) by the peroxisomal-targeting signal 1 receptor."
    Vanhooren J.C.T., Fransen M., de Bethune B., Baumgart E., Baes M., Torrekens S., van Leuven F., Mannaerts G.P., van Veldhoven P.P.
    Eur. J. Biochem. 239:302-309(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    Tissue: Liver.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACOX3_RAT
AccessioniPrimary (citable) accession number: Q63448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 113 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.