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Q9EPL9

- ACOX3_MOUSE

UniProt

Q9EPL9 - ACOX3_MOUSE

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Protein
Peroxisomal acyl-coenzyme A oxidase 3
Gene
Acox3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Oxidizes the CoA-esters of 2-methyl-branched fatty acids By similarity.

Catalytic activityi

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

Cofactori

FAD By similarity.

Pathwayi

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. pristanoyl-CoA oxidase activity Source: MGI

GO - Biological processi

  1. fatty acid beta-oxidation Source: MGI
  2. fatty acid beta-oxidation using acyl-CoA oxidase Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00661.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1933156. Acox3.

Subcellular locationi

Peroxisome Reviewed prediction

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. peroxisomal matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 700699Peroxisomal acyl-coenzyme A oxidase 3
PRO_0000204686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811Phosphothreonine By similarity
Modified residuei505 – 5051N6-succinyllysine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EPL9.
PaxDbiQ9EPL9.
PRIDEiQ9EPL9.

PTM databases

PhosphoSiteiQ9EPL9.

Expressioni

Gene expression databases

ArrayExpressiQ9EPL9.
BgeeiQ9EPL9.
CleanExiMM_ACOX3.
GenevestigatoriQ9EPL9.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000109876.

Structurei

3D structure databases

ProteinModelPortaliQ9EPL9.
SMRiQ9EPL9. Positions 21-668.

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00530000062919.
HOGENOMiHOG000245077.
HOVERGENiHBG101107.
KOiK00232.
OrthoDBiEOG744T8F.
PhylomeDBiQ9EPL9.
TreeFamiTF314226.

Family and domain databases

Gene3Di2.40.110.10. 1 hit.
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.

Q9EPL9-1 [UniParc]FASTAAdd to Basket

« Hide

MGSLPEEKDS ALWSDTPKGP LSAYRARASF NSGELLLFWD GQDVIHFKKT    50
IFSTLENDPL FARSYGADLP LEKLRELNFL RCKRVFEYGF FKVEELLKNP 100
LKILVLINCL GMYDWSLANK CVLHMLVFGT TVFVSGSEKH FKYLEKIYSL 150
EIFGCFALTE LSHGSNTKAM RTTAHYDPDT QEFILHSPDF EAAKFWVGNL 200
GKTATHAVVF AQLYMPDGQC HGLHSFLVQI RDTKTLLPMT GVMVGDIGKK 250
LGQNGLDNGF AMFNKVRIPR QNLLDRTGNI TSEGTYNSPF KDVRQRLGAS 300
LGSLSSGRIS IISMSVVNLK LAVSIAIRFS ATRCQFGPTD KEEIPVLEYP 350
LQQWRILPYL AAAYALDHFS KTIFMDLIEV QSARLRGDHS DQQAELGREI 400
HALASAGKPL ASWTAQRGIQ ECREACGGHG YLAMNRFGDL RNDNDPNCTY 450
EGDNNVLLQQ TSNYLLSLLE PPLQDGAHFT SPLKTVDFLE AYPGILGQKF 500
LGSSKADWMD SAAPLAAYRW LVCYLLQESH RRYCQEKKSR GSDFEARNNS 550
QVYGCRPLAL AFMELTVMQR FHEHIHSSGL SPSLRTVLGR LSTLYGLWCL 600
SQHMALLYRG GYISGEQTGR AMEDAILTLC EQLKDDAVAL VDVIAPSDFV 650
LNSPIAKADG ELYKNLWAAV LQQNGVLERA AWWPEFSANK SVADRLKSQL 700
Length:700
Mass (Da):78,404
Last modified:February 20, 2007 - v2
Checksum:i85C448E38A4A0C67
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1782DP → ES in CAC20692. 1 Publication
Sequence conflicti364 – 3641Y → H in CAC20692. 1 Publication
Sequence conflicti408 – 4092KP → NR in CAC20692. 1 Publication
Sequence conflicti555 – 5551C → V in CAC20692. 1 Publication
Sequence conflicti576 – 5761H → Y in AAH44725. 1 Publication
Sequence conflicti593 – 5942TL → SV in CAC20692. 1 Publication
Sequence conflicti607 – 6071L → S in CAC20692. 1 Publication
Sequence conflicti669 – 6691A → R in CAC20692. 1 Publication
Sequence conflicti681 – 6811A → R in CAC20692. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ278430 mRNA. Translation: CAC20692.1.
BC044725 mRNA. Translation: AAH44725.1.
BC055019 mRNA. Translation: AAH55019.1.
CCDSiCCDS19232.1.
RefSeqiNP_109646.2. NM_030721.2.
XP_006504261.1. XM_006504198.1.
UniGeneiMm.291503.

Genome annotation databases

EnsembliENSMUST00000068947; ENSMUSP00000063412; ENSMUSG00000029098.
ENSMUST00000114237; ENSMUSP00000109875; ENSMUSG00000029098.
GeneIDi80911.
KEGGimmu:80911.
UCSCiuc008xdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ278430 mRNA. Translation: CAC20692.1 .
BC044725 mRNA. Translation: AAH44725.1 .
BC055019 mRNA. Translation: AAH55019.1 .
CCDSi CCDS19232.1.
RefSeqi NP_109646.2. NM_030721.2.
XP_006504261.1. XM_006504198.1.
UniGenei Mm.291503.

3D structure databases

ProteinModelPortali Q9EPL9.
SMRi Q9EPL9. Positions 21-668.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000109876.

PTM databases

PhosphoSitei Q9EPL9.

Proteomic databases

MaxQBi Q9EPL9.
PaxDbi Q9EPL9.
PRIDEi Q9EPL9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068947 ; ENSMUSP00000063412 ; ENSMUSG00000029098 .
ENSMUST00000114237 ; ENSMUSP00000109875 ; ENSMUSG00000029098 .
GeneIDi 80911.
KEGGi mmu:80911.
UCSCi uc008xdx.1. mouse.

Organism-specific databases

CTDi 8310.
MGIi MGI:1933156. Acox3.

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00530000062919.
HOGENOMi HOG000245077.
HOVERGENi HBG101107.
KOi K00232.
OrthoDBi EOG744T8F.
PhylomeDBi Q9EPL9.
TreeFami TF314226.

Enzyme and pathway databases

UniPathwayi UPA00661 .

Miscellaneous databases

NextBioi 350282.
PROi Q9EPL9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9EPL9.
Bgeei Q9EPL9.
CleanExi MM_ACOX3.
Genevestigatori Q9EPL9.

Family and domain databases

Gene3Di 2.40.110.10. 1 hit.
InterProi IPR006091. 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 ]
Pfami PF01756. ACOX. 1 hit.
PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 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. "Cloning of the mouse pristanoyl-CoA oxidase."
    Van Veldhoven P.P., Ghys K.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N and FVB/N-3.
    Tissue: Liver and Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACOX3_MOUSE
AccessioniPrimary (citable) accession number: Q9EPL9
Secondary accession number(s): Q7TPP6, Q80UQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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