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Protein

Peroxisomal acyl-coenzyme A oxidase 2

Gene

Acox2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycoprostanic acids.By similarity

Catalytic activityi

(25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestan-26-oyl-CoA + reduced acceptor.

Cofactori

FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal acyl-coenzyme A oxidase 2 (EC:1.17.99.3)
Alternative name(s):
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
Trihydroxycoprostanoyl-CoA oxidase
Short name:
THCA-CoA oxidase
Short name:
THCCox
Gene namesi
Name:Acox2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1934852. Acox2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681Peroxisomal acyl-coenzyme A oxidase 2PRO_0000204682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131PhosphothreonineBy similarity
Modified residuei66 – 661N6-succinyllysineCombined sources
Modified residuei137 – 1371N6-succinyllysineCombined sources
Modified residuei303 – 3031N6-succinyllysineCombined sources
Modified residuei453 – 4531N6-succinyllysineCombined sources
Modified residuei561 – 5611N6-succinyllysineCombined sources
Modified residuei667 – 6671N6-succinyllysineCombined sources

Post-translational modificationi

Acetylation of Lys-667 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QXD1.
MaxQBiQ9QXD1.
PaxDbiQ9QXD1.
PRIDEiQ9QXD1.

PTM databases

iPTMnetiQ9QXD1.
PhosphoSiteiQ9QXD1.

Expressioni

Gene expression databases

BgeeiQ9QXD1.
CleanExiMM_ACOX2.
ExpressionAtlasiQ9QXD1. baseline and differential.
GenevisibleiQ9QXD1. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9QXD1. 2 interactions.
MINTiMINT-1866639.
STRINGi10090.ENSMUSP00000022271.

Structurei

3D structure databases

ProteinModelPortaliQ9QXD1.
SMRiQ9QXD1. Positions 25-675.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi679 – 6813Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00530000062919.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiQ9QXD1.
KOiK10214.
OMAiHEAWNQT.
OrthoDBiEOG7D59MV.
TreeFamiTF300672.

Family and domain databases

Gene3Di1.10.540.10. 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.

Sequencei

Sequence statusi: Complete.

Q9QXD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNPGDRVSL GETWSREVHP DIDSERHSPS FSVERLTNIL DGGIPNTELR
60 70 80 90 100
RRVESLIQRD PVFNLKHLYF MTRDELYEDA VQKRFHLEKL AWSLGWSEDG
110 120 130 140 150
PERIYADRVL AGYNNLNLHG IAMNAIRSLG SDEQIAKWGQ LGKNFQIITT
160 170 180 190 200
YAQTELGHGT YLQGLETEAT YDATTQEFVI HSPTMTSIKW WPGDLGRTVT
210 220 230 240 250
HAVVLAHLIC LGARHGMHAF IVPIRSLEDH TPLPGITVGD IGPKMGFENI
260 270 280 290 300
DNGFLRLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL
310 320 330 340 350
LYKGFLPTLQ KACTIAVRYA VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ
360 370 380 390 400
LAVSYALHFM TTSLLQFFHS SYSDILKRDF SLLPELHALS TGMKAMSSDF
410 420 430 440 450
CAQGTEICRR ACGGHGYSKL SGLPTLVTQA IASCTYEGEN TVLYLQVARF
460 470 480 490 500
LMKSYLQAQV SPGSIPQKPL PQSVMYLATP RPARCPAQTA ADFRCPEVYT
510 520 530 540 550
TAWAYVSARL IRDATQHTQT LMRSGVDQYD AWNQTSVIHL QAAKAHCYFL
560 570 580 590 600
TVRNFKEAVE KLDNEPEIQR VLQNLCDLYA LNGILTNSGD FLHDGFLSGA
610 620 630 640 650
QVDMARTAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYQRLF
660 670 680
EWAQKSPANT QENPAYKKYI RPLMQSWKPK L
Length:681
Mass (Da):76,863
Last modified:July 27, 2011 - v2
Checksum:i32C65231326BA0FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261R → W in CAB65251 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238492 mRNA. Translation: CAB65251.1.
BC021339 mRNA. Translation: AAH21339.1.
CCDSiCCDS36801.1.
RefSeqiNP_001155139.1. NM_001161667.1.
NP_444345.2. NM_053115.2.
XP_006518171.1. XM_006518108.2.
UniGeneiMm.28700.

Genome annotation databases

EnsembliENSMUST00000022271; ENSMUSP00000022271; ENSMUSG00000021751.
ENSMUST00000164598; ENSMUSP00000126464; ENSMUSG00000021751.
GeneIDi93732.
KEGGimmu:93732.
UCSCiuc007sey.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238492 mRNA. Translation: CAB65251.1.
BC021339 mRNA. Translation: AAH21339.1.
CCDSiCCDS36801.1.
RefSeqiNP_001155139.1. NM_001161667.1.
NP_444345.2. NM_053115.2.
XP_006518171.1. XM_006518108.2.
UniGeneiMm.28700.

3D structure databases

ProteinModelPortaliQ9QXD1.
SMRiQ9QXD1. Positions 25-675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QXD1. 2 interactions.
MINTiMINT-1866639.
STRINGi10090.ENSMUSP00000022271.

PTM databases

iPTMnetiQ9QXD1.
PhosphoSiteiQ9QXD1.

Proteomic databases

EPDiQ9QXD1.
MaxQBiQ9QXD1.
PaxDbiQ9QXD1.
PRIDEiQ9QXD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022271; ENSMUSP00000022271; ENSMUSG00000021751.
ENSMUST00000164598; ENSMUSP00000126464; ENSMUSG00000021751.
GeneIDi93732.
KEGGimmu:93732.
UCSCiuc007sey.2. mouse.

Organism-specific databases

CTDi8309.
MGIiMGI:1934852. Acox2.

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00530000062919.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiQ9QXD1.
KOiK10214.
OMAiHEAWNQT.
OrthoDBiEOG7D59MV.
TreeFamiTF300672.

Enzyme and pathway databases

ReactomeiR-MMU-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

ChiTaRSiAcox2. mouse.
NextBioi351575.
PROiQ9QXD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXD1.
CleanExiMM_ACOX2.
ExpressionAtlasiQ9QXD1. baseline and differential.
GenevisibleiQ9QXD1. MM.

Family and domain databases

Gene3Di1.10.540.10. 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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Amery L., Van Veldhoven P.P.
    Submitted (APR-1999) 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.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  4. "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-66; LYS-137; LYS-303; LYS-453; LYS-561 AND LYS-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACOX2_MOUSE
AccessioniPrimary (citable) accession number: Q9QXD1
Secondary accession number(s): Q8VCB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 123 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. 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.