Reviewed, UniProtKB/Swiss-Prot Q9QXD1 (ACOX2_MOUSE)

Names and origin

Protein names

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 names

Name:

Acox2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	681 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxidizes the CoA esters of the bile acid intermediates di- and tri-hyroxycoprostanic acids By similarity.
Catalytic activity	(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.
Cofactor	FAD By similarity.
Subcellular location	Peroxisome By similarity.
Post-translational modification	Acetylation of Lys-667 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity Inferred from electronic annotation. Source: EC FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro acyl-CoA oxidase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 681	681	Peroxisomal acyl-coenzyme A oxidase 2		PRO_0000204682
Regions
	Motif	679 – 681	3	Microbody targeting signal Potential
Amino acid modifications
	Modified residue	417	1	Phosphotyrosine By similarity
	Modified residue	667	1	N6-acetyllysine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9QXD1-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5AE34936AEDA8FF9	FASTA	681	76,893
	10 20 30 40 50 60 MGNPGDRVSL GETWSREVHP DIDSEWHSPS FSVERLTNIL DGGIPNTELR RRVESLIQRD 70 80 90 100 110 120 PVFNLKHLYF MTRDELYEDA VQKRFHLEKL AWSLGWSEDG PERIYADRVL AGYNNLNLHG 130 140 150 160 170 180 IAMNAIRSLG SDEQIAKWGQ LGKNFQIITT YAQTELGHGT YLQGLETEAT YDATTQEFVI 190 200 210 220 230 240 HSPTMTSIKW WPGDLGRTVT HAVVLAHLIC LGARHGMHAF IVPIRSLEDH TPLPGITVGD 250 260 270 280 290 300 IGPKMGFENI DNGFLRLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL 310 320 330 340 350 360 LYKGFLPTLQ KACTIAVRYA VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ LAVSYALHFM 370 380 390 400 410 420 TTSLLQFFHS SYSDILKRDF SLLPELHALS TGMKAMSSDF CAQGTEICRR ACGGHGYSKL 430 440 450 460 470 480 SGLPTLVTQA IASCTYEGEN TVLYLQVARF LMKSYLQAQV SPGSIPQKPL PQSVMYLATP 490 500 510 520 530 540 RPARCPAQTA ADFRCPEVYT TAWAYVSARL IRDATQHTQT LMRSGVDQYD AWNQTSVIHL 550 560 570 580 590 600 QAAKAHCYFL TVRNFKEAVE KLDNEPEIQR VLQNLCDLYA LNGILTNSGD FLHDGFLSGA 610 620 630 640 650 660 QVDMARTAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYQRLF EWAQKSPANT 670 680 QENPAYKKYI RPLMQSWKPK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Amery L., Van Veldhoven P.P. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-667, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ238492 mRNA. Translation: CAB65251.1.
IPI	IPI00134870.
UniGene	Mm.28700
3D structure databases
HSSP	HSSP built from PDB template 1IS2 based on UniProtKB P07872.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QXD1.
PTM databases
PhosphoSite	Q9QXD1.
Proteomic databases
PRIDE	Q9QXD1.
Genome annotation databases
Ensembl	ENSMUST00000022271; ENSMUSP00000022271; ENSMUSG00000021751; Mus musculus. [Genome view]
UCSC	uc007sez.1. mouse.
Organism-specific databases
CTD	93732.
MGI	MGI:1934852. Acox2.
Phylogenomic databases
HOGENOM	Q9QXD1.
HOVERGEN	Q9QXD1.
Enzyme and pathway databases
BRENDA	1.17.99.3. 244.
Gene expression databases
ArrayExpress	Q9QXD1.
Bgee	Q9QXD1.
CleanEx	MM_ACOX2.
Genevestigator	Q9QXD1.
GermOnline	ENSMUSG00000021751. Mus musculus.
Family and domain databases
InterPro	IPR006091. Acyl-CoA_Oxase/DH_M. IPR012258. Acyl-CoA_oxidase. IPR002655. Acyl-CoA_oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHER	PTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	351575.
SOURCE	Search...

Entry information

Entry name

ACOX2_MOUSE

Accession

Primary (citable) accession number: Q9QXD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	May 1, 2000
Last modified:	October 13, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)