Reviewed, UniProtKB/Swiss-Prot O02767 (ACOX2_RABIT)

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
Synonyms:	THCA

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	681 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids By similarity. Ref.1
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.
Tissue specificity	Liver and kidney.
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
Technical term	Direct protein sequencing
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
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_0000204683
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 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O02767-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 7BF3550F353FB2E3	FASTA	681	76,199
	10 20 30 40 50 60 MGIPVHRVSL GDAWSSRMHP DMESERCAQS FSVERLTNIL DGGAQHTALR RKVESIIHGN 70 80 90 100 110 120 PQFSSKDNYF MSQNELYEAA TRKRYHLQKI AQRMGWTEEG RELEYAHRAL SADLNLNLQG 130 140 150 160 170 180 IFLKALRSLG SEEQIAKWEP LGKTFQIIST YAQTELGHGT YLQGLETEAT YDAATQEFVI 190 200 210 220 230 240 HSPTVTATKW WPGDLGRSAT HALILAQLIC SGARRGMHAF IVPVRSLQDH TPLPGITIGD 250 260 270 280 290 300 IGPKMGLQHI DNGFLKMDHV RVPRENMLSR FAQVLPDGAY IKLGTAQSNY LGMLVTRVHL 310 320 330 340 350 360 LLGAILSPLQ KACVIATRYS VIRHQCRLRP SDPEVKILEH QTQQQKLFPQ LAMCYAFHFL 370 380 390 400 410 420 ATGLLEFFQQ AYKNILDRDF TLLPELHALS TGTKAMMSDF CTQGAEQCRR ACGGHGYSKL 430 440 450 460 470 480 SGLPSLVTSV TASCTYEGEN TVLYLQVARF LVKSCLQAQG FPGSTSQRSL PRSVSYLALP 490 500 510 520 530 540 DLARCPAQTA ADFFCPALYT AAWAHVAARL TKDSVHHLQA LRQSGADEHE AWNQTTIIHL 550 560 570 580 590 600 QAAKAHCYYI SVKSFKEALE KLENEPAIQQ VLKRLCDLHA LHGILTNSGD FLHDGFLSGA 610 620 630 640 650 660 QVDMARTAYM DLLPLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF EWAQRSPTNT 670 680 QENPAYKKYI QPLLQSWRSN L

References

[1]

"Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase from rabbit liver." Pedersen J.J., Eggertsen G., Hellman U., Andersson U., Bjoerkhem I. J. Biol. Chem. 272:18481-18489(1997) [PubMed: 9218493] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION. Strain: New Zealand white. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13279 mRNA. Translation: CAA73728.1.
RefSeq	NP_001076232.1.
UniGene	Ocu.3294
3D structure databases
SMR	O02767. Positions 18-671.
ModBase	Search...
Protein-protein interaction databases
STRING	O02767.
Genome annotation databases
GeneID	100009549.
Organism-specific databases
CTD	100009549.
Phylogenomic databases
eggNOG	maNOG15063.
HOVERGEN	O02767.
Enzyme and pathway databases
BRENDA	1.17.99.3. 255.
Family and domain databases
InterPro	IPR006090. Acyl-CoA_Oxase/DH_1. 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. 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. PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACOX2_RABIT

Accession

Primary (citable) accession number: O02767

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	July 1, 1997
Last modified:	January 19, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)