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P97562 (ACOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:Thcox
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length681 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Tissue specificity

Most abundant in liver. Also expressed in kidney. Not present in any other tissues tested.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 681681Peroxisomal acyl-coenzyme A oxidase 2
PRO_0000204684

Regions

Motif679 – 6813Microbody targeting signal Potential

Amino acid modifications

Modified residue31Phosphoserine Ref.2
Modified residue6671N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P97562 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 3599D71365D38932

FASTA68176,799
        10         20         30         40         50         60 
MGSPMHRVSL GDHWSWQVHP DIDSERHSPS FSVERLTNIL DGGLPNTVLR RKVESIIQSD 

        70         80         90        100        110        120 
PVFNLKKLYF MTREELYEDA IQKRFHLEKL AWSLGWSEDG PERIYANRVL DGNVNLSLHG 

       130        140        150        160        170        180 
VAMNAIRSLG SDEQIAKWGQ LCKNFQIITT YAQTELGHGT YLQGLETEAT YDEARQELVI 

       190        200        210        220        230        240 
HSPTMTSTKW WPGDLGWSVT HAVVLAQLTC LGVRHGMHAF IVPIRSLEDH TPLPGITVGD 

       250        260        270        280        290        300 
IGPKMGLEHI DNGFLQLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL 

       310        320        330        340        350        360 
LCKGILPSLQ KACIIATRYS VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ LAVSYAFHFT 

       370        380        390        400        410        420 
ATSLSEFFHS SYSAILKRDF SLLPELHALS TGMKATFADF CAQGAEICRR ACGGHGYSKL 

       430        440        450        460        470        480 
SGLPTLVARA TASCTYEGEN TVLYLQVARF LMKSYLQAQA SPGATPQKPL PQSVMYIATQ 

       490        500        510        520        530        540 
RPARCSAQTA ADFRCPDVYT TAWAYVSTRL IRDAAHRTQT LMKSGVDQHD AWNQTTVIHL 

       550        560        570        580        590        600 
QAAKAHCYFI TVKNFKEAVE KLDKEPEIQR VLQRLCDLYA LHGVLTNSGD FLHDGFLSGA 

       610        620        630        640        650        660 
QVDMAREAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYERLF EWAQKYPANT 

       670        680 
QENPAYKKYI RPLMLGWRHK M

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and further characterization of rat peroxisomal trihydroxycoprostanoyl-CoA oxidase."
Baumgart E., Vanhooren J.C.T., Fransen M., Van Leuven F., Fahimi H.D., Van Veldhoven P.P., Mannaerts G.P.
Biochem. J. 320:115-121(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-33; 74-83; 128-137; 265-270; 328-336; 454-464 AND 656-667, FUNCTION.
Tissue: Liver.
[2]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
Strain: Fischer.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X95189 mRNA. Translation: CAA64488.1.
IPIIPI00205561.
UniGeneRn.10622.

3D structure databases

ProteinModelPortalP97562.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010260.

PTM databases

PhosphoSiteP97562.

Proteomic databases

PaxDbP97562.
PRIDEP97562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD628684. Acox2.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000181256.
HOVERGENHBG050451.
InParanoidP97562.
OrthoDBEOG46143J.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14328.
BRENDA1.17.99.3. 5301.

Gene expression databases

ArrayExpressP97562.
GenevestigatorP97562.
GermOnlineENSRNOG00000007378. Rattus norvegicus.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006091. 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.
[Graphical view]
PANTHERPTHR10909:SF11. PTHR10909:SF11. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMSSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNetSearch...

Other

NextBio624023.

Entry information

Entry nameACOX2_RAT
AccessionPrimary (citable) accession number: P97562
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 1997
Last modified: May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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