Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisomal acyl-coenzyme A oxidase 2

Gene

Acox2

Organism
Rattus norvegicus (Rat)
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.1 Publication

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

  • 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity Source: RGD
  • acyl-CoA dehydrogenase activity Source: InterPro
  • acyl-CoA oxidase activity Source: InterPro
  • fatty acid binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
  • fatty acid metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14328.
BRENDAi1.17.99.3. 5301.

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
Synonyms:Thcox
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628684. Acox2.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681Peroxisomal acyl-coenzyme A oxidase 2PRO_0000204684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineCombined sources
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei66 – 661N6-succinyllysineBy similarity
Modified residuei137 – 1371N6-succinyllysineBy similarity
Modified residuei303 – 3031N6-succinyllysineBy similarity
Modified residuei453 – 4531N6-succinyllysineBy similarity
Modified residuei561 – 5611N6-succinyllysineBy similarity
Modified residuei667 – 6671N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP97562.
PRIDEiP97562.

PTM databases

iPTMnetiP97562.
PhosphoSiteiP97562.

Expressioni

Tissue specificityi

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

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010260.

Structurei

3D structure databases

ProteinModelPortaliP97562.
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.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiP97562.
PhylomeDBiP97562.

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.

P97562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSPMHRVSL GDHWSWQVHP DIDSERHSPS FSVERLTNIL DGGLPNTVLR
60 70 80 90 100
RKVESIIQSD PVFNLKKLYF MTREELYEDA IQKRFHLEKL AWSLGWSEDG
110 120 130 140 150
PERIYANRVL DGNVNLSLHG VAMNAIRSLG SDEQIAKWGQ LCKNFQIITT
160 170 180 190 200
YAQTELGHGT YLQGLETEAT YDEARQELVI HSPTMTSTKW WPGDLGWSVT
210 220 230 240 250
HAVVLAQLTC LGVRHGMHAF IVPIRSLEDH TPLPGITVGD IGPKMGLEHI
260 270 280 290 300
DNGFLQLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL
310 320 330 340 350
LCKGILPSLQ KACIIATRYS VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ
360 370 380 390 400
LAVSYAFHFT ATSLSEFFHS SYSAILKRDF SLLPELHALS TGMKATFADF
410 420 430 440 450
CAQGAEICRR ACGGHGYSKL SGLPTLVARA TASCTYEGEN TVLYLQVARF
460 470 480 490 500
LMKSYLQAQA SPGATPQKPL PQSVMYIATQ RPARCSAQTA ADFRCPDVYT
510 520 530 540 550
TAWAYVSTRL IRDAAHRTQT LMKSGVDQHD AWNQTTVIHL QAAKAHCYFI
560 570 580 590 600
TVKNFKEAVE KLDKEPEIQR VLQRLCDLYA LHGVLTNSGD FLHDGFLSGA
610 620 630 640 650
QVDMAREAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYERLF
660 670 680
EWAQKYPANT QENPAYKKYI RPLMLGWRHK M
Length:681
Mass (Da):76,799
Last modified:May 1, 1997 - v1
Checksum:i3599D71365D38932
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95189 mRNA. Translation: CAA64488.1.
UniGeneiRn.10622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95189 mRNA. Translation: CAA64488.1.
UniGeneiRn.10622.

3D structure databases

ProteinModelPortaliP97562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010260.

PTM databases

iPTMnetiP97562.
PhosphoSiteiP97562.

Proteomic databases

PaxDbiP97562.
PRIDEiP97562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi628684. Acox2.

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiP97562.
PhylomeDBiP97562.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14328.
BRENDAi1.17.99.3. 5301.

Miscellaneous databases

PROiP97562.

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. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACOX2_RAT
AccessioniPrimary (citable) accession number: P97562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.