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
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.By similarity1 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

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

BRENDAi1.17.99.3. 1749.

Chemistry databases

SwissLipidsiSLP:000001293.

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:THCA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002046831 – 681Peroxisomal acyl-coenzyme A oxidase 2Add BLAST681

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineBy similarity1
Modified residuei66N6-succinyllysineBy similarity1
Modified residuei137N6-succinyllysineBy similarity1
Modified residuei453N6-succinyllysineBy similarity1
Modified residuei561N6-succinyllysineBy similarity1
Modified residuei667N6-succinyllysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO02767.

Expressioni

Tissue specificityi

Liver and kidney.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000016578.

Structurei

3D structure databases

ProteinModelPortaliO02767.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi679 – 681Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiO02767.
KOiK10214.

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.

O02767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIPVHRVSL GDAWSSRMHP DMESERCAQS FSVERLTNIL DGGAQHTALR
60 70 80 90 100
RKVESIIHGN PQFSSKDNYF MSQNELYEAA TRKRYHLQKI AQRMGWTEEG
110 120 130 140 150
RELEYAHRAL SADLNLNLQG IFLKALRSLG SEEQIAKWEP LGKTFQIIST
160 170 180 190 200
YAQTELGHGT YLQGLETEAT YDAATQEFVI HSPTVTATKW WPGDLGRSAT
210 220 230 240 250
HALILAQLIC SGARRGMHAF IVPVRSLQDH TPLPGITIGD IGPKMGLQHI
260 270 280 290 300
DNGFLKMDHV RVPRENMLSR FAQVLPDGAY IKLGTAQSNY LGMLVTRVHL
310 320 330 340 350
LLGAILSPLQ KACVIATRYS VIRHQCRLRP SDPEVKILEH QTQQQKLFPQ
360 370 380 390 400
LAMCYAFHFL ATGLLEFFQQ AYKNILDRDF TLLPELHALS TGTKAMMSDF
410 420 430 440 450
CTQGAEQCRR ACGGHGYSKL SGLPSLVTSV TASCTYEGEN TVLYLQVARF
460 470 480 490 500
LVKSCLQAQG FPGSTSQRSL PRSVSYLALP DLARCPAQTA ADFFCPALYT
510 520 530 540 550
AAWAHVAARL TKDSVHHLQA LRQSGADEHE AWNQTTIIHL QAAKAHCYYI
560 570 580 590 600
SVKSFKEALE KLENEPAIQQ VLKRLCDLHA LHGILTNSGD FLHDGFLSGA
610 620 630 640 650
QVDMARTAYM DLLPLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF
660 670 680
EWAQRSPTNT QENPAYKKYI QPLLQSWRSN L
Length:681
Mass (Da):76,199
Last modified:July 1, 1997 - v1
Checksum:i7BF3550F353FB2E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13279 mRNA. Translation: CAA73728.1.
RefSeqiNP_001076232.1. NM_001082763.1.
UniGeneiOcu.3294.

Genome annotation databases

GeneIDi100009549.
KEGGiocu:100009549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13279 mRNA. Translation: CAA73728.1.
RefSeqiNP_001076232.1. NM_001082763.1.
UniGeneiOcu.3294.

3D structure databases

ProteinModelPortaliO02767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000016578.

Chemistry databases

SwissLipidsiSLP:000001293.

Proteomic databases

PRIDEiO02767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009549.
KEGGiocu:100009549.

Organism-specific databases

CTDi8309.

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiO02767.
KOiK10214.

Enzyme and pathway databases

BRENDAi1.17.99.3. 1749.

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...

Entry informationi

Entry nameiACOX2_RABIT
AccessioniPrimary (citable) accession number: O02767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 1, 1997
Last modified: October 5, 2016
This is version 102 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.