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UniProtKB/Swiss-Prot entry Q5RAU0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACOX3_PONAB
Primary accession number Q5RAU0
Secondary accession numbers None
Integrated into Swiss-Prot on June 12, 2007
Sequence was last modified on December 21, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 23)
Name and origin of the protein
Protein name Peroxisomal acyl-coenzyme A oxidase 3
Synonyms EC 1.3.3.6
Pristanoyl-CoA oxidase
Branched-chain acyl-CoA oxidase
BRCACox
Gene name
Name: ACOX3
From
Pongo abelii (Sumatran orangutan) [TaxID: 9601] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Pongo.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CR858922; CAH91120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001125655.1; -.
3D structure databases
ModBase Q5RAU0.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from InterPro).
GO:0003995; Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997; Molecular function: acyl-CoA oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.
Gene3D G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.
PANTHER PTHR10909:SF11; Acyl-CoA_oxidase; 1.
Pfam PF01756; ACOX; 1.
PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000168; Acyl-CoA_oxidase; 1.
ProtoNet Q5RAU0.
Genome annotation databases
GeneID 100172575; -.
Phylogenomic databases
HOVERGEN Q5RAU0; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   700  700     Peroxisomal acyl-coenzyme A oxidase 3. PRO_0000290353
MOTIF   698   700  3     Microbody targeting signal (By similarity). 
COMPBIAS   340   343  4     Poly-Glu. 
Sequence information
Length: 700 AA [This is the length of the unprocessed precursor] Molecular weight: 77865 Da [This is the MW of the unprocessed precursor] CRC64: C405A0D65A2796E5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MASTVEGGDT ALLPEFPGGP LDAYRARASF SWKELALFTE GEDMLRFKKT IFSALENDPL 

        70         80         90        100        110        120 
FARSPGADLS LEKYRELNFL RCRRIFEYDF LSVEDMFKSP LKVLTLIQCL GMYDSSLAAK 

       130        140        150        160        170        180 
YLIHSLVFGS AIYSSGSERH LTYIQKIFRM EIFGCFALTE LSHGSNTKAI RTTAHYDPAT 

       190        200        210        220        230        240 
EEFIIHSPDF EAAKFWVGNM GKTATHAVVF AKLYVPGDQC HGLHPFIVQI RDSKTLLPMP 

       250        260        270        280        290        300 
GVMVGDIGKK LGQNGLDNGF AMFHKVRVPR QSLLNRMGDV TPEGTYVSSF KDVRQHFGAT 

       310        320        330        340        350        360 
LGSLSWSRVS IVSLAILNLK LAVAIALRFS ATRRQFGPTE EEEIPVLEYP MQQWRLLPYL 

       370        380        390        400        410        420 
AAIYALDHFS KSLFLDLMEL QQGLASGDRS ARQAELGREI HALASASKPL ASWTTQQGIQ 

       430        440        450        460        470        480 
ECREACGGHG YLAMNRLGVL RDDNDPNCTY EGDNNILLQQ TSNYLLGLLA HQVQDGACFR 

       490        500        510        520        530        540 
SPLKSVDFLD AYPGILDQKF EVSSVADCLD SAVALAAYKW LVCYLLRETY QKLNQEKRSG 

       550        560        570        580        590        600 
SSDFEARNKC QVSHGRPLAL AFVELTVVQR FHEHVHQPCV PPSLRAVLGR LSALYALWSL 

       610        620        630        640        650        660 
SRHAALLYRG GYFSGEQAGE VLESAVLALC SQLKDDAVAL VDVIAPPDFI LDSPIGRADG 

       670        680        690        700 
ELYKNLWGAI LQESKALERA SWWPEFSVNK PVIGSLKSKL
Q5RAU0 in FASTA format

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