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Q9R0H0 (ACOX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal acyl-coenzyme A oxidase 1
Short name=AOX
EC=1.3.3.6
Alternative name(s):
Palmitoyl-CoA oxidase
Gene names
Name:Acox1
Synonyms:Acox, Paox
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs By similarity.

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Sequence caution

The sequence BAE41642.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Peroxisomal acyl-coenzyme A oxidase 1
PRO_0000204678

Regions

Motif659 – 6613Microbody targeting signal

Sites

Active site4211Proton acceptor By similarity
Binding site1391FAD By similarity
Binding site1781FAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue2551N6-acetyllysine By similarity
Modified residue2671N6-acetyllysine Ref.6
Modified residue3101Phosphoserine Ref.7
Modified residue4371N6-acetyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue6431N6-acetyllysine Ref.6
Modified residue6491Phosphoserine Ref.7
Modified residue6521N6-acetyllysine By similarity

Experimental info

Sequence conflict221I → V in AAB62926. Ref.1
Sequence conflict2631G → D in BAE41642. Ref.5
Sequence conflict5161W → R in BAE41642. Ref.5
Sequence conflict5231L → I in BAE41642. Ref.5
Sequence conflict6481E → Q in AAB62926. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0H0 [UniParc].

Last modified July 27, 2011. Version 5.
Checksum: 4140DB77A4CE7BE6

FASTA66174,649
        10         20         30         40         50         60 
MNPDLRKERA AATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY 

        70         80         90        100        110        120 
EVAVKKSATM VKKMREFGIA DPEEIMWFKK LHMVNFVEPV GLNYSMFIPT LLNQGTTAQQ 

       130        140        150        160        170        180 
EKWMHPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITRGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL 

       250        260        270        280        290        300 
KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGSAA QSLSKACTIA 

       310        320        330        340        350        360 
IRYSAVRRQS EIKRSEPEPQ ILDFQTQQYK LFPLLATAYA FHFLGRYIKE TYMRINESIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKIYD QVQSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTLVDINSL 

       490        500        510        520        530        540 
DSLTEAYKLR AARLVEIAAK NLQAQVSHRK SKEVAWNLTS VDLVRASEAH CHYVTVKVFA 

       550        560        570        580        590        600 
DKLPKIQDRA VQAVLRNLCL LYSLYGISQK GGDFLEGNII TGAQMSQVNS RILELLTVTR 

       610        620        630        640        650        660 
PNAVALVDAF DFKDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY YKHLKPLQSK 


L

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase."
Nohammer C., El-Shabrawi Y., Schauer S., Hiden M., Berger J., Forss-Petter S., Winter E., Eferl R., Zechner R., Hoefler G.
Eur. J. Biochem. 267:1254-1260(2000) [PubMed: 10672038] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Saibara T., Adachi K.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-661.
Strain: NOD.
Tissue: Dendritic cell.
[6]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-643, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-649, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF006688 mRNA. Translation: AAB62926.1.
AB034914 mRNA. Translation: BAA86870.1.
AL669925, AL607108 Genomic DNA. Translation: CAM16381.1.
AL607108, AL669925 Genomic DNA. Translation: CAM24037.1.
CH466558 Genomic DNA. Translation: EDL34562.1.
AK170217 mRNA. Translation: BAE41642.1. Different initiation.
IPIIPI00127558.
UniGeneMm.356689.

3D structure databases

ProteinModelPortalQ9R0H0.
SMRQ9R0H0. Positions 1-655.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9R0H0.

PTM databases

PhosphoSiteQ9R0H0.

Proteomic databases

PRIDEQ9R0H0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777.

Organism-specific databases

MGIMGI:1330812. Acox1.

Phylogenomic databases

GeneTreeENSGT00530000062919.
HOGENOMHBG737904.
HOVERGENHBG050451.
InParanoidQ9R0H0.
PhylomeDBQ9R0H0.

Gene expression databases

ArrayExpressQ9R0H0.
BgeeQ9R0H0.
CleanExMM_ACOX1.
MM_PAOX.
GenevestigatorQ9R0H0.
GermOnlineENSMUSG00000020777. Mus musculus.

Family and domain databases

InterProIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR023570. Acyl-CoA_oxidase_perosiome.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]
Gene3DG3DSA: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.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 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

SOURCESearch...

Entry information

Entry nameACOX1_MOUSE
AccessionPrimary (citable) accession number: Q9R0H0
Secondary accession number(s): A2A850, O35616, Q3TDG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 97 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents