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UniProtKB/Swiss-Prot entry O54754

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

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Entry information
Entry name ADO_MOUSE
Primary accession number O54754
Secondary accession numbers Q9WU85 Q9Z2Z5
Integrated into Swiss-Prot on May 15, 2002
Sequence was last modified on May 1, 1999 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name Aldehyde oxidase
Synonyms EC 1.2.3.1
Retinal oxidase
Gene name
Name: Aox1
Synonyms: Ao, Ro
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=CD-1;
TISSUE=Liver;
DOI=10.1042/0264-6021:3410071; PubMed=10377246 [NCBI, ExPASy, EBI, Israel, Japan]
Kurosaki M., Demontis S., Barzago M.M., Garattini E., Terao M.;
"Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone.";
Biochem. J. 341:71-80(1999).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA;
TISSUE=Liver;
DOI=10.1006/abbi.1999.1129; PubMed=10190983 [NCBI, ExPASy, EBI, Israel, Japan]
Huang D.-Y., Furukawa A., Ichikawa Y.;
"Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli.";
Arch. Biochem. Biophys. 364:264-272(1999).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
STRAIN=129/Sv;
TISSUE=Thymus;
DOI=10.1016/S0167-4781(99)00174-8; PubMed=10673024 [NCBI, ExPASy, EBI, Israel, Japan]
Demontis S., Kurosaki M., Saccone S., Salvatore M., Garattini E., Terao M.;
"The mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping and functional characterization of the 5'-flanking region.";
Biochim. Biophys. Acta 1489:207-222(1999).
[4]
 NUCLEOTIDE SEQUENCE OF 561-746, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
TISSUE=Liver;
PubMed=9243637 [NCBI, ExPASy, EBI, Israel, Japan]
Bendotti C., Prosperini E., Kurosaki M., Garattini E., Terao M.;
"Selective localization of mouse aldehyde oxidase mRNA in the choroid plexus and motor neurons.";
NeuroReport 8:2343-2349(1997).
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
AF076216; AAC99382.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB017482; BAA36834.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121945; AAD31763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121911; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121912; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121913; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121914; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121915; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121916; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121917; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121918; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121919; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121920; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121921; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121922; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121923; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121924; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121925; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121926; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121927; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121928; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121929; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121930; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121931; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121932; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121933; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121934; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121935; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121936; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121937; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121938; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121939; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121940; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121941; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121942; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121943; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF121944; AAD31763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_033806.2; -.
UniGene Mm.26787
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase O54754.
Organism-specific databases
MGI MGI:88035; Aox1.
Gene expression databases
ArrayExpress O54754; -.
CleanEx MM_AOX1; -.
GermOnline ENSMUSG00000063558; Mus musculus.
Ontologies
GO
GO:0004031; Molecular function: aldehyde oxidase activity (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR016208; Ald_Oxase/xanthine_DHase.
IPR014313; Aldehyde_oxidase.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR012675; b-grasp_ferredoxin-like.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR001041; Ferredoxin.
IPR002346; Mopterin_DHase_FAD-bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02969; mam_aldehyde_ox; 1.
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS O54754.
Genome annotation databases
Ensembl ENSMUSG00000063558; Mus musculus. [Contig view]
GeneID 11761; -.
KEGG mmu:11761; -.
Phylogenomic databases
HOGENOM O54754; -.
HOVERGEN O54754; -.
Other
SOURCE Aox1; Mus musculus.
ProtoNet O54754.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1333  1333     Aldehyde oxidase. PRO_0000166106
DOMAIN   4     91  88     2Fe-2S ferredoxin-type. 
DOMAIN   235    420  186     FAD-binding PCMH-type. 
METAL   43     43        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   48     48        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   51     51        Iron-sulfur (2Fe-2S) (By similarity). 
VARIANT   109    109  1     H -> Q (in strain: 129/Sv). 
VARIANT   168    168  1     A -> G (in strain: C57BL/6 X CBA and 129/Sv). 
VARIANT   449    449  1     R -> T (in strain: C57BL/6 X CBA). 
VARIANT   492    492  1     R -> A (in strain: C57BL/6 X CBA). 
VARIANT   686    687  2     KQ -> NE (in strain: 129/Sv). 
VARIANT   857    857  1     E -> D (in strain: 129/Sv). 
VARIANT   983    983  1     E -> D (in strain: C57BL/6 X CBA). 
VARIANT   1169   1169  1     N -> D (in strain: C57BL/6 X CBA and 129/Sv). 
VARIANT   1329   1329  1     C -> W (in strain: C57BL/6 X CBA and 129/Sv). 
Sequence information
Length: 1333 AA [This is the length of the unprocessed precursor] Molecular weight: 146678 Da [This is the MW of the unprocessed precursor] CRC64: 320CF0A3742F6AC5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDPIQLLFYV NGQKVVEKNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP 

        70         80         90        100        110        120 
STKAIRHHPV NACLTPICSL HGTAVTTVEG LGNTRTRLHP IQERIAKCHG TQCGFCTPGM 

       130        140        150        160        170        180 
VMSMYALLRN HPEPTLDQLT DALGGNLCRC TGYRPIIDAC KTFCKASACC QSKENGVCCL 

       190        200        210        220        230        240 
DQEINGLAES QEEDKTSPEL FSEEEFLPLD PTQELIFPPE LMRIAEKQPP KTRVFYGERV 

       250        260        270        280        290        300 
TWISPVTLKE LVEAKFKYPQ APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELGVISQAR 

       310        320        330        340        350        360 
DGLTLGAGLS LDQVKDILAD IVQKLPEEKT QTYRALLKHL RTLAGSQIRN MASLGGHIVS 

       370        380        390        400        410        420 
RHLDSDLNPL LAVGNCTLNL LSKDGERRIP LSEEFLRKCP EADLKPQEVL VSVNIPWSRK 

       430        440        450        460        470        480 
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIEELSI LYGGVGSTII SAKNSCQRLI 

       490        500        510        520        530        540 
GRPWNEGMLD TRCRLVLDEV TLAASAPGGK VEFKRTLIIS FLFKFYLEVS QGLKREDPGH 

       550        560        570        580        590        600 
SPSLAGNHES ALDDLHSKHP WRTLTHQNVD PAQLPQDPIG RPIMHLSGIK HATGEAIYCD 

       610        620        630        640        650        660 
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQEAN TFGTETFLAT 

       670        680        690        700        710        720 
DEVHCVGHLV CAVIADSETR AKQAAKQVKV VYQDLAPLIL TIEEAIQHKS FFKSERKLEC 

       730        740        750        760        770        780 
GNVDEAFKIV DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKYIQDIV 

       790        800        810        820        830        840 
AATLKLSANK VMCHVRRVGG AFGGKVGKTS ILAAITAFAA SKHGRAVRCI LERGEDMLIT 

       850        860        870        880        890        900 
GGRHPYLGKY KAGFMNEGRI LALDVEHYCN GGCSLDESLW VIEMGLLKLD NAYKFPNLRC 

       910        920        930        940        950        960 
RGWACRTNLP SNTALRGFGF PQAGLVTEAC ITEVAIKCGL SPEQVRTINM YKHVDTTHYK 

       970        980        990       1000       1010       1020 
QEFSAKALSE CWRECMAKCS YFERKAAIGK FNAENSWKKR GMAVIPLKFP VGIGSVAMGQ 

      1030       1040       1050       1060       1070       1080 
AAALVHIYLD GSALVSHGGI EMGQGVHTKM IQVVSRELRM PMSSVHLRGT STETVPNTNA 

      1090       1100       1110       1120       1130       1140 
SGGSVVADLN GLAVKDACQT LLKRLEPIIS KNPQGTWKDW AQTAFDQSIS LSAVGYFRGY 

      1150       1160       1170       1180       1190       1200 
ESNIDWEKGE GHPFEYFVFG AACSEVEINC LTGDHKNIRT NIVMDVGHSI NPALDIGQVE 

      1210       1220       1230       1240       1250       1260 
GAFIQGMGLY TIEELSYSPQ GTLYSRGPNQ YKIPAICDIP TEMHISFLPP SEHSNTLYSS 

      1270       1280       1290       1300       1310       1320 
KGLGESGVFL GCSVFFAIHD AVKAARQERG ISGPWKLNSP LTPEKIRMAC EDKFTKMIPR 

      1330 
DEPGSYVPCN IPV
O54754 in FASTA format

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