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UniProtKB/Swiss-Prot entry Q9Z0U5

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

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Entry information
Entry name ADO_RAT
Primary accession number Q9Z0U5
Secondary accession number Q9R240
Integrated into Swiss-Prot on May 15, 2002
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 69)
Name and origin of the protein
Protein name Aldehyde oxidase
Synonym EC 1.2.3.1
Gene name
Name: Aox1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
DOI=10.1074/jbc.274.6.3878; PubMed=9920943 [NCBI, ExPASy, EBI, Israel, Japan]
Wright R.M., Clayton D.A., Riley M.G., McManaman J.L., Repine J.E.;
"cDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase (rAOX1). Differences in redox status may distinguish male and female forms of hepatic APX.";
J. Biol. Chem. 274:3878-3886(1999).
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
AF110477; AAD16999.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110478; AAD17000.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_062236.2; -.
UniGene Rn.15681
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q9Z0U5.
PTM databases
PhosphoSite Q9Z0U5; -.
Organism-specific databases
RGD 620528; Aox1.
Gene expression databases
ArrayExpress Q9Z0U5; -.
GermOnline ENSRNOG00000015354; Rattus norvegicus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004031; Molecular function: aldehyde oxidase activity (inferred from electronic annotation from EC).
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:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051287; Molecular function: NAD binding (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 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).
ProtoNet Q9Z0U5.
Genome annotation databases
Ensembl ENSRNOG00000015354; Rattus norvegicus. [Contig view]
GeneID 54349; -.
KEGG rno:54349; -.
Phylogenomic databases
HOVERGEN Q9Z0U5; -.
Other
NextBio 611028; -.
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_0000166108
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   119    120  2     GM -> AR. 
VARIANT   649    649  1     A -> T (in males). 
VARIANT   1276   1276  1     F -> L (in males). 
VARIANT   1315   1315  1     T -> R (in males). 
Sequence information
Length: 1333 AA [This is the length of the unprocessed precursor] Molecular weight: 146921 Da [This is the MW of the unprocessed precursor] CRC64: 516B6CE395EB05C8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDPPQLLFYV NGQKVVENNV DPEMMLLPYL RKNLRLTGTK YGCGGGGCGA CTVMISRYNP 

        70         80         90        100        110        120 
STKSIRHHPV NACLTPICSL YGTAVTTVEG IGNTRTRLHP VQERIAKCHS TQCGFCTPGM 

       130        140        150        160        170        180 
VMSMYALLRN HPEPSLDQLT DALGGNLCRC TGYRPIIDAC KTFCRASGCC ESKENGVCCL 

       190        200        210        220        230        240 
DQGINGSAEF QEGDETSPEL FSEKEFQPLD PTQELIFPPE LMRIAEKQPP KTRVFYSNRM 

       250        260        270        280        290        300 
TWISPVTLEE LVEAKFKYPG APIVMGYTSV GPEVKFKGVF HPIIISPDRI EELSIINQTG 

       310        320        330        340        350        360 
DGLTLGAGLS LDQVKDILTD VVQKLPEETT QTYRALLKHL RTLAGSQIRN MASLGGHIVS 

       370        380        390        400        410        420 
RHLDSDLNPL LAVGNCTLNL LSKDGKRQIP LSEQFLRKCP DSDLKPQEVL VSVNIPCSRK 

       430        440        450        460        470        480 
WEFVSAFRQA QRQQNALAIV NSGMRVLFRE GGGVIKELSI LYGGVGPTTI GAKNSCQKLI 

       490        500        510        520        530        540 
GRPWNEEMLD TACRLVLDEV TLAGSAPGGK VEFKRTLIIS FLFKFYLEVL QGLKREDPGH 

       550        560        570        580        590        600 
YPSLTNNYES ALEDLHSKHH WRTLTHQNVD SMQLPQDPIG RPIMHLSGIK HATGEAIYCD 

       610        620        630        640        650        660 
DMPAVDRELF LTFVTSSRAH AKIVSIDLSE ALSLPGVVDI ITADHLQDAT TFGTETLLAT 

       670        680        690        700        710        720 
DKVHCVGQLV CAVIADSETR AKQAAKHVKV VYRDLEPLIL TIEEAIQHKS FFESERKLEC 

       730        740        750        760        770        780 
GNVDEAFKIA DQILEGEIHI GGQEHFYMET QSMLVVPKGE DGEIDIYVST QFPKHIQDIV 

       790        800        810        820        830        840 
AATLKLSVNK VMCHVRRVGG AFGGKVGKTS IMAAITAFAA SKHGRAVRCT LERGEDMLIT 

       850        860        870        880        890        900 
GGRHPYLGKY KVGFMRDGRI VALDVEHYCN GGSSLDESLW VIEMGLLKMD NAYKFPNLRC 

       910        920        930        940        950        960 
RGWACRTNLP SHTALRGFGF PQAGLVTEAC VTEVAIRCGL SPEQVRTINM YKQIDNTHYK 

       970        980        990       1000       1010       1020 
QEFSAKTLFE CWRECMAKCS YSERKTAVGK FNAENSWKKR GMAVIPLKFP VGVGSVAMGQ 

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

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

      1150       1160       1170       1180       1190       1200 
ESNINWEKGE GHPFEYFVYG AACSEVEIDC LTGDHKNIRT DIVMDVGHSI NPALDIGQVE 

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

      1270       1280       1290       1300       1310       1320 
KGLGESGVFL GCSVFFAIHD AVRAARQERG ISGPWKLTSP LTPEKIRMAC EDKFTKMIPR 

      1330 
DEPGSYVPWN IPV
Q9Z0U5 in FASTA format

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