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Reviewed, UniProtKB/Swiss-Prot Q9Z0U5 (ADO_RAT)

Last modified November 4, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aldehyde oxidase
    EC=1.2.3.1
Gene names
Name: Aox1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2).

Cofactor

Binds 2 2Fe-2S clusters By similarity.

FAD By similarity.

Molybdopterin By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

CytoplasmBy similarity.

Tissue specificity

Expression detected in liver, heart, lung, spleen and kidney.

Post-translational modification

The N-terminus is blocked.

Polymorphism

The sequence variants between males and females may be due to differences between individual animals rather than true gender differences.

Miscellaneous

Male and female rats possess kinetically distinct forms of AXO1 which may be due to differences in redox states. The sequence shown here is that of a female.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

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Ontologies

Keywords

   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Ligand2Fe-2S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

aldehyde oxidase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

molybdenum ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13331333Aldehyde oxidase
PRO_0000166108

Regions

Domain4 – 91882Fe-2S ferredoxin-type
Domain235 – 420186FAD-binding PCMH-type

Sites

Metal binding431Iron-sulfur (2Fe-2S) By similarity
Metal binding481Iron-sulfur (2Fe-2S) By similarity
Metal binding511Iron-sulfur (2Fe-2S) By similarity

Natural variations

Natural variant119 – 1202GM → AR
Natural variant6491A → T in males.
Natural variant12761F → L in males.
Natural variant13151T → R in males.

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Sequences

Sequence LengthMass (Da)Tools
Q9Z0U5-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 516B6CE395EB05C8

FASTA1,333146,921
        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

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References

[1]"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."
Wright R.M., Clayton D.A., Riley M.G., McManaman J.L., Repine J.E.
J. Biol. Chem. 274:3878-3886(1999) [PubMed: 9920943] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.

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Cross-references

Sequence databases

AF110477 mRNA. Translation: AAD16999.1.
AF110478 mRNA. Translation: AAD17000.1.
RefSeqNP_062236.2.
UniGeneRn.15681

3D structure databases

HSSPHSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000015354. Rattus norvegicus. [Contig view]
GeneID54349.
KEGGrno:54349.

Organism-specific databases

RGD620528. Aox1.

Phylogenomic databases

HOVERGENQ9Z0U5.

Gene expression databases

ArrayExpressQ9Z0U5.
GermOnlineENSRNOG00000015354. Rattus norvegicus.

Family and domain databases

InterProIPR002888. 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]
Gene3DG3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits.
G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit.
G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
ProDomPD186071. 2Fe-2S_bind. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio611028.

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Entry information

Entry nameADO_RAT
AccessionPrimary (citable) accession number: Q9Z0U5
Secondary accession number(s): Q9R240
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: May 1, 1999
Last modified: November 4, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents