Reviewed, UniProtKB/Swiss-Prot Q9Z0U5 (ADO_RAT)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase
    EC=1.2.3.1

Gene names

Name:

Aox1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	An aldehyde + H2O + O2 = a carboxylic acid + H2O2.
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	drug metabolic process Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Traceable author statement. Source: RGD
Cellular component	cytosol Traceable author statement. Source: RGD
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Ref.1 Inferred from direct assay. Source: RGD electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1333	1333	Aldehyde oxidase		PRO_0000166108
Regions
	Domain	4 – 91	88	2Fe-2S ferredoxin-type
	Domain	235 – 420	186	FAD-binding PCMH-type
Sites
	Metal binding	43	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	51	1	Iron-sulfur (2Fe-2S) By similarity
Natural variations
	Natural variant	119 – 120	2	GM → AR
	Natural variant	649	1	A → T in males.
	Natural variant	1276	1	F → L in males.
	Natural variant	1315	1	T → R in males.

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0U5-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 516B6CE395EB05C8	FASTA	1,333	146,921
	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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF110477 mRNA. Translation: AAD16999.1. AF110478 mRNA. Translation: AAD17000.1.
IPI	IPI00208185.
RefSeq	NP_062236.2.
UniGene	Rn.15681
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z0U5.
Proteomic databases
PRIDE	Q9Z0U5.
Genome annotation databases
Ensembl	ENSRNOT00000021389; ENSRNOP00000021389; ENSRNOG00000015354; Rattus norvegicus. [Genome view]
GeneID	54349.
KEGG	rno:54349.
Organism-specific databases
CTD	54349.
RGD	620528. Aox1.
Phylogenomic databases
HOVERGEN	Q9Z0U5.
Enzyme and pathway databases
BRENDA	1.2.3.1. 248.
Gene expression databases
ArrayExpress	Q9Z0U5.
Genevestigator	Q9Z0U5.
GermOnline	ENSRNOG00000015354. Rattus norvegicus.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA: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.
Pfam	PF01315. 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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	611028.

Entry information

Entry name

ADO_RAT

Accession

Primary (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:	October 13, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)