Reviewed, UniProtKB/Swiss-Prot O54754 (ADO_MOUSE)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase
    EC=1.2.3.1
Alternative name(s):
    Retinal oxidase

Gene names

Name:	Aox1
Synonyms:	Ao, Ro

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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 + 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	Cytoplasm.
Tissue specificity	Highest expression in esophagus. Moderately low expression in lung, liver, heart and testis. In brain, expression is very high in choroid plexus, high in hind brain and low in hippocampus and cerebellum. In spinal cord expression is strongest in anterior horns. Low expression detected in spleen and eye. Not detected in stomach, small intestine, large intestine, skin or striated muscle. AXO1 expression in the livers of mice is approximately seven times greater in males than females.
Developmental stage	Expressed in adult liver but not in neonatal or embryonic liver.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Inferred from direct assay. Source: MGI electron carrier activity Inferred from direct assay. Source: MGI iron ion binding Inferred from electronic annotation. Source: InterPro 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_0000166106
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	109	1	H → Q in strain: 129/Sv.
	Natural variant	168	1	A → G in strain: C57BL/6 X CBA and 129/Sv.
	Natural variant	449	1	R → T in strain: C57BL/6 X CBA.
	Natural variant	492	1	R → A in strain: C57BL/6 X CBA.
	Natural variant	686 – 687	2	KQ → NE in strain: 129/Sv.
	Natural variant	857	1	E → D in strain: 129/Sv.
	Natural variant	983	1	E → D in strain: C57BL/6 X CBA.
	Natural variant	1169	1	N → D in strain: C57BL/6 X CBA and 129/Sv.
	Natural variant	1329	1	C → W in strain: C57BL/6 X CBA and 129/Sv.

Sequences

	Sequence		Length	Mass (Da)
	O54754-1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: 320CF0A3742F6AC5	FASTA	1,333	146,678
	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

References

[1]	"Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone." Kurosaki M., Demontis S., Barzago M.M., Garattini E., Terao M. Biochem. J. 341:71-80(1999) [PubMed: 10377246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: CD-1. Tissue: Liver.
[2]	"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." Huang D.-Y., Furukawa A., Ichikawa Y. Arch. Biochem. Biophys. 364:264-272(1999) [PubMed: 10190983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6 X CBA. Tissue: Liver.
[3]	"The mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping and functional characterization of the 5'-flanking region." Demontis S., Kurosaki M., Saccone S., Salvatore M., Garattini E., Terao M. Biochim. Biophys. Acta 1489:207-222(1999) [PubMed: 10673024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE. Strain: 129/Sv. Tissue: Thymus.
[4]	"Selective localization of mouse aldehyde oxidase mRNA in the choroid plexus and motor neurons." Bendotti C., Prosperini E., Kurosaki M., Garattini E., Terao M. NeuroReport 8:2343-2349(1997) [PubMed: 9243637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 561-746, TISSUE SPECIFICITY. Strain: C57BL/6J. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF076216 mRNA. Translation: AAC99382.1. AB017482 mRNA. Translation: BAA36834.1. AF121945 , AF121911, AF121912, AF121913, AF121914, AF121915, AF121916, AF121917, AF121918, AF121919, AF121920, AF121921, AF121922, AF121923, AF121924, AF121925, AF121926, AF121927, AF121928, AF121929, AF121930, AF121931, AF121932, AF121933, AF121934, AF121935, AF121936, AF121937, AF121938, AF121939, AF121940, AF121941, AF121942, AF121943, AF121944 Genomic DNA. Translation: AAD31763.1.
RefSeq	NP_033806.2.
UniGene	Mm.26787
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
PTM databases
PhosphoSite	O54754.
Genome annotation databases
Ensembl	ENSMUSG00000063558. Mus musculus. [Contig view]
GeneID	11761.
KEGG	mmu:11761.
Organism-specific databases
MGI	MGI:88035. Aox1.
Phylogenomic databases
HOGENOM	O54754.
HOVERGEN	O54754.
Gene expression databases
ArrayExpress	O54754.
CleanEx	MM_AOX1.
GermOnline	ENSMUSG00000063558. Mus musculus.
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]
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	279515.
SOURCE	Search...

Entry information

Entry name

ADO_MOUSE

Accession

Primary (citable) accession number: O54754
Secondary accession number(s): Q9WU85, Q9Z2Z5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	May 1, 1999
Last modified:	November 25, 2008
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)