Q06278 (ADO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldehyde oxidase
EC=1.2.3.1

Gene names

Name:	AOX1
Synonyms:	AO

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1338 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	An aldehyde + H2O + O2 = a carboxylate + H2O2.
Cofactor	Binds 2 2Fe-2S clusters. FAD. Molybdopterin.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Abundant in liver, lower levels in lung, skeletal muscle, pancreas. Undetected in heart, brain and kidney.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.
Caution	Was originally (Ref.1) thought to be a xanthine dehydrogenase.
Sequence caution	The sequence AAA96650.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302. The sequence AAB83966.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inflammatory response Traceable author statement Ref.1. Source: ProtInc reactive oxygen species metabolic process Traceable author statement PubMed 7570184. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Traceable author statement PubMed 7570184. Source: ProtInc electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro molybdopterin cofactor binding Inferred from electronic annotation. Source: InterPro xanthine dehydrogenase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1338	1338	Aldehyde oxidase		PRO_0000166104
Regions
	Domain	5 – 92	88	2Fe-2S ferredoxin-type
	Domain	236 – 421	186	FAD-binding PCMH-type
Sites
	Metal binding	44	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	49	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	52	1	Iron-sulfur (2Fe-2S) By similarity
Natural variations
	Natural variant	314	1	Q → R. Corresponds to variant rs58185012 [ dbSNP | Ensembl ].		VAR_061136
	Natural variant	802	1	R → C. Corresponds to variant rs41309768 [ dbSNP | Ensembl ].		VAR_047517
	Natural variant	1297	1	H → R. Corresponds to variant rs3731722 [ dbSNP | Ensembl ].		VAR_047518
Experimental info
	Sequence conflict	41	1	K → P in AAA96650. Ref.1
	Sequence conflict	41	1	K → P in AAB83966. Ref.2
	Sequence conflict	127	1	T → P in AAA96650. Ref.1
	Sequence conflict	127	1	T → P in AAB83966. Ref.2
	Sequence conflict	152	1	T → H in AAA96650. Ref.1
	Sequence conflict	152	1	T → H in AAB83966. Ref.2
	Sequence conflict	227	1	E → D in AAA96650. Ref.1
	Sequence conflict	227	1	E → D in AAB83966. Ref.2
	Sequence conflict	251	1	E → D in AAA96650. Ref.1
	Sequence conflict	418	1	Y → I in AAA96650. Ref.1
	Sequence conflict	418	1	Y → I in AAB83966. Ref.2
	Sequence conflict	501	1	V → L in AAB83966. Ref.2
	Sequence conflict	627	1	I → N in AAB83966. Ref.2
	Sequence conflict	929	1	A → V in AAA96650. Ref.1
	Sequence conflict	929	1	A → V in AAB83966. Ref.2
	Sequence conflict	1019	1	G → A in AAA96650. Ref.1
	Sequence conflict	1019	1	G → A in AAB83966. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q06278 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 2AB5E543F18C9261	FASTA	1,338	147,918
	10 20 30 40 50 60 MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN 70 80 90 100 110 120 PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH PVQERIAKCH GTQCGFCTPG 130 140 150 160 170 180 MVMSIYTLLR NHPEPTLDQL TDALGGNLCR CTGYRPIIDA CKTFCKTSGC CQSKENGVCC 190 200 210 220 230 240 LDQGINGLPE FEEGSKTSPK LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER 250 260 270 280 290 300 MMWFSPVTLK ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA 310 320 330 340 350 360 YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR NMASLGGHII 370 380 390 400 410 420 SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC PNADLKPQEI LVSVNIPYSR 430 440 450 460 470 480 KWEFVSAFRQ AQRQENALAI VNSGMRVFFG EGDGIIRELC ISYGGVGPAT ICAKNSCQKL 490 500 510 520 530 540 IGRHWNEQML DIACRLILNE VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV 550 560 570 580 590 600 HYPSLADKYE SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 610 620 630 640 650 660 DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV NSFCFFTEAE 670 680 690 700 710 720 KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL EPLILTIEES IQHNSSFKPE 730 740 750 760 770 780 RKLEYGNVDE AFKVVDQILE GEIHMGGQEH FYMETQSMLV VPKGEDQEMD VYVSTQFPKY 790 800 810 820 830 840 IQDIVASTLK LPANKVMCHV RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE 850 860 870 880 890 900 DMLITGGRHP YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF 910 920 930 940 950 960 PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV RIINMYKEID 970 980 990 1000 1010 1020 QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN YWKKKGLAMV PLKFPVGLGS 1030 1040 1050 1060 1070 1080 RAAGQAAALV HIYLDGSVLV THGGIEMGQG VHTKMIQVVS RELRMPMSNV HLRGTSTETV 1090 1100 1110 1120 1130 1140 PNANISGGSV VADLNGLAVK DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG 1150 1160 1170 1180 1190 1200 YFRGYESDMN WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 1210 1220 1230 1240 1250 1260 IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI ALLPPSQNSN 1270 1280 1290 1300 1310 1320 TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL TLNSPLTPEK IRMACEDKFT 1330 KMIPRDEPGS YVPWNVPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase." Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E. Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 gene." Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E. Redox Rep. 3:135-144(1997) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II." Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T. Biochem. Biophys. Res. Commun. 282:1194-1200(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11005 mRNA. Translation: AAA96650.1. Frameshift. AF017060 , AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift. AF010260 Genomic DNA. Translation: AAB83968.1. AB046692 mRNA. Translation: BAB40305.1. AC007163 Genomic DNA. Translation: AAX93285.1. AC080164 Genomic DNA. Translation: AAY24265.1. CH471063 Genomic DNA. Translation: EAW70209.1. BC117179 mRNA. Translation: AAI17180.1. BC117181 mRNA. Translation: AAI17182.1.
IPI	IPI00029715.
PIR	A49634.
RefSeq	NP_001150.3. NM_001159.3.
UniGene	Hs.406238.
3D structure databases
ProteinModelPortal	Q06278.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06278. 4 interactions.
STRING	9606.ENSP00000363832.
PTM databases
PhosphoSite	Q06278.
Polymorphism databases
DMDM	215273968.
Proteomic databases
PaxDb	Q06278.
PRIDE	Q06278.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374700; ENSP00000363832; ENSG00000138356.
GeneID	316.
KEGG	hsa:316.
UCSC	uc002uvx.3. human.
Organism-specific databases
CTD	316.
GeneCards	GC02P201450.
H-InvDB	HIX0029780.
HGNC	HGNC:553. AOX1.
HPA	HPA040199. HPA040215.
MIM	602841. gene.
neXtProt	NX_Q06278.
PharmGKB	PA24842.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4630.
HOGENOM	HOG000191197.
HOVERGEN	HBG004182.
KO	K00157.
OMA	WACRTNL.
OrthoDB	EOG4DNF3N.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000138356-MONOMER.
SABIO-RK	Q06278.
Gene expression databases
ArrayExpress	Q06278.
Bgee	Q06278.
CleanEx	HS_AOX1.
Genevestigator	Q06278.
GermOnline	ENSG00000138356. Homo sapiens.
Family and domain databases
Gene3D	1.10.150.120. 1 hit. 3.10.20.30. 1 hit. 3.30.365.10. 6 hits. 3.30.43.10. 1 hit. 3.30.465.10. 1 hit. 3.90.1170.50. 1 hit.
InterPro	IPR002888. 2Fe-2S-bd. IPR001041. 2Fe-2S_ferredoxin-type. 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. Beta-grasp_dom. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR002346. Mopterin_DH_FAD-bd. IPR022407. OxRdtase_Mopterin_BS. [Graphical view]
PANTHER	PTHR11908:SF10. PTHR11908:SF10. 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.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
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
BindingDB	Q06278.
ChEMBL	CHEMBL3257.
ChiTaRS	AOX1. human.
DrugBank	DB00484. Brimonidine. DB00477. Chlorpromazine. DB00426. Famciclovir. DB00170. Menadione. DB00563. Methotrexate. DB00157. NADH. DB00377. Palonosetron. DB00299. Penciclovir. DB00481. Raloxifene. DB00962. Zaleplon. DB00909. Zonisamide.
GenomeRNAi	316.
NextBio	1283.
SOURCE	Search...

Entry information

Entry name

ADO_HUMAN

Accession

Primary (citable) accession number: Q06278
Secondary accession number(s): O14765 , Q53RR8, Q53TV3, Q9BYF0, Q9UPG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.