Reviewed, UniProtKB/Swiss-Prot Q06278 (ADO_HUMAN)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase
    EC=1.2.3.1

Gene names

Name:	AOX1
Synonyms:	AO

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1338 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. 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
Gene Ontology (GO)
Biological process	inflammatory response Ref.1 Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic process Traceable author statement. Source: ProtInc
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 Traceable author statement. Source: ProtInc electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW xanthine dehydrogenase activity Ref.1 Traceable author statement. 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	802	1	R → C: dbSNP rs41309768.		VAR_047517
	Natural variant	1297	1	H → R: dbSNP rs3731722.		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)
	Q06278-1 [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: 8248161] [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]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. AC007163 Genomic DNA. Translation: AAX93285.1. AC080164 Genomic DNA. Translation: AAY24265.1.
PIR	A49634.
UniGene	Hs.406238
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
PTM databases
PhosphoSite	Q06278.
Genome annotation databases
Ensembl	ENSG00000138356. Homo sapiens. [Contig view]
Organism-specific databases
H-InvDB	HIX0029780.
HGNC	HGNC:553. AOX1.
MIM	602841. gene.
PharmGKB	PA24842.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q06278.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000138356-MON.
Gene expression databases
ArrayExpress	Q06278.
CleanEx	HS_AOX1.
GermOnline	ENSG00000138356. Homo sapiens.
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
DrugBank	DB00484. Brimonidine. DB00477. Chlorpromazine. DB00426. Famciclovir. DB00170. Menadione. DB00563. Methotrexate. DB00157. NADH. DB00377. Palonosetron. DB00299. Penciclovir. DB00481. Raloxifene. DB00962. Zaleplon. DB00909. Zonisamide.
LinkHub	Q06278.
SOURCE	Search...

Entry information

Entry name

ADO_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 25, 2008
Last modified:	November 25, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)