AOX1

Protein identityUniProt · HPA

UniProt accession

Q06278

Gene

AOX1

Ensembl

ENSG00000138356

Chromosome

2

Canonical length

1338 aa

Protein class

Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Subcellular location

Nuclear bodies,Microtubules,Cytokinetic bridge,Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1338 residues, UniProt reviewed canonical sequence.

>Q06278|AOX1
     1  MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN
    61  PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH PVQERIAKCH GTQCGFCTPG
   121  MVMSIYTLLR NHPEPTLDQL TDALGGNLCR CTGYRPIIDA CKTFCKTSGC CQSKENGVCC
   181  LDQGINGLPE FEEGSKTSPK LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER
   241  MMWFSPVTLK ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA
   301  YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR NMASLGGHII
   361  SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC PNADLKPQEI LVSVNIPYSR
   421  KWEFVSAFRQ AQRQENALAI VNSGMRVFFG EGDGIIRELC ISYGGVGPAT ICAKNSCQKL
   481  IGRHWNEQML DIACRLILNE VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV
   541  HYPSLADKYE SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC
   601  DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV NSFCFFTEAE
   661  KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL EPLILTIEES IQHNSSFKPE
   721  RKLEYGNVDE AFKVVDQILE GEIHMGGQEH FYMETQSMLV VPKGEDQEMD VYVSTQFPKY
   781  IQDIVASTLK LPANKVMCHV RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE
   841  DMLITGGRHP YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF
   901  PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV RIINMYKEID
   961  QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN YWKKKGLAMV PLKFPVGLGS
  1021  RAAGQAAALV HIYLDGSVLV THGGIEMGQG VHTKMIQVVS RELRMPMSNV HLRGTSTETV
  1081  PNANISGGSV VADLNGLAVK DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG
  1141  YFRGYESDMN WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID
  1201  IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI ALLPPSQNSN
  1261  TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL TLNSPLTPEK IRMACEDKFT
  1321  KMIPRDEPGS YVPWNVPI

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against AOX1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.2

Highest tissue expression

833 nTPM

Expression across tissuesHPA

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.94

gnomAD pLI

0

gnomAD missense Z

0.18

DepMap mean gene effect

-0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• lipid metabolic process
• xenobiotic metabolic process

Molecular functions

• 2 iron, 2 sulfur cluster binding
• aldehyde oxidase activity
• FAD binding
• flavin adenine dinucleotide binding
• identical protein binding
• iron ion binding
• molybdopterin cofactor binding
• NAD binding
• protein homodimerization activity

Cellular components

• cytosol
• extracellular exosome
• intercellular bridge
• microtubule cytoskeleton
• nuclear body

Protein domainsUniProt · Pfam · InterPro

• Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
• 2Fe-2S ferredoxin-type iron-sulfur binding domain
• Molybdopterin dehydrogenase, FAD-binding
• [2Fe-2S]-binding
• CO dehydrogenase flavoprotein, C-terminal
• 2Fe-2S ferredoxin, iron-sulphur binding site
• Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain
• Beta-grasp domain superfamily
• FAD-binding domain, PCMH-type
• FAD-binding, type PCMH, subdomain 1
• FAD-binding, type PCMH, subdomain 2
• Aldehyde oxidase/xanthine dehydrogenase-like
• Oxidoreductase, molybdopterin binding site
• 2Fe-2S ferredoxin-like superfamily
• FAD-binding, type PCMH-like superfamily
• CO dehydrogenase flavoprotein, C-terminal domain superfamily
• Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily
• [2Fe-2S]-binding domain superfamily
• Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily
• Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain
• 2Fe-2S iron-sulfur cluster binding domain
• FAD binding domain in molybdopterin dehydrogenase
• Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
• [2Fe-2S] binding domain
• Molybdopterin cofactor-binding domain
• CO dehydrogenase flavoprotein C-terminal domain
• Molybdopterin cofactor-binding domain
• Aldehyde oxidase

KeywordsUniProt

• 2Fe-2S
• Cytoplasm
• FAD
• Flavoprotein
• Iron
• Iron-sulfur
• Lipid metabolism
• Metal-binding
• Molybdenum
• Oxidoreductase
• Phosphoprotein