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Index > Protein center > AOX1(Gene name) > Rabbit
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  • AOX1 (Gene name),
  • Aldehyde oxidase 1 (Protein name ),  AOXA_RABIT from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    AOX1(AO);
    Protein name:
    Aldehyde oxidase 1;
    Alternative:
    Retinal oxidase;1.17.3.-;Azaheterocycle hydroxylase 1);Retinoic acid synthase;
    Organism:
    Rabbit (Oryctolagus cuniculus). 
    General Annotation
    Sub Unit:
    Homodimer.
    Function:
    Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use hypoxanthine and all-trans-retinol as substrate.
    Subcellular Location:
    Cytoplasm
    Protein Attributes:
    Sequence length:
    1334
    Sequence:
    50:
    MEPAPELLFY | VNGRKVVEKQ | VDPETMLLPY | LRKKLRLTGT | KYGCGGGGCG | 
    100:
    ACTVMISRYN | RVTKKIRHYP | VNACLTPICS | LYGAAVTTVE | GIGSTTTRLH | 
    150:
    PVQERIAKFH | GTQCGFCTPG | MVMSMYALLR | NHPEPTLDQL | ADALGGNLCR | 
    200:
    CTGYRPIIEA | YKTFCKTSDC | CQNKENGFCC | LDQGINGLPE | VEEENQTRPN | 
    250:
    LFSEEEYLPL | DPTQELIFPP | ELMTMAEKQP | QRTRVFSGER | MMWISPVTLK | 
    300:
    ALLEAKSTYP | QAPVVMGNTS | VGPGVKFKGI | FHPVIISPDS | IEELNVVSHT | 
    350:
    HSGLTLGAGL | SLAQVKDILA | DVVQKVPEEN | AQTYRALLKH | LGTLAGSQIR | 
    400:
    NMASLGGHII | SRHLDSDLNP | LLAVGNCTLN | VLSKEGERQI | PLDEQFLSRC | 
    450:
    PEADLKPQEI | LASVHIPYSR | KWEFVLAFRQ | AQRKQNALAI | VNSGMRVFFG | 
    500:
    EGDGIIRELA | ISYGGVGPTI | ICAKNSCQKL | IGRSWNEEML | DTACRLILDE | 
    550:
    VSLPGSAPGG | KVEFKRTLII | SFLFKFYLEV | SQILKRMAPG | LSPHLADKYE | 
    600:
    SALQDLHARY | SWSTLKDQDV | DARQLSQDPI | GHPVMHLSGV | KHATGEAIYL | 
    650:
    DDMPAVDQEL | FMAFVTSPRA | HAKIVSTDLL | EALSLPGVVD | IVTAEHLQDG | 
    700:
    NTFYTEKLLA | ADEVLCVGQL | VCAVIAESEV | QAKQAAKQVK | IVYEDLEPVI | 
    750:
    LSIEEAIEQK | SFFEPERKLE | YGNVDEAFKV | VDQILEGEIH | MGGQEHFYME | 
    800:
    TQSVLVVPKG | EDQEMDVYAS | TQFPKYIQDM | VAAVLKLPVN | KVMCHVKRVG | 
    850:
    GAFGGKVFKA | SIMAAIAAFA | ANKHGRAVRC | ILERGEDMLI | TGGRHPYLGK | 
    900:
    YKAGFMNDGR | IVALDVEHYS | NGGCSLDESL | LVIEMGLLKM | ENAYKFPNLR | 
    950:
    CRGWACRTNL | PSNTAFRGFG | FPQAGLITEC | CITEVAAKCG | LSPEKVRAIN | 
    1000:
    FYKEIDQTPY | KQEINAKNLT | QCWNECLAKS | SYFQRKVAVE | KFNAENYWKQ | 
    1050:
    RGLAIIPFKY | PRGLGSVAYG | QAAALVHVYL | DGSVLVTHGG | IEMGQGVHTK | 
    1100:
    MIQVVSRELK | MPMSNVHLRG | TSTETVPNTN | ASGGSVVADL | NGLAVKDACQ | 
    1150:
    TLLKRLEPII | NKNPQGTWKE | WAQAAFDKSI | SLSATGYFRG | YDSNIDWDKG | 
    1200:
    EGHPFEYFVY | GAACSEVEID | CLTGDHKTIR | TDIVMDVGYS | INPALDIGQV | 
    1250:
    EGAFIQGMGL | YTIEELHYSP | QGILYSRGPN | QYKIPAICDI | PAELNVTFLP | 
    1300:
    PSEKSNTLYS | SKGLGESGVF | MGCSVFFAIR | EAVCAARQAR | GLSAPWKLSS | 
    1334:
    PLTPEKIRMA | CEDKFTKMIP | RDKPGSYVPW | NVPV
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    Pfam:
    SMR:
    UniGene:
    Uniprot:
     
    FOR
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    CLIA Kit for Rabbit Aldehyde oxidase 1
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    CLIA Kit for Rabbit Aldehyde oxidase 1
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    CLIA Kit for Rabbit Aldehyde oxidase 1
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    Packing:
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    Packing:
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    Polyclonal Antibody for Rabbit Aldehyde oxidase 1
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    Packing:
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    Polyclonal Antibody for Rabbit Aldehyde oxidase 1
    Monoclonal Antibody for Rabbit Aldehyde oxidase 1
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    Monoclonal Antibody for Rabbit Aldehyde oxidase 1
    Protein for Rabbit Aldehyde oxidase 1
    Protein for Rabbit Aldehyde oxidase 1
    Protein for Rabbit Aldehyde oxidase 1
    Protein for Rabbit Aldehyde oxidase 1
    Protein for Rabbit Aldehyde oxidase 1

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    References
    1. 1.
      "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] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 857-884; 891-943 AND 1272-1293;FUNCTION;TISSUE SPECIFICITY
      strain: Japanese white.
      tissue: Liver.
    2. 2.
      "Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase."
      Turner N.A. , Doyle W.A. , Ventom A.M. , Bray R.C.
      Eur. J. Biochem.232:646-657(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 203-231 AND 574-597;FUNCTION AS OXIDASE;COFACTOR
      tissue: Liver.
    3. 3.
      "Characteristic properties of retinal oxidase (retinoic acid synthase) from rabbit hepatocytes."
      Tsujita M. , Tomita S. , Miura S. , Ichikawa Y.
      Biochim. Biophys. Acta1204:108-116(1994) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION AS OXIDASE;CATALYTIC ACTIVITY;SUBSTRATE SPECIFICITY;BIOPHYSICOCHEMICAL PROPERTIES;HOMODIMER;SUBCELLULAR LOCATION;TISSUE SPECIFICITY;REACTION MECHANISM;BLOCKAGE OF N-TERMINUS;ENZYME REGULATION
    4. 4.
      "In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver."
      Rashidi M.R. , Smith J.A. , Clarke S.E. , Beedham C.
      Drug Metab. Dispos.25:805-813(1997) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE;CATALYTIC ACTIVITY;ENZYME REGULATION;BIOPHYSICOCHEMICAL PROPERTIES
    5. 5.
      "Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression."
      Kurosaki M. , Bolis M. , Fratelli M. , Barzago M.M. , Pattini L. , Perretta G. , Terao M. , Garattini E.
      Cell. Mol. Life Sci.70:1807-1830(2013) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION OF PARALOGS
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