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Entry version 140 (16 Jan 2019)
Sequence version 2 (15 May 2002)
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Protein

Aldehyde oxidase 1

Gene

AOX1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, 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.4 Publications

Miscellaneous

The reaction follows an ordered Bi-Bi kinetic mechanism. During retinal oxidation, incorporates the oxygen of water into retinoate, but not that of molecular oxygen (PubMed:8305467).1 Publication
AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by hydralazine and menadione. Not inhibited by BOF-4272 or allopurinol, xanthine dehydrogenase potent inhibitors. In contrast to guinea pig, human and rat, isovanillin is not an inhibitor but a substrate for AOX1 in rabbit.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=8 µM for all-trans-retinal1 Publication
  2. KM=13 µM for 9-cis-retinal1 Publication
  3. KM=0.9 mM for 13-cis-retinal1 Publication
  4. KM=0.11 mM for N-methylnicotinamide1 Publication
  5. KM=94.7 µM for O21 Publication
  6. KM=0.44 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)1 Publication
  7. KM=45 µM for isovanillin (at 37 degrees Celsius and pH 7)1 Publication
  1. Vmax=192 nmol/min/mg enzyme with all-trans-retinal as substrate1 Publication
  2. Vmax=57 nmol/min/mg enzyme with 9-cis-retinal as substrate1 Publication
  3. Vmax=105 nmol/min/mg enzyme with 13-cis-retinal as substrate1 Publication
  4. Vmax=267 nmol/min/mg enzyme with N-methylnicotinamide as substrate1 Publication
  5. Vmax=114 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate1 Publication
  6. Vmax=211 nmol/min/mg enzyme with isovanillin as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi44Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi52Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi74Iron-sulfur 1 (2Fe-2S)By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei113MolybdopterinBy similarity1
Metal bindingi114Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi117Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi149Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi151Iron-sulfur 2 (2Fe-2S)By similarity1
Binding sitei151MolybdopterinBy similarity1
Binding sitei345FAD; via amide nitrogenBy similarity1
Binding sitei354FADBy similarity1
Binding sitei358FADBy similarity1
Binding sitei367FADBy similarity1
Binding sitei411FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei1043Molybdopterin; via carbonyl oxygenBy similarity1
Binding sitei1199MolybdopterinBy similarity1
Binding sitei1264Molybdopterin; via carbonyl oxygenBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1266Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi264 – 271FADBy similarity8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.3.1 1749

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P80456

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aldehyde oxidase 1By similarity (EC:1.2.3.12 Publications)
Alternative name(s):
Azaheterocycle hydroxylase 11 Publication (EC:1.17.3.-1 Publication)
Retinal oxidase1 Publication
Retinoic acid synthase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AOX1By similarity
Synonyms:AO
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1641356

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001661071 – 1334Aldehyde oxidase 1Add BLAST1334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1064PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P80456

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Very high expression in liver and lung. High expression in kidney, pancreas, brain stem and spinal cord. Moderate expression in heart, testis, eye, cerebral cortex and cerebellum. Low expression in stomach and muscle.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000012025

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P80456

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P80456

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P80456

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni802 – 803Molybdopterin bindingBy similarity2
Regioni1084 – 1087Molybdopterin bindingBy similarity4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000191197

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004182

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P80456

KEGG Orthology (KO)

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KOi
K00157

Database of Orthologous Groups

More...
OrthoDBi
48717at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002888 2Fe-2S-bd
IPR036884 2Fe-2S-bd_dom_sf
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
IPR006058 2Fe2S_fd_BS
IPR000674 Ald_Oxase/Xan_DH_a/b
IPR036856 Ald_Oxase/Xan_DH_a/b_sf
IPR016208 Ald_Oxase/xanthine_DH
IPR014313 Aldehyde_oxidase
IPR008274 AldOxase/xan_DH_Mopterin-bd
IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
IPR005107 CO_DH_flav_C
IPR036683 CO_DH_flav_C_dom_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR002346 Mopterin_DH_FAD-bd
IPR022407 OxRdtase_Mopterin_BS

Pfam protein domain database

More...
Pfami
View protein in 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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000127 Xanthine_DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47741 SSF47741, 1 hit
SSF54292 SSF54292, 1 hit
SSF54665 SSF54665, 1 hit
SSF55447 SSF55447, 1 hit
SSF56003 SSF56003, 1 hit
SSF56176 SSF56176, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR02969 mam_aldehyde_ox, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00197 2FE2S_FER_1, 1 hit
PS51085 2FE2S_FER_2, 1 hit
PS51387 FAD_PCMH, 1 hit
PS00559 MOLYBDOPTERIN_EUK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P80456-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEPAPELLFY VNGRKVVEKQ VDPETMLLPY LRKKLRLTGT KYGCGGGGCG
60 70 80 90 100
ACTVMISRYN RVTKKIRHYP VNACLTPICS LYGAAVTTVE GIGSTTTRLH
110 120 130 140 150
PVQERIAKFH GTQCGFCTPG MVMSMYALLR NHPEPTLDQL ADALGGNLCR
160 170 180 190 200
CTGYRPIIEA YKTFCKTSDC CQNKENGFCC LDQGINGLPE VEEENQTRPN
210 220 230 240 250
LFSEEEYLPL DPTQELIFPP ELMTMAEKQP QRTRVFSGER MMWISPVTLK
260 270 280 290 300
ALLEAKSTYP QAPVVMGNTS VGPGVKFKGI FHPVIISPDS IEELNVVSHT
310 320 330 340 350
HSGLTLGAGL SLAQVKDILA DVVQKVPEEN AQTYRALLKH LGTLAGSQIR
360 370 380 390 400
NMASLGGHII SRHLDSDLNP LLAVGNCTLN VLSKEGERQI PLDEQFLSRC
410 420 430 440 450
PEADLKPQEI LASVHIPYSR KWEFVLAFRQ AQRKQNALAI VNSGMRVFFG
460 470 480 490 500
EGDGIIRELA ISYGGVGPTI ICAKNSCQKL IGRSWNEEML DTACRLILDE
510 520 530 540 550
VSLPGSAPGG KVEFKRTLII SFLFKFYLEV SQILKRMAPG LSPHLADKYE
560 570 580 590 600
SALQDLHARY SWSTLKDQDV DARQLSQDPI GHPVMHLSGV KHATGEAIYL
610 620 630 640 650
DDMPAVDQEL FMAFVTSPRA HAKIVSTDLL EALSLPGVVD IVTAEHLQDG
660 670 680 690 700
NTFYTEKLLA ADEVLCVGQL VCAVIAESEV QAKQAAKQVK IVYEDLEPVI
710 720 730 740 750
LSIEEAIEQK SFFEPERKLE YGNVDEAFKV VDQILEGEIH MGGQEHFYME
760 770 780 790 800
TQSVLVVPKG EDQEMDVYAS TQFPKYIQDM VAAVLKLPVN KVMCHVKRVG
810 820 830 840 850
GAFGGKVFKA SIMAAIAAFA ANKHGRAVRC ILERGEDMLI TGGRHPYLGK
860 870 880 890 900
YKAGFMNDGR IVALDVEHYS NGGCSLDESL LVIEMGLLKM ENAYKFPNLR
910 920 930 940 950
CRGWACRTNL PSNTAFRGFG FPQAGLITEC CITEVAAKCG LSPEKVRAIN
960 970 980 990 1000
FYKEIDQTPY KQEINAKNLT QCWNECLAKS SYFQRKVAVE KFNAENYWKQ
1010 1020 1030 1040 1050
RGLAIIPFKY PRGLGSVAYG QAAALVHVYL DGSVLVTHGG IEMGQGVHTK
1060 1070 1080 1090 1100
MIQVVSRELK MPMSNVHLRG TSTETVPNTN ASGGSVVADL NGLAVKDACQ
1110 1120 1130 1140 1150
TLLKRLEPII NKNPQGTWKE WAQAAFDKSI SLSATGYFRG YDSNIDWDKG
1160 1170 1180 1190 1200
EGHPFEYFVY GAACSEVEID CLTGDHKTIR TDIVMDVGYS INPALDIGQV
1210 1220 1230 1240 1250
EGAFIQGMGL YTIEELHYSP QGILYSRGPN QYKIPAICDI PAELNVTFLP
1260 1270 1280 1290 1300
PSEKSNTLYS SKGLGESGVF MGCSVFFAIR EAVCAARQAR GLSAPWKLSS
1310 1320 1330
PLTPEKIRMA CEDKFTKMIP RDKPGSYVPW NVPV
Length:1,334
Mass (Da):147,138
Last modified:May 15, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0747A0569C2C062A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB009345 mRNA Translation: BAA81726.1

NCBI Reference Sequences

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RefSeqi
NP_001075459.1, NM_001081990.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Ocu.2359

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
100008601

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100008601

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009345 mRNA Translation: BAA81726.1
RefSeqiNP_001075459.1, NM_001081990.1
UniGeneiOcu.2359

3D structure databases

ProteinModelPortaliP80456
SMRiP80456
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012025

Chemistry databases

BindingDBiP80456
ChEMBLiCHEMBL1641356

Proteomic databases

PRIDEiP80456

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008601
KEGGiocu:100008601

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
316

Phylogenomic databases

eggNOGiKOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA
HOGENOMiHOG000191197
HOVERGENiHBG004182
InParanoidiP80456
KOiK00157
OrthoDBi48717at2759

Enzyme and pathway databases

BRENDAi1.2.3.1 1749
SABIO-RKiP80456

Miscellaneous databases

Protein Ontology

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PROi
PR:P80456

Family and domain databases

InterProiView protein in InterPro
IPR002888 2Fe-2S-bd
IPR036884 2Fe-2S-bd_dom_sf
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
IPR006058 2Fe2S_fd_BS
IPR000674 Ald_Oxase/Xan_DH_a/b
IPR036856 Ald_Oxase/Xan_DH_a/b_sf
IPR016208 Ald_Oxase/xanthine_DH
IPR014313 Aldehyde_oxidase
IPR008274 AldOxase/xan_DH_Mopterin-bd
IPR037165 AldOxase/xan_DH_Mopterin-bd_sf
IPR005107 CO_DH_flav_C
IPR036683 CO_DH_flav_C_dom_sf
IPR016166 FAD-bd_PCMH
IPR036318 FAD-bd_PCMH-like_sf
IPR002346 Mopterin_DH_FAD-bd
IPR022407 OxRdtase_Mopterin_BS
PfamiView protein in 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
PIRSFiPIRSF000127 Xanthine_DH, 1 hit
SMARTiView protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit
SUPFAMiSSF47741 SSF47741, 1 hit
SSF54292 SSF54292, 1 hit
SSF54665 SSF54665, 1 hit
SSF55447 SSF55447, 1 hit
SSF56003 SSF56003, 1 hit
SSF56176 SSF56176, 1 hit
TIGRFAMsiTIGR02969 mam_aldehyde_ox, 1 hit
PROSITEiView protein in PROSITE
PS00197 2FE2S_FER_1, 1 hit
PS51085 2FE2S_FER_2, 1 hit
PS51387 FAD_PCMH, 1 hit
PS00559 MOLYBDOPTERIN_EUK, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAOXA_RABIT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P80456
Secondary accession number(s): Q9XTA9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 15, 2002
Last modified: January 16, 2019
This is version 140 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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