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Q00519 (XDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xanthine dehydrogenase/oxidase

Including the following 2 domains:

  1. Xanthine dehydrogenase
    Short name=XD
    EC=1.17.1.4
  2. Xanthine oxidase
    Short name=XO
    EC=1.17.3.2
    Alternative name(s):
    Xanthine oxidoreductase
    Short name=XOR
Gene names
Name:Xdh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species By similarity.

Catalytic activity

Xanthine + NAD+ + H2O = urate + NADH.

Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Xanthine + H2O + O2 = urate + H2O2.

Cofactor

Binds 2 2Fe-2S clusters By similarity.

FAD By similarity.

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Enzyme regulation

Can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups By similarity.

Subunit structure

Homodimer. Interacts with BTN1A1. Ref.4

Subcellular location

Cytoplasm By similarity. Peroxisome By similarity. Secreted By similarity.

Induction

By interferon.

Post-translational modification

Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O) By similarity.

Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O) By similarity.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Peroxisome
Secreted
   Ligand2Fe-2S
FAD
Flavoprotein
Iron
Iron-sulfur
Metal-binding
Molybdenum
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from mutant phenotype PubMed 12502743. Source: MGI

negative regulation of endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular endothelial growth factor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of vasculogenesis

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay PubMed 17597094. Source: MGI

positive regulation of p38MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 12502743. Source: MGI

xanthine catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

UDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

molybdenum ion binding

Inferred from electronic annotation. Source: InterPro

molybdopterin cofactor binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxidoreductase activity

Inferred from direct assay PubMed 17597094. Source: MGI

xanthine dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

xanthine oxidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 13351334Xanthine dehydrogenase/oxidase
PRO_0000166085

Regions

Domain7 – 94882Fe-2S ferredoxin-type
Domain231 – 416186FAD-binding PCMH-type
Nucleotide binding259 – 2668FAD By similarity
Nucleotide binding349 – 3535FAD By similarity

Sites

Active site12641Proton acceptor By similarity
Metal binding461Iron-sulfur 1 By similarity
Metal binding511Iron-sulfur 1 By similarity
Metal binding541Iron-sulfur 1 By similarity
Metal binding761Iron-sulfur 1 By similarity
Metal binding1151Iron-sulfur 2 By similarity
Metal binding1181Iron-sulfur 2 By similarity
Metal binding1501Iron-sulfur 2 By similarity
Metal binding1521Iron-sulfur 2 By similarity
Metal binding7701Molybdenum By similarity
Metal binding8011Molybdenum; via carbonyl oxygen By similarity
Metal binding9151Molybdenum; via amide nitrogen By similarity
Metal binding10821Molybdenum; via amide nitrogen By similarity
Binding site3391FAD By similarity
Binding site3621FAD By similarity
Binding site4061FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4241FAD By similarity
Binding site8051Substrate By similarity
Binding site8831Substrate By similarity
Binding site9171Substrate By similarity
Binding site10131Substrate; via amide nitrogen By similarity

Amino acid modifications

Glycosylation10761N-linked (GlcNAc...) Potential
Disulfide bond538 ↔ 995In oxidase form By similarity

Experimental info

Sequence conflict2411V → I in CAA44705. Ref.2
Sequence conflict6211M → T in CAA52997. Ref.1
Sequence conflict12471L → V in CAA52997. Ref.1
Sequence conflict12471L → V in CAA44705. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q00519 [UniParc].

Last modified July 27, 2011. Version 5.
Checksum: 56AD3E0C75E00F98

FASTA1,335146,562
        10         20         30         40         50         60 
MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG CGACTVMISK 

        70         80         90        100        110        120 
YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL HPVQERIAKS HGSQCGFCTP 

       130        140        150        160        170        180 
GIVMSMYTLL RNKPEPTVEE IENAFQGNLC RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN 

       190        200        210        220        230        240 
CCMSQTKDQT IAPSSSLFNP EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ 

       250        260        270        280        290        300 
VSTMEELLDL KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS 

       310        320        330        340        350        360 
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI GGNIITASPI 

       370        380        390        400        410        420 
SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL SPEEILVSIV IPYSRKGEFF 

       430        440        450        460        470        480 
SAFKQASRRE DDIAKVTSGM RVLFKPGTTE VQELSLCFGG MADRTVSALK TTPKQLSKSW 

       490        500        510        520        530        540 
NEELLQDVCA GLAEELHLAP DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK 

       550        560        570        580        590        600 
LDPTFASATL LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP 

       610        620        630        640        650        660 
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG IFNDETVFAK 

       670        680        690        700        710        720 
DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT IQDAIKNNSF YGPEVKIEKG 

       730        740        750        760        770        780 
DLKKGFSEAD NVVSGELYIG GQEHFYLETH CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA 

       790        800        810        820        830        840 
KMLGVPDNRI VVRVKRMGGG FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG 

       850        860        870        880        890        900 
GRHPFLAKYK VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT 

       910        920        930        940        950        960 
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY KEGDLTHFNQ 

       970        980        990       1000       1010       1020 
KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG LCIIPTKFGI SFTLSFLNQG 

      1030       1040       1050       1060       1070       1080 
GALVHVYTDG SVLLTHGGTE MGQGLHTKMV QVASRALKIP TSKIHITETS TNTVPNTSPT 

      1090       1100       1110       1120       1130       1140 
AASASADLNG QAIYEACQTI LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN 

      1150       1160       1170       1180       1190       1200 
LGYSFETNSG NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG 

      1210       1220       1230       1240       1250       1260 
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC PNKRAIYASK 

      1270       1280       1290       1300       1310       1320 
AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD SPATPEKIRN ACVDQFTTLC 

      1330 
ATGTPENCKS WSVRI 

« Hide

References

« Hide 'large scale' references
[1]"Chromosomal mapping, isolation, and characterization of the mouse xanthine dehydrogenase gene."
Cazzaniga G., Terao M., Lo Schiavo P., Galbiati F., Segalla F., Seldin M.F., Garattini E.
Genomics 23:390-402(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
Tissue: Spleen.
[2]"Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase. Regulation of its transcript by interferons in vivo."
Terao M., Cazzaniga G., Ghezzi P., Bianchi M., Falciani F., Perani P., Garattini E.
Biochem. J. 283:863-870(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane."
Ishii T., Aoki N., Noda A., Adachi T., Nakamura R., Matsuda T.
Biochim. Biophys. Acta 1245:285-292(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9, INTERACTION WITH BTN1A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75129 expand/collapse EMBL AC list , X75128, X75127, X75126, X75125, X75124, X75123, X75122, X75121, X75120, X75119, X75130, X75131, X75132, X75133, X75134, X75135, X75136, X75137, X75138, X75139, X75140, X75141, X75142, X75143, X75151, X75152, X75153, X75154, X75144, X75145, X75146, X75147, X75148, X75149, X75150 Genomic DNA. Translation: CAA52997.1.
X62932 mRNA. Translation: CAA44705.1.
AC159187 Genomic DNA. No translation available.
CT025731 Genomic DNA. No translation available.
PIRXOMSDH. I48374.
RefSeqNP_035853.2. NM_011723.3.
UniGeneMm.11223.

3D structure databases

ProteinModelPortalQ00519.
SMRQ00519. Positions 7-166, 197-530, 574-1318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ00519. 2 interactions.
MINTMINT-1866314.
STRING10090.ENSMUSP00000024866.

PTM databases

PhosphoSiteQ00519.

Proteomic databases

PaxDbQ00519.
PRIDEQ00519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
GeneID22436.
KEGGmmu:22436.
UCSCuc008dno.1. mouse.

Organism-specific databases

CTD7498.
MGIMGI:98973. Xdh.

Phylogenomic databases

eggNOGCOG4630.
GeneTreeENSGT00390000003772.
HOGENOMHOG000191197.
HOVERGENHBG004182.
InParanoidQ00519.
KOK00106.
OMACDETFFA.
OrthoDBEOG7QRQSZ.
TreeFamTF353036.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14019.

Gene expression databases

ArrayExpressQ00519.
BgeeQ00519.
CleanExMM_XDH.
GenevestigatorQ00519.

Family and domain databases

Gene3D1.10.150.120. 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.
InterProIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
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.
IPR014309. Xanthine_DH_Mopterin-bd_su.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamPF01315. 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]
PIRSFPIRSF000127. Xanthine_DH. 1 hit.
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsTIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSXDH. mouse.
NextBio302885.
PROQ00519.
SOURCESearch...

Entry information

Entry nameXDH_MOUSE
AccessionPrimary (citable) accession number: Q00519
Secondary accession number(s): E9QLM9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 131 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot