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Q00519

- XDH_MOUSE

UniProt

Q00519 - XDH_MOUSE

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Protein
Xanthine dehydrogenase/oxidase
Gene
Xdh
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.
Xanthine + H2O + O2 = urate + H2O2.

Cofactori

Binds 2 2Fe-2S clusters By similarity.
FAD By similarity.
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Iron-sulfur 1 By similarity
Metal bindingi51 – 511Iron-sulfur 1 By similarity
Metal bindingi54 – 541Iron-sulfur 1 By similarity
Metal bindingi76 – 761Iron-sulfur 1 By similarity
Metal bindingi115 – 1151Iron-sulfur 2 By similarity
Metal bindingi118 – 1181Iron-sulfur 2 By similarity
Metal bindingi150 – 1501Iron-sulfur 2 By similarity
Metal bindingi152 – 1521Iron-sulfur 2 By similarity
Binding sitei339 – 3391FAD By similarity
Binding sitei362 – 3621FAD By similarity
Binding sitei406 – 4061FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei424 – 4241FAD By similarity
Metal bindingi770 – 7701Molybdenum By similarity
Metal bindingi801 – 8011Molybdenum; via carbonyl oxygen By similarity
Binding sitei805 – 8051Substrate By similarity
Binding sitei883 – 8831Substrate By similarity
Metal bindingi915 – 9151Molybdenum; via amide nitrogen By similarity
Binding sitei917 – 9171Substrate By similarity
Binding sitei1013 – 10131Substrate; via amide nitrogen By similarity
Metal bindingi1082 – 10821Molybdenum; via amide nitrogen By similarity
Active sitei1264 – 12641Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi259 – 2668FAD By similarity
Nucleotide bindingi349 – 3535FAD By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  3. electron carrier activity Source: InterPro
  4. flavin adenine dinucleotide binding Source: UniProtKB
  5. iron ion binding Source: InterPro
  6. molybdenum ion binding Source: InterPro
  7. molybdopterin cofactor binding Source: UniProtKB
  8. oxidoreductase activity Source: MGI
  9. protein binding Source: MGI
  10. xanthine dehydrogenase activity Source: UniProtKB
  11. xanthine oxidase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. lactation Source: MGI
  3. negative regulation of endothelial cell differentiation Source: Ensembl
  4. negative regulation of endothelial cell proliferation Source: Ensembl
  5. negative regulation of gene expression Source: Ensembl
  6. negative regulation of protein kinase B signaling Source: Ensembl
  7. negative regulation of protein phosphorylation Source: Ensembl
  8. negative regulation of vascular endothelial growth factor signaling pathway Source: Ensembl
  9. negative regulation of vasculogenesis Source: Ensembl
  10. oxidation-reduction process Source: MGI
  11. positive regulation of p38MAPK cascade Source: Ensembl
  12. positive regulation of reactive oxygen species metabolic process Source: Ensembl
  13. regulation of epithelial cell differentiation Source: MGI
  14. xanthine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14019.
SABIO-RKQ00519.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Xanthine oxidase (EC:1.17.3.2)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
Gene namesi
Name:Xdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:98973. Xdh.

Subcellular locationi

Cytoplasm By similarity. Peroxisome By similarity. Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13351334Xanthine dehydrogenase/oxidase
PRO_0000166085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi538 ↔ 995In oxidase form By similarity
Glycosylationi1076 – 10761N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ00519.
PaxDbiQ00519.
PRIDEiQ00519.

PTM databases

PhosphoSiteiQ00519.

Expressioni

Inductioni

By interferon.

Gene expression databases

ArrayExpressiQ00519.
BgeeiQ00519.
CleanExiMM_XDH.
GenevestigatoriQ00519.

Interactioni

Subunit structurei

Homodimer. Interacts with BTN1A1.1 Publication

Protein-protein interaction databases

IntActiQ00519. 2 interactions.
MINTiMINT-1866314.
STRINGi10090.ENSMUSP00000024866.

Structurei

3D structure databases

ProteinModelPortaliQ00519.
SMRiQ00519. Positions 7-166, 197-530, 574-1318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 94882Fe-2S ferredoxin-type
Add
BLAST
Domaini231 – 416186FAD-binding PCMH-type
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4630.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ00519.
KOiK00106.
OMAiCDETFFA.
OrthoDBiEOG7QRQSZ.
TreeFamiTF353036.

Family and domain databases

Gene3Di1.10.150.120. 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.
InterProiIPR002888. 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]
PfamiPF01315. 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]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00519-1 [UniParc]FASTAAdd to Basket

« Hide

MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG     50
CGACTVMISK YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL 100
HPVQERIAKS HGSQCGFCTP GIVMSMYTLL RNKPEPTVEE IENAFQGNLC 150
RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN CCMSQTKDQT IAPSSSLFNP 200
EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ VSTMEELLDL 250
KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS 300
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI 350
GGNIITASPI SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL 400
SPEEILVSIV IPYSRKGEFF SAFKQASRRE DDIAKVTSGM RVLFKPGTTE 450
VQELSLCFGG MADRTVSALK TTPKQLSKSW NEELLQDVCA GLAEELHLAP 500
DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK LDPTFASATL 550
LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP 600
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG 650
IFNDETVFAK DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT 700
IQDAIKNNSF YGPEVKIEKG DLKKGFSEAD NVVSGELYIG GQEHFYLETH 750
CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA KMLGVPDNRI VVRVKRMGGG 800
FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG GRHPFLAKYK 850
VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT 900
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY 950
KEGDLTHFNQ KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG 1000
LCIIPTKFGI SFTLSFLNQG GALVHVYTDG SVLLTHGGTE MGQGLHTKMV 1050
QVASRALKIP TSKIHITETS TNTVPNTSPT AASASADLNG QAIYEACQTI 1100
LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN LGYSFETNSG 1150
NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG 1200
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC 1250
PNKRAIYASK AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD 1300
SPATPEKIRN ACVDQFTTLC ATGTPENCKS WSVRI 1335
Length:1,335
Mass (Da):146,562
Last modified:July 27, 2011 - v5
Checksum:i56AD3E0C75E00F98
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411V → I in CAA44705. 1 Publication
Sequence conflicti621 – 6211M → T in CAA52997. 1 Publication
Sequence conflicti1247 – 12471L → V in CAA52997. 1 Publication
Sequence conflicti1247 – 12471L → V in CAA44705. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75129
, 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.
CCDSiCCDS28967.1.
PIRiI48374. XOMSDH.
RefSeqiNP_035853.2. NM_011723.3.
UniGeneiMm.11223.

Genome annotation databases

EnsembliENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
GeneIDi22436.
KEGGimmu:22436.
UCSCiuc008dno.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75129
, 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.
CCDSi CCDS28967.1.
PIRi I48374. XOMSDH.
RefSeqi NP_035853.2. NM_011723.3.
UniGenei Mm.11223.

3D structure databases

ProteinModelPortali Q00519.
SMRi Q00519. Positions 7-166, 197-530, 574-1318.
ModBasei Search...

Protein-protein interaction databases

IntActi Q00519. 2 interactions.
MINTi MINT-1866314.
STRINGi 10090.ENSMUSP00000024866.

PTM databases

PhosphoSitei Q00519.

Proteomic databases

MaxQBi Q00519.
PaxDbi Q00519.
PRIDEi Q00519.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024866 ; ENSMUSP00000024866 ; ENSMUSG00000024066 .
GeneIDi 22436.
KEGGi mmu:22436.
UCSCi uc008dno.1. mouse.

Organism-specific databases

CTDi 7498.
MGIi MGI:98973. Xdh.

Phylogenomic databases

eggNOGi COG4630.
GeneTreei ENSGT00390000003772.
HOGENOMi HOG000191197.
HOVERGENi HBG004182.
InParanoidi Q00519.
KOi K00106.
OMAi CDETFFA.
OrthoDBi EOG7QRQSZ.
TreeFami TF353036.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-14019.
SABIO-RK Q00519.

Miscellaneous databases

ChiTaRSi XDH. mouse.
NextBioi 302885.
PROi Q00519.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00519.
Bgeei Q00519.
CleanExi MM_XDH.
Genevestigatori Q00519.

Family and domain databases

Gene3Di 1.10.150.120. 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.
InterProi IPR002888. 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 ]
Pfami 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 ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
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.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
TIGR02965. xanthine_xdhB. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiXDH_MOUSE
AccessioniPrimary (citable) accession number: Q00519
Secondary accession number(s): E9QLM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi