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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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-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 1By similarity
Metal bindingi51 – 511Iron-sulfur 1By similarity
Metal bindingi54 – 541Iron-sulfur 1By similarity
Metal bindingi76 – 761Iron-sulfur 1By similarity
Metal bindingi115 – 1151Iron-sulfur 2By similarity
Metal bindingi118 – 1181Iron-sulfur 2By similarity
Metal bindingi150 – 1501Iron-sulfur 2By similarity
Metal bindingi152 – 1521Iron-sulfur 2By similarity
Binding sitei339 – 3391FADBy similarity
Binding sitei362 – 3621FADBy similarity
Binding sitei406 – 4061FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei424 – 4241FADBy similarity
Metal bindingi770 – 7701MolybdenumBy similarity
Metal bindingi801 – 8011Molybdenum; via carbonyl oxygenBy similarity
Binding sitei805 – 8051SubstrateBy similarity
Binding sitei883 – 8831SubstrateBy similarity
Metal bindingi915 – 9151Molybdenum; via amide nitrogenBy similarity
Binding sitei917 – 9171SubstrateBy similarity
Binding sitei1013 – 10131Substrate; via amide nitrogenBy similarity
Metal bindingi1082 – 10821Molybdenum; via amide nitrogenBy similarity
Active sitei1264 – 12641Proton acceptorBy similarity

Regions

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

GO - Molecular functioni

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

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.
ReactomeiREACT_253802. Purine catabolism.
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 space Source: Ensembl
  2. peroxisome Source: UniProtKB-KW
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/oxidasePRO_0000166085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi538 ↔ 995In oxidase formBy similarity
Glycosylationi1076 – 10761N-linked (GlcNAc...)Sequence Analysis

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

BgeeiQ00519.
CleanExiMM_XDH.
ExpressionAtlasiQ00519. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG
60 70 80 90 100
CGACTVMISK YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL
110 120 130 140 150
HPVQERIAKS HGSQCGFCTP GIVMSMYTLL RNKPEPTVEE IENAFQGNLC
160 170 180 190 200
RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN CCMSQTKDQT IAPSSSLFNP
210 220 230 240 250
EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ VSTMEELLDL
260 270 280 290 300
KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS
310 320 330 340 350
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI
360 370 380 390 400
GGNIITASPI SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL
410 420 430 440 450
SPEEILVSIV IPYSRKGEFF SAFKQASRRE DDIAKVTSGM RVLFKPGTTE
460 470 480 490 500
VQELSLCFGG MADRTVSALK TTPKQLSKSW NEELLQDVCA GLAEELHLAP
510 520 530 540 550
DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK LDPTFASATL
560 570 580 590 600
LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP
610 620 630 640 650
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG
660 670 680 690 700
IFNDETVFAK DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT
710 720 730 740 750
IQDAIKNNSF YGPEVKIEKG DLKKGFSEAD NVVSGELYIG GQEHFYLETH
760 770 780 790 800
CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA KMLGVPDNRI VVRVKRMGGG
810 820 830 840 850
FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG GRHPFLAKYK
860 870 880 890 900
VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT
910 920 930 940 950
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY
960 970 980 990 1000
KEGDLTHFNQ KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG
1010 1020 1030 1040 1050
LCIIPTKFGI SFTLSFLNQG GALVHVYTDG SVLLTHGGTE MGQGLHTKMV
1060 1070 1080 1090 1100
QVASRALKIP TSKIHITETS TNTVPNTSPT AASASADLNG QAIYEACQTI
1110 1120 1130 1140 1150
LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN LGYSFETNSG
1160 1170 1180 1190 1200
NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG
1210 1220 1230 1240 1250
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC
1260 1270 1280 1290 1300
PNKRAIYASK AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD
1310 1320 1330
SPATPEKIRN ACVDQFTTLC ATGTPENCKS WSVRI
Length:1,335
Mass (Da):146,562
Last modified:July 27, 2011 - v5
Checksum:i56AD3E0C75E00F98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411V → I in CAA44705. (PubMed:1590774)Curated
Sequence conflicti621 – 6211M → T in CAA52997. (PubMed:7835888)Curated
Sequence conflicti1247 – 12471L → V in CAA52997. (PubMed:7835888)Curated
Sequence conflicti1247 – 12471L → V in CAA44705. (PubMed:1590774)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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.
Reactomei REACT_253802. Purine catabolism.
SABIO-RK Q00519.

Miscellaneous databases

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

Gene expression databases

Bgeei Q00519.
CleanExi MM_XDH.
ExpressionAtlasi Q00519. baseline and differential.
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: November 26, 2014
This is version 137 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