Xanthine dehydrogenase/oxidase - Mus musculus (Mouse)

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Q00519 (XDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Xanthine dehydrogenase/oxidase

Including the following 2 domains:

Xanthine dehydrogenase
Short name=XD
EC=1.17.1.4
Xanthine oxidase
Short name=XO
EC=1.17.3.2
Alternative name(s):
Xanthine oxidoreductase
Short name=XOR

Gene names

Name:

Xdh

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 ion (molybdopterin) per subunit.
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 component	Cytoplasm Peroxisome Secreted
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara lactation Inferred from mutant phenotype PubMed 12502743. Source: MGI negative regulation of endothelial cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of gene expression Inferred from electronic annotation. Source: Compara negative regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara negative regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara negative regulation of vascular endothelial growth factor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of vasculogenesis Inferred from electronic annotation. Source: Compara positive regulation of p38MAPK cascade Inferred from electronic annotation. Source: Compara positive regulation of reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara 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_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2 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 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 1335

1334

Xanthine dehydrogenase/oxidase

PRO_0000166085

Regions

Domain

7 – 94

2Fe-2S ferredoxin-type

Domain

231 – 416

186

FAD-binding PCMH-type

Nucleotide binding

259 – 266

FAD By similarity

Nucleotide binding

349 – 353

FAD By similarity

Sites

Active site

1264

Proton acceptor By similarity

Metal binding

Iron-sulfur 1 By similarity

Metal binding

Iron-sulfur 1 By similarity

Metal binding

Iron-sulfur 1 By similarity

Metal binding

Iron-sulfur 1 By similarity

Metal binding

115

Iron-sulfur 2 By similarity

Metal binding

118

Iron-sulfur 2 By similarity

Metal binding

150

Iron-sulfur 2 By similarity

Metal binding

152

Iron-sulfur 2 By similarity

Metal binding

770

Molybdenum By similarity

Metal binding

801

Molybdenum; via carbonyl oxygen By similarity

Metal binding

915

Molybdenum; via amide nitrogen By similarity

Metal binding

1082

Molybdenum; via amide nitrogen By similarity

Binding site

339

FAD By similarity

Binding site

362

FAD By similarity

Binding site

406

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

424

FAD By similarity

Binding site

805

Substrate By similarity

Binding site

883

Substrate By similarity

Binding site

917

Substrate By similarity

Binding site

1013

Substrate; via amide nitrogen By similarity

Amino acid modifications

Glycosylation

1076

N-linked (GlcNAc...) Potential

Disulfide bond

538 ↔ 995

In oxidase form By similarity

Experimental info

Sequence conflict

241

V → I in CAA44705. Ref.2

Sequence conflict

621

M → T in CAA52997. Ref.1

Sequence conflict

1247

L → V in CAA52997. Ref.1

Sequence conflict

1247

L → V in CAA44705. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q00519 [UniParc].

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

1,335

146,562

        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' referencesShow '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. 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 X75150 Genomic DNA. Translation: CAA52997.1. X62932 mRNA. Translation: CAA44705.1. AC159187 Genomic DNA. No translation available. CT025731 Genomic DNA. No translation available.
IPI	IPI00352984.
PIR	XOMSDH. I48374.
RefSeq	NP_035853.2. NM_011723.2.
UniGene	Mm.11223.
3D structure databases
ProteinModelPortal	Q00519.
SMR	Q00519. Positions 7-166, 197-530, 574-1318.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000024866.
PTM databases
PhosphoSite	Q00519.
Proteomic databases
PaxDb	Q00519.
PRIDE	Q00519.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024866; ENSMUSP00000024866; ENSMUSG00000024066.
GeneID	22436.
KEGG	mmu:22436.
Organism-specific databases
CTD	7498.
MGI	MGI:98973. Xdh.
Phylogenomic databases
eggNOG	COG4630.
GeneTree	ENSGT00390000003772.
HOGENOM	HOG000191197.
HOVERGEN	HBG004182.
InParanoid	Q00519.
KO	K00106.
OMA	FKNMLFP.
OrthoDB	EOG45X7V8.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14019.
Gene expression databases
ArrayExpress	Q00519.
Bgee	Q00519.
CleanEx	MM_XDH.
Genevestigator	Q00519.
GermOnline	ENSMUSG00000024066. Mus musculus.
Family and domain databases
Gene3D	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.
InterPro	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]
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. [Graphical view]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR02963. xanthine_xdhA. 1 hit. TIGR02965. xanthine_xdhB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	XDH. mouse.
NextBio	302885.
SOURCE	Search...

Entry information

Entry name

XDH_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents