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Protein

Xanthine dehydrogenase/oxidase

Gene

Xdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.2 Publications
Hypoxanthine + NAD+ + H2O = xanthine + NADH.2 Publications
Xanthine + H2O + O2 = urate + H2O2.2 Publications

Cofactori

Protein has several cofactor binding sites:

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Iron-sulfur 11
Metal bindingi48Iron-sulfur 11
Metal bindingi51Iron-sulfur 11
Metal bindingi73Iron-sulfur 11
Metal bindingi112Iron-sulfur 21
Metal bindingi115Iron-sulfur 21
Metal bindingi147Iron-sulfur 21
Metal bindingi149Iron-sulfur 21
Binding sitei336FADBy similarity1
Binding sitei359FAD2 Publications1
Binding sitei403FAD; via amide nitrogen and carbonyl oxygen2 Publications1
Binding sitei421FADBy similarity1
Metal bindingi767MolybdenumBy similarity1
Metal bindingi798Molybdenum; via carbonyl oxygenBy similarity1
Binding sitei802Substrate1
Binding sitei880Substrate1
Metal bindingi912Molybdenum; via amide nitrogenBy similarity1
Binding sitei914SubstrateBy similarity1
Binding sitei1010Substrate; via amide nitrogen1
Metal bindingi1079Molybdenum; via amide nitrogenBy similarity1
Active sitei1261Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi256 – 263FAD2 Publications8
Nucleotide bindingi346 – 350FAD2 Publications5

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: InterPro
  • flavin adenine dinucleotide binding Source: UniProtKB
  • iron ion binding Source: InterPro
  • molybdopterin cofactor binding Source: UniProtKB
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: GO_Central
  • xanthine dehydrogenase activity Source: UniProtKB
  • xanthine oxidase activity Source: UniProtKB

GO - Biological processi

  • bone resorption Source: RGD
  • response to aluminum ion Source: RGD
  • 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-15163.
BRENDAi1.17.1.4. 5301.
1.17.3.2. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.42 Publications)
Short name:
XD
Xanthine oxidase (EC:1.17.3.22 Publications)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
Gene namesi
Name:Xdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62043. Xdh.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular space Source: RGD
  • peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi335 – 336WF → AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication2
Mutagenesisi535C → A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316. 1 Publication1
Mutagenesisi992C → R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316. 1 Publication1
Mutagenesisi1316C → S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075246.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001660862 – 1331Xanthine dehydrogenase/oxidaseAdd BLAST1330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi535 ↔ 992In oxidase form1 Publication
Glycosylationi1073N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP22985.
PRIDEiP22985.

PTM databases

iPTMnetiP22985.
PhosphoSitePlusiP22985.

Expressioni

Inductioni

By interferon.

Interactioni

Subunit structurei

Homodimer. Interacts with BTN1A1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009634.

Chemistry databases

BindingDBiP22985.

Structurei

Secondary structure

11331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi13 – 17Combined sources5
Helixi26 – 32Combined sources7
Beta strandi44 – 48Combined sources5
Beta strandi52 – 59Combined sources8
Turni60 – 63Combined sources4
Beta strandi64 – 71Combined sources8
Helixi72 – 74Combined sources3
Helixi77 – 79Combined sources3
Beta strandi84 – 86Combined sources3
Helixi88 – 91Combined sources4
Beta strandi94 – 96Combined sources3
Helixi99 – 106Combined sources8
Helixi116 – 129Combined sources14
Helixi135 – 140Combined sources6
Turni141 – 144Combined sources4
Beta strandi148 – 150Combined sources3
Helixi153 – 159Combined sources7
Helixi160 – 162Combined sources3
Helixi197 – 199Combined sources3
Helixi205 – 207Combined sources3
Helixi213 – 218Combined sources6
Beta strandi226 – 229Combined sources4
Beta strandi234 – 237Combined sources4
Helixi241 – 250Combined sources10
Helixi263 – 269Combined sources7
Beta strandi275 – 279Combined sources5
Helixi284 – 287Combined sources4
Beta strandi289 – 291Combined sources3
Beta strandi293 – 299Combined sources7
Helixi304 – 317Combined sources14
Helixi320 – 322Combined sources3
Helixi324 – 334Combined sources11
Helixi339 – 342Combined sources4
Helixi347 – 353Combined sources7
Helixi361 – 366Combined sources6
Beta strandi370 – 375Combined sources6
Beta strandi378 – 383Combined sources6
Helixi386 – 388Combined sources3
Beta strandi402 – 409Combined sources8
Beta strandi415 – 422Combined sources8
Beta strandi424 – 428Combined sources5
Beta strandi432 – 441Combined sources10
Beta strandi445 – 461Combined sources17
Turni466 – 468Combined sources3
Helixi470 – 472Combined sources3
Beta strandi476 – 478Combined sources3
Helixi479 – 492Combined sources14
Helixi504 – 528Combined sources25
Turni529 – 531Combined sources3
Helixi532 – 535Combined sources4
Helixi540 – 546Combined sources7
Beta strandi555 – 559Combined sources5
Beta strandi565 – 567Combined sources3
Helixi582 – 586Combined sources5
Helixi593 – 595Combined sources3
Beta strandi603 – 609Combined sources7
Beta strandi611 – 621Combined sources11
Helixi625 – 627Combined sources3
Beta strandi631 – 635Combined sources5
Helixi637 – 639Combined sources3
Beta strandi645 – 647Combined sources3
Beta strandi652 – 655Combined sources4
Beta strandi658 – 660Combined sources3
Beta strandi666 – 674Combined sources9
Helixi675 – 683Combined sources9
Beta strandi686 – 691Combined sources6
Helixi698 – 703Combined sources6
Beta strandi707 – 710Combined sources4
Beta strandi712 – 717Combined sources6
Helixi719 – 725Combined sources7
Beta strandi727 – 736Combined sources10
Beta strandi748 – 753Combined sources6
Beta strandi760 – 764Combined sources5
Helixi769 – 780Combined sources12
Helixi784 – 786Combined sources3
Beta strandi787 – 792Combined sources6
Turni798 – 801Combined sources4
Beta strandi802 – 804Combined sources3
Helixi806 – 819Combined sources14
Beta strandi823 – 826Combined sources4
Helixi829 – 835Combined sources7
Beta strandi842 – 850Combined sources9
Beta strandi856 – 866Combined sources11
Helixi874 – 883Combined sources10
Turni884 – 888Combined sources5
Beta strandi892 – 901Combined sources10
Turni912 – 915Combined sources4
Helixi916 – 934Combined sources19
Helixi938 – 945Combined sources8
Helixi964 – 974Combined sources11
Helixi977 – 990Combined sources14
Beta strandi992 – 1008Combined sources17
Helixi1012 – 1014Combined sources3
Beta strandi1016 – 1023Combined sources8
Beta strandi1029 – 1034Combined sources6
Beta strandi1038 – 1040Combined sources3
Helixi1042 – 1054Combined sources13
Helixi1058 – 1060Combined sources3
Beta strandi1061 – 1063Combined sources3
Turni1068 – 1070Combined sources3
Turni1079 – 1081Combined sources3
Helixi1082 – 1107Combined sources26
Beta strandi1108 – 1111Combined sources4
Helixi1113 – 1122Combined sources10
Beta strandi1128 – 1134Combined sources7
Turni1142 – 1145Combined sources4
Beta strandi1151 – 1165Combined sources15
Turni1166 – 1168Combined sources3
Beta strandi1171 – 1181Combined sources11
Helixi1188 – 1207Combined sources20
Turni1224 – 1226Combined sources3
Helixi1232 – 1234Combined sources3
Beta strandi1237 – 1243Combined sources7
Turni1250 – 1252Combined sources3
Helixi1253 – 1255Combined sources3
Helixi1264 – 1267Combined sources4
Helixi1268 – 1285Combined sources18
Beta strandi1286 – 1289Combined sources4
Helixi1301 – 1307Combined sources7
Helixi1311 – 1316Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WYGX-ray2.60A1-1331[»]
2E3TX-ray2.28A/B1-1331[»]
3AN1X-ray1.73A/B1-1331[»]
4YRWX-ray1.99A/B1-1315[»]
4YSWX-ray1.99A/B1-1315[»]
4YTYX-ray2.20A/B1-1331[»]
4YTZX-ray2.30A/B1-1315[»]
ProteinModelPortaliP22985.
SMRiP22985.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22985.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini228 – 413FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

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

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP22985.
KOiK00106.
PhylomeDBiP22985.

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.
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.
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.

P22985-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA
60 70 80 90 100
CTVMISKYDR LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV
110 120 130 140 150
QERIARSHGS QCGFCTPGIV MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT
160 170 180 190 200
GYRPILQGFR TFAKDGGCCG GSGNNPNCCM NQTKDQTVSL SPSLFNPEDF
210 220 230 240 250
KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST MEELLDLKAQ
260 270 280 290 300
HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
310 320 330 340 350
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN
360 370 380 390 400
IITASPISDL NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE
410 420 430 440 450
EILLSIEIPY SKEGEFFSAF KQASRREDDI AKVTSGMRVL FKPGTIEVQE
460 470 480 490 500
LSLCFGGMAD RTISALKTTP KQLSKSWNEE LLQSVCAGLA EELQLAPDAP
510 520 530 540 550
GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP TFASATLLFQ
560 570 580 590 600
KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
610 620 630 640 650
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN
660 670 680 690 700
DETVFAKDEV TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD
710 720 730 740 750
AINNNSFYGS EIKIEKGDLK KGFSEADNVV SGELYIGGQE HFYLETNCTI
760 770 780 790 800
AVPKGEAGEM ELFVSTQNTM KTQSFVAKML GVPDNRIVVR VKRMGGGFGG
810 820 830 840 850
KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH PFLAKYKVGF
860 870 880 890 900
MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
910 920 930 940 950
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG
960 970 980 990 1000
DLTHFNQKLE GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI
1010 1020 1030 1040 1050
IPTKFGISFT LPFLNQGGAL VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA
1060 1070 1080 1090 1100
SRALKIPTSK IHISETSTNT VPNTSPTAAS ASADLNGQGV YEACQTILKR
1110 1120 1130 1140 1150
LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY SFETNSGNPF
1160 1170 1180 1190 1200
HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1210 1220 1230 1240 1250
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK
1260 1270 1280 1290 1300
RAIYASKAVG EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT
1310 1320 1330
PEKIRNACVD QFTTLCVTGV PENCKSWSVR I
Length:1,331
Mass (Da):146,243
Last modified:January 23, 2007 - v3
Checksum:iBF2586A9C63A0B2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05579 mRNA. Translation: AAA42349.1.
AH000836 Unassigned DNA. Translation: AAA18869.1.
RefSeqiNP_058850.1. NM_017154.1.
UniGeneiRn.202951.

Genome annotation databases

GeneIDi497811.
KEGGirno:497811.
UCSCiRGD:62043. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05579 mRNA. Translation: AAA42349.1.
AH000836 Unassigned DNA. Translation: AAA18869.1.
RefSeqiNP_058850.1. NM_017154.1.
UniGeneiRn.202951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WYGX-ray2.60A1-1331[»]
2E3TX-ray2.28A/B1-1331[»]
3AN1X-ray1.73A/B1-1331[»]
4YRWX-ray1.99A/B1-1315[»]
4YSWX-ray1.99A/B1-1315[»]
4YTYX-ray2.20A/B1-1331[»]
4YTZX-ray2.30A/B1-1315[»]
ProteinModelPortaliP22985.
SMRiP22985.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009634.

Chemistry databases

BindingDBiP22985.
ChEMBLiCHEMBL1075246.

PTM databases

iPTMnetiP22985.
PhosphoSitePlusiP22985.

Proteomic databases

PaxDbiP22985.
PRIDEiP22985.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi497811.
KEGGirno:497811.
UCSCiRGD:62043. rat.

Organism-specific databases

CTDi7498.
RGDi62043. Xdh.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP22985.
KOiK00106.
PhylomeDBiP22985.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15163.
BRENDAi1.17.1.4. 5301.
1.17.3.2. 5301.

Miscellaneous databases

EvolutionaryTraceiP22985.
PROiP22985.

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.
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.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXDH_RAT
AccessioniPrimary (citable) accession number: P22985
Secondary accession number(s): Q63157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.