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Protein

Dihydropteridine reductase

Gene

Qdpr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.By similarity

Catalytic activityi

A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 3525NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteridine reductase (EC:1.5.1.34)
Alternative name(s):
HDHPR
Quinoid dihydropteridine reductase
Gene namesi
Name:Qdpr
Synonyms:Dhpr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:97836. Qdpr.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • neuron projection Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Dihydropteridine reductasePRO_0000054637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-succinyllysineCombined sources
Modified residuei76 – 761N6-succinyllysineCombined sources
Modified residuei93 – 931N6-succinyllysineCombined sources
Modified residuei99 – 991N6-succinyllysineCombined sources

Proteomic databases

EPDiQ8BVI4.
MaxQBiQ8BVI4.
PaxDbiQ8BVI4.
PRIDEiQ8BVI4.

2D gel databases

REPRODUCTION-2DPAGEQ8BVI4.

PTM databases

iPTMnetiQ8BVI4.
PhosphoSiteiQ8BVI4.
SwissPalmiQ8BVI4.

Expressioni

Gene expression databases

BgeeiQ8BVI4.
CleanExiMM_QDPR.
ExpressionAtlasiQ8BVI4. baseline and differential.
GenevisibleiQ8BVI4. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8BVI4. 5 interactions.
MINTiMINT-2513757.
STRINGi10090.ENSMUSP00000015950.

Structurei

3D structure databases

ProteinModelPortaliQ8BVI4.
SMRiQ8BVI4. Positions 6-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiQ8BVI4.
KOiK00357.
OMAiANVTVKM.
OrthoDBiEOG7060RV.
PhylomeDBiQ8BVI4.
TreeFamiTF105932.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BVI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVV
60 70 80 90 100
VKMTDSFTEQ ADQVTADVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN
110 120 130 140 150
CDMMWKQSMW TSTISSHLAT KHLKEGGLLT LAGAKAALDG TPGMIGYGMA
160 170 180 190 200
KGAVHQLCQS LAGKNSGMPP GAAAIAVLPV TLDTPMNRKS MPEADFSSWT
210 220 230 240
PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY F
Length:241
Mass (Da):25,570
Last modified:April 12, 2005 - v2
Checksum:i2ED25295D38C494B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671G → D in BAC37135 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011351 mRNA. Translation: BAB27559.1.
AK078123 mRNA. Translation: BAC37135.1.
AK159107 mRNA. Translation: BAE34823.1.
AK161660 mRNA. Translation: BAE36516.1.
AK166694 mRNA. Translation: BAE38951.1.
BC002107 mRNA. Translation: AAH02107.1.
CCDSiCCDS19272.1.
RefSeqiNP_077198.1. NM_024236.2.
XP_011250288.1. XM_011251986.1.
UniGeneiMm.30204.

Genome annotation databases

EnsembliENSMUST00000015950; ENSMUSP00000015950; ENSMUSG00000015806.
GeneIDi102643271.
110391.
KEGGimmu:102643271.
mmu:110391.
UCSCiuc008xix.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011351 mRNA. Translation: BAB27559.1.
AK078123 mRNA. Translation: BAC37135.1.
AK159107 mRNA. Translation: BAE34823.1.
AK161660 mRNA. Translation: BAE36516.1.
AK166694 mRNA. Translation: BAE38951.1.
BC002107 mRNA. Translation: AAH02107.1.
CCDSiCCDS19272.1.
RefSeqiNP_077198.1. NM_024236.2.
XP_011250288.1. XM_011251986.1.
UniGeneiMm.30204.

3D structure databases

ProteinModelPortaliQ8BVI4.
SMRiQ8BVI4. Positions 6-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BVI4. 5 interactions.
MINTiMINT-2513757.
STRINGi10090.ENSMUSP00000015950.

PTM databases

iPTMnetiQ8BVI4.
PhosphoSiteiQ8BVI4.
SwissPalmiQ8BVI4.

2D gel databases

REPRODUCTION-2DPAGEQ8BVI4.

Proteomic databases

EPDiQ8BVI4.
MaxQBiQ8BVI4.
PaxDbiQ8BVI4.
PRIDEiQ8BVI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015950; ENSMUSP00000015950; ENSMUSG00000015806.
GeneIDi102643271.
110391.
KEGGimmu:102643271.
mmu:110391.
UCSCiuc008xix.2. mouse.

Organism-specific databases

CTDi5860.
MGIiMGI:97836. Qdpr.

Phylogenomic databases

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiQ8BVI4.
KOiK00357.
OMAiANVTVKM.
OrthoDBiEOG7060RV.
PhylomeDBiQ8BVI4.
TreeFamiTF105932.

Enzyme and pathway databases

ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

PROiQ8BVI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVI4.
CleanExiMM_QDPR.
ExpressionAtlasiQ8BVI4. baseline and differential.
GenevisibleiQ8BVI4. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-93; 125-135; 165-188 AND 218-233, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain and Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-93 AND LYS-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDHPR_MOUSE
AccessioniPrimary (citable) accession number: Q8BVI4
Secondary accession number(s): Q3TT09, Q9D0K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: June 8, 2016
This is version 113 of the entry and version 2 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

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.