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UniProtKB/Swiss-Prot entry Q8BVI4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHPR_MOUSE
Primary accession number Q8BVI4
Secondary accession numbers Q3TT09 Q9D0K4
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on April 12, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Dihydropteridine reductase
Synonyms EC 1.5.1.34
HDHPR
Quinoid dihydropteridine reductase
Gene name
Name: Qdpr
Synonyms: Dhpr
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Medulla oblongata;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 77-93; 165-188 AND 218-233, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 125-135, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK011351; BAB27559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK078123; BAC37135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK159107; BAE34823.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK161660; BAE36516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166694; BAE38951.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002107; AAH02107.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_077198.1; -.
UniGene Mm.30204
3D structure databases
HSSP P11348; 1DHR. [HSSP ENTRY / PDB]
SMR Q8BVI4; 6-241.
ModBase Q8BVI4.
2D gel databases
REPRODUCTION-2DPAGE Q8BVI4; -.
Organism-specific databases
MGI MGI:97836; Qdpr.
Gene expression databases
ArrayExpress Q8BVI4; -.
CleanEx MM_QDPR; -.
GermOnline ENSMUSG00000015806; Mus musculus.
Ontologies
GO
GO:0004155; Molecular function: 6,7-dihydropteridine reductase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006729; Biological process: tetrahydrobiopterin biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PROSITE PS00061; ADH_SHORT; 1.
BLOCKS Q8BVI4.
Genome annotation databases
Ensembl ENSMUSG00000015806; Mus musculus. [Contig view]
GeneID 110391; -.
KEGG mmu:110391; -.
NMPDR fig|10090.3.peg.11568; -.
Phylogenomic databases
HOGENOM Q8BVI4; -.
HOVERGEN Q8BVI4; -.
Other
SOURCE Qdpr; Mus musculus.
ProtoNet Q8BVI4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; NADP; Oxidoreductase; Tetrahydrobiopterin biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   241  240     Dihydropteridine reductase. PRO_0000054637
NP_BIND   11    35  25     NADP (By similarity). 
ACT_SITE   147   147        Proton acceptor (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
CONFLICT   167   167        G -> D (in Ref. 1; BAC37135). 
Sequence information
Length: 241 AA [This is the length of the unprocessed precursor] Molecular weight: 25570 Da [This is the MW of the unprocessed precursor] CRC64: 2ED25295D38C494B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVV VKMTDSFTEQ 

        70         80         90        100        110        120 
ADQVTADVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN CDMMWKQSMW TSTISSHLAT 

       130        140        150        160        170        180 
KHLKEGGLLT LAGAKAALDG TPGMIGYGMA KGAVHQLCQS LAGKNSGMPP GAAAIAVLPV 

       190        200        210        220        230        240 
TLDTPMNRKS MPEADFSSWT PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY 


F 

Q8BVI4 in FASTA format

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