Reviewed, UniProtKB/Swiss-Prot Q8BVI4 (DHPR_MOUSE)

Names and origin

Protein names

Recommended name:
    Dihydropteridine reductase
    EC=1.5.1.34
Alternative name(s):
    HDHPR
    Quinoid dihydropteridine reductase

Gene names

Name:	Qdpr
Synonyms:	Dhpr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	241 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	The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases By similarity.
Catalytic activity	A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrobiopterin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	6,7-dihydropteridine reductase activity Inferred from sequence or structural similarity. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 241	240	Dihydropteridine reductase		PRO_0000054637
Regions
	Nucleotide binding	11 – 35	25	NADP By similarity
Sites
	Active site	147	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	167	1	G → D in BAC37135. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BVI4-1 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 2ED25295D38C494B	FASTA	241	25,570
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [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: 15489334] [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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00459279.
RefSeq	NP_077198.1.
UniGene	Mm.30204
3D structure databases
HSSP	HSSP built from PDB template 1DHR based on UniProtKB P11348.
SMR	Q8BVI4. Positions 6-241.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BVI4.
2-D gel databases
REPRODUCTION-2DPAGE	Q8BVI4.
Proteomic databases
PRIDE	Q8BVI4.
Genome annotation databases
Ensembl	ENSMUST00000015950; ENSMUSP00000015950; ENSMUSG00000015806; Mus musculus. [Genome view]
GeneID	110391.
KEGG	mmu:110391.
NMPDR	fig|10090.3.peg.11568.
UCSC	uc008xix.1. mouse.
Organism-specific databases
CTD	110391.
MGI	MGI:97836. Qdpr.
Phylogenomic databases
HOGENOM	Q8BVI4.
HOVERGEN	Q8BVI4.
OMA	ICVAGGW.
Enzyme and pathway databases
BRENDA	1.5.1.34. 244.
Gene expression databases
ArrayExpress	Q8BVI4.
Bgee	Q8BVI4.
CleanEx	MM_QDPR.
Genevestigator	Q8BVI4.
GermOnline	ENSMUSG00000015806. Mus musculus.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	363915.
SOURCE	Search...

Entry information

Entry name

DHPR_MOUSE

Accession

Primary (citable) accession number: Q8BVI4
Secondary accession number(s): Q3TT09, Q9D0K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)