ID   DHPR_MOUSE              Reviewed;         241 AA.
AC   Q8BVI4; Q3TT09; Q9D0K4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Dihydropteridine reductase;
DE            EC=1.5.1.34;
DE   AltName: Full=HDHPR;
DE   AltName: Full=Quinoid dihydropteridine reductase;
GN   Name=Qdpr; Synonyms=Dhpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 77-93; 125-135; 165-188 AND 218-233, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4),
CC       is an essential cofactor for phenylalanine, tyrosine, and
CC       tryptophan hydroxylases (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a
CC       6,7-dihydropteridine + NAD(P)H.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AK011351; BAB27559.1; -; mRNA.
DR   EMBL; AK078123; BAC37135.1; -; mRNA.
DR   EMBL; AK159107; BAE34823.1; -; mRNA.
DR   EMBL; AK161660; BAE36516.1; -; mRNA.
DR   EMBL; AK166694; BAE38951.1; -; mRNA.
DR   EMBL; BC002107; AAH02107.1; -; mRNA.
DR   IPI; IPI00459279; -.
DR   RefSeq; NP_077198.1; -.
DR   UniGene; Mm.30204; -.
DR   HSSP; P11348; 1DHR.
DR   SMR; Q8BVI4; 6-241.
DR   REPRODUCTION-2DPAGE; Q8BVI4; -.
DR   PRIDE; Q8BVI4; -.
DR   Ensembl; ENSMUSG00000015806; Mus musculus.
DR   GeneID; 110391; -.
DR   KEGG; mmu:110391; -.
DR   NMPDR; fig|10090.3.peg.11568; -.
DR   MGI; MGI:97836; Qdpr.
DR   HOGENOM; Q8BVI4; -.
DR   HOVERGEN; Q8BVI4; -.
DR   OMA; Q8BVI4; ICVAGGW.
DR   BRENDA; 1.5.1.34; 244.
DR   NextBio; 363915; -.
DR   ArrayExpress; Q8BVI4; -.
DR   Bgee; Q8BVI4; -.
DR   CleanEx; MM_QDPR; -.
DR   GermOnline; ENSMUSG00000015806; Mus musculus.
DR   GO; GO:0004155; F:6,7-dihydropteridine reductase activity; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; NADP; Oxidoreductase;
KW   Tetrahydrobiopterin biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    241       Dihydropteridine reductase.
FT                                /FTId=PRO_0000054637.
FT   NP_BIND      11     35       NADP (By similarity).
FT   ACT_SITE    147    147       Proton acceptor (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    167    167       G -> D (in Ref. 1; BAC37135).
SQ   SEQUENCE   241 AA;  25570 MW;  2ED25295D38C494B CRC64;
     MAASGEARRV LVYGGRGALG SRCVQAFRAR NWWVASIDVV ENEEASASVV VKMTDSFTEQ
     ADQVTADVGK LLGDQKVDAI LCVAGGWAGG NAKSKSLFKN CDMMWKQSMW TSTISSHLAT
     KHLKEGGLLT LAGAKAALDG TPGMIGYGMA KGAVHQLCQS LAGKNSGMPP GAAAIAVLPV
     TLDTPMNRKS MPEADFSSWT PLEFLVETFH DWITGNKRPN SGSLIQVVTT DGKTELTPAY
     F
//