DHPR_MOUSE
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 03-AUG-2022, entry version 144.
DE RecName: Full=Dihydropteridine reductase;
DE EC=1.5.1.34 {ECO:0000250|UniProtKB:P09417};
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-93 AND LYS-99,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the conversion of quinonoid dihydrobiopterin into
CC tetrahydrobiopterin. {ECO:0000250|UniProtKB:P09417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine +
CC H(+) + NADH; Xref=Rhea:RHEA:17869, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.5.1.34;
CC Evidence={ECO:0000250|UniProtKB:P09417};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17871;
CC Evidence={ECO:0000250|UniProtKB:P09417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydropteridine + NADP(+) = 6,7-dihydropteridine +
CC H(+) + NADPH; Xref=Rhea:RHEA:17865, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.34;
CC Evidence={ECO:0000250|UniProtKB:P09417};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17867;
CC Evidence={ECO:0000250|UniProtKB:P09417};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11348}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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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 CCDS; CCDS19272.1; -.
DR RefSeq; NP_077198.1; NM_024236.2.
DR AlphaFoldDB; Q8BVI4; -.
DR SMR; Q8BVI4; -.
DR BioGRID; 225559; 7.
DR STRING; 10090.ENSMUSP00000015950; -.
DR iPTMnet; Q8BVI4; -.
DR PhosphoSitePlus; Q8BVI4; -.
DR SwissPalm; Q8BVI4; -.
DR REPRODUCTION-2DPAGE; Q8BVI4; -.
DR EPD; Q8BVI4; -.
DR jPOST; Q8BVI4; -.
DR MaxQB; Q8BVI4; -.
DR PaxDb; Q8BVI4; -.
DR PeptideAtlas; Q8BVI4; -.
DR PRIDE; Q8BVI4; -.
DR ProteomicsDB; 279647; -.
DR Antibodypedia; 23074; 223 antibodies from 29 providers.
DR DNASU; 110391; -.
DR Ensembl; ENSMUST00000015950; ENSMUSP00000015950; ENSMUSG00000015806.
DR GeneID; 110391; -.
DR KEGG; mmu:110391; -.
DR UCSC; uc008xix.2; mouse.
DR CTD; 5860; -.
DR MGI; MGI:97836; Qdpr.
DR VEuPathDB; HostDB:ENSMUSG00000015806; -.
DR eggNOG; KOG4022; Eukaryota.
DR GeneTree; ENSGT00390000000470; -.
DR InParanoid; Q8BVI4; -.
DR OMA; DWWVASI; -.
DR OrthoDB; 1585354at2759; -.
DR PhylomeDB; Q8BVI4; -.
DR TreeFam; TF105932; -.
DR Reactome; R-MMU-8964208; Phenylalanine metabolism.
DR BioGRID-ORCS; 110391; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q8BVI4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BVI4; protein.
DR Bgee; ENSMUSG00000015806; Expressed in substantia nigra and 259 other tissues.
DR ExpressionAtlas; Q8BVI4; baseline and differential.
DR Genevisible; Q8BVI4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0004155; F:6,7-dihydropteridine reductase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070404; F:NADH binding; ISO:MGI.
DR GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase; Reference proteome;
KW Tetrahydrobiopterin biosynthesis.
FT CHAIN 1..241
FT /note="Dihydropteridine reductase"
FT /id="PRO_0000054637"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 76
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 99
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 167
FT /note="G -> D (in Ref. 1; BAC37135)"
FT /evidence="ECO:0000305"
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
