GenomeNet

Database: UniProt
Entry: Q8CHR6
LinkDB: Q8CHR6
Original site: Q8CHR6 
ID   DPYD_MOUSE              Reviewed;        1025 AA.
AC   Q8CHR6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JAN-2019, entry version 131.
DE   RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)];
DE            Short=DHPDHase;
DE            Short=DPD;
DE            EC=1.3.1.2;
DE   AltName: Full=Dihydrothymine dehydrogenase;
DE   AltName: Full=Dihydrouracil dehydrogenase;
GN   Name=Dpyd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, and Liver;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the
CC       reduction of uracil and thymine (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil;
CC         Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.3.1.2;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron
CC       atoms per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inactivated by 5-iodouracil. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; BC039699; AAH39699.1; -; mRNA.
DR   CCDS; CCDS17797.1; -.
DR   RefSeq; NP_740748.1; NM_170778.2.
DR   UniGene; Mm.27907; -.
DR   ProteinModelPortal; Q8CHR6; -.
DR   SMR; Q8CHR6; -.
DR   IntAct; Q8CHR6; 2.
DR   MINT; Q8CHR6; -.
DR   STRING; 10090.ENSMUSP00000039429; -.
DR   iPTMnet; Q8CHR6; -.
DR   PhosphoSitePlus; Q8CHR6; -.
DR   SwissPalm; Q8CHR6; -.
DR   jPOST; Q8CHR6; -.
DR   MaxQB; Q8CHR6; -.
DR   PaxDb; Q8CHR6; -.
DR   PeptideAtlas; Q8CHR6; -.
DR   PRIDE; Q8CHR6; -.
DR   Ensembl; ENSMUST00000039177; ENSMUSP00000039429; ENSMUSG00000033308.
DR   GeneID; 99586; -.
DR   KEGG; mmu:99586; -.
DR   UCSC; uc008rdh.1; mouse.
DR   CTD; 1806; -.
DR   MGI; MGI:2139667; Dpyd.
DR   eggNOG; KOG0399; Eukaryota.
DR   eggNOG; COG0167; LUCA.
DR   eggNOG; COG0493; LUCA.
DR   eggNOG; COG1146; LUCA.
DR   GeneTree; ENSGT00500000044896; -.
DR   HOGENOM; HOG000007797; -.
DR   HOVERGEN; HBG004351; -.
DR   InParanoid; Q8CHR6; -.
DR   KO; K00207; -.
DR   OMA; HWKRNAD; -.
DR   OrthoDB; 592753at2759; -.
DR   PhylomeDB; Q8CHR6; -.
DR   TreeFam; TF105791; -.
DR   Reactome; R-MMU-73621; Pyrimidine catabolism.
DR   UniPathway; UPA00131; -.
DR   PRO; PR:Q8CHR6; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000033308; Expressed in 250 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q8CHR6; baseline and differential.
DR   Genevisible; Q8CHR6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IDA:MGI.
DR   GO; GO:0004159; F:dihydrouracil dehydrogenase (NAD+) activity; ISO:MGI.
DR   GO; GO:0071949; F:FAD binding; ISO:MGI.
DR   GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0002058; F:uracil binding; ISO:MGI.
DR   GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007623; P:circadian rhythm; ISO:MGI.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; ISO:MGI.
DR   GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IDA:MGI.
DR   GO; GO:0042493; P:response to drug; ISO:MGI.
DR   GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0006214; P:thymidine catabolic process; ISS:UniProtKB.
DR   GO; GO:0006210; P:thymine catabolic process; ISO:MGI.
DR   GO; GO:0006212; P:uracil catabolic process; ISS:UniProtKB.
DR   GO; GO:0019860; P:uracil metabolic process; ISO:MGI.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF01180; DHO_dh; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acetylation; Complete proteome; Cytoplasm; FAD; Flavoprotein;
KW   FMN; Iron; Iron-sulfur; Metal-binding; NADP; Nucleotide-binding;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN         1   1025       Dihydropyrimidine dehydrogenase
FT                                [NADP(+)].
FT                                /FTId=PRO_0000327501.
FT   DOMAIN       69    100       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      944    976       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      978   1007       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     194    198       FAD. {ECO:0000250}.
FT   NP_BIND     218    226       FAD. {ECO:0000250}.
FT   NP_BIND     340    343       NADP. {ECO:0000250}.
FT   NP_BIND     364    365       NADP. {ECO:0000250}.
FT   NP_BIND     437    439       NADP. {ECO:0000250}.
FT   NP_BIND     480    489       FAD. {ECO:0000250}.
FT   NP_BIND     481    487       NADP. {ECO:0000250}.
FT   NP_BIND     574    575       FMN. {ECO:0000250}.
FT   NP_BIND     793    795       FMN. {ECO:0000250}.
FT   NP_BIND     816    817       FMN. {ECO:0000250}.
FT   REGION      668    670       Substrate binding. {ECO:0000250}.
FT   REGION      736    737       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    671    671       Proton acceptor. {ECO:0000250}.
FT   METAL        79     79       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        82     82       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        87     87       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        91     91       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       130    130       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       136    136       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       140    140       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       156    156       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       953    953       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       956    956       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       959    959       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       963    963       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       986    986       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       989    989       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       992    992       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   METAL       996    996       Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
FT   BINDING     129    129       FAD; via carbonyl oxygen. {ECO:0000250}.
FT   BINDING     235    235       FAD. {ECO:0000250}.
FT   BINDING     261    261       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     371    371       NADP. {ECO:0000250}.
FT   BINDING     550    550       FMN. {ECO:0000250}.
FT   BINDING     609    609       Substrate. {ECO:0000250}.
FT   BINDING     709    709       FMN. {ECO:0000250}.
FT   BINDING     767    767       FMN; via amide nitrogen. {ECO:0000250}.
FT   MOD_RES     384    384       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q12882}.
FT   MOD_RES     905    905       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
SQ   SEQUENCE   1025 AA;  111253 MW;  AA1D1B3E3B72C504 CRC64;
     MAGVLSRDAP DIESILALNP RVQAHATLRS TAAKKLDKKH WKRNTDKNCF TCEKLESNFD
     DIKHTTLGER GALREAVRCL KCADAPCQKS CPTSLDIKSF ITSIANKNYY GAAKLIFSDN
     PLGLTCGMVC PTSDLCVGGC NLHAAEEGPI NIGGLQQFAT EVFKAMNIPQ IRNPSLPPPE
     HMPEAYSAKI ALFGAGPASI SCASFLARLG YSNITIFEKQ EYVGGLSTSE IPQFRLPYDV
     VNFEIELMKD LGVKIICGKS LSTDEMTLSS LKENGYRAAF IGIGLPEPKK DHIFQGLTQV
     QGFYTSKDFL PLVAKSSKTG MCACHSPLPS IRGAVIVLGA GDTAFDCATS ALRCGALRVF
     IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKD GKIVAMQFVR TEQDETGNWV
     EDEEQTVRLK ADVVISAFGS VLEDPKVKEA LSPIKFNRWG LPEVNPETMQ TSEPWVFAGG
     DVVGMANTTV ESVNDGKQAS WYIHKHIQAQ YGTSVPSQPT MPLFYTPVDL VDISVEMAGL
     RFPNPFGLAS ATPATSTPMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPLY
     GPGQSSFLNI ELISEKTAAY WCHSVTELKA DFPDNILIAS IMCSYNKSDW MELSKMAEAS
     GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVRVPFFAKL TPNVTDIVSI
     ARAAKEGGAD GVTATNTVSG LMGLKADGTP WPAVGIGRRT TYGGVSGTAI RPIALRAVTA
     IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL
     KSIEELADWD GQSPPIISHQ KGKPVPRVAE LMGQKLPSFG PYLEQRKKII AASKIRQKDQ
     NTACSPLQRK HFNSQKPIPA IKDVIGKSLQ YLGTFGEMSI MEQVVALIDE EMCINCGKCY
     MTCNDSGYQA IQFDPETHLP TVSDTCTGCT LCLSVCPIMD CIRMVSRATP YQPKRGLPLA
     VKPVC
//
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