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Dihydrofolate reductase (EC 1.5.1.3)

 DYR_MOUSE               Reviewed;         187 AA.
P00375; P70693; Q61485; Q61487; Q61579;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-APR-2018, entry version 167.
RecName: Full=Dihydrofolate reductase;
EC=1.5.1.3 {ECO:0000269|PubMed:19748785, ECO:0000269|PubMed:25980602};
Name=Dhfr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6282858;
Crouse G.F., Simonsen C.C., McEwan R.N., Schimke R.T.;
"Structure of amplified normal and variant dihydrofolate reductase
genes in mouse sarcoma S180 cells.";
J. Biol. Chem. 257:7887-7897(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6573667; DOI=10.1073/pnas.80.9.2495;
Simonsen C.C., Levinson A.D.;
"Isolation and expression of an altered mouse dihydrofolate reductase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:2495-2499(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2263462; DOI=10.1093/nar/18.23.7025;
McIvor R.S., Simonsen C.C.;
"Isolation and characterization of a variant dihydrofolate reductase
cDNA from methotrexate-resistant murine L5178Y cells.";
Nucleic Acids Res. 18:7025-7032(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
PROTEIN SEQUENCE OF 2-187.
TISSUE=Lymphoma;
PubMed=762074;
Stone D., Paterson S.J., Raper J.H., Phillips A.W.;
"The amino acid sequence of dihydrofolate reductase from the mouse
lymphoma L1210.";
J. Biol. Chem. 254:480-488(1979).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
PubMed=2982814;
McGrogan M., Simonsen C.C., Smouse D.T., Farnham P.J., Schimke R.T.;
"Heterogeneity at the 5' termini of mouse dihydrofolate reductase
mRNAs. Evidence for multiple promoter regions.";
J. Biol. Chem. 260:2307-2314(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-24; 50-127 AND 154-187.
PubMed=6244105; DOI=10.1016/0092-8674(80)90510-3;
Nunberg J.H., Kaufman R.J., Chang A.C.Y., Cohen S.N., Schimke R.T.;
"Structure and genomic organization of the mouse dihydrofolate
reductase gene.";
Cell 19:355-364(1980).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-24 AND 50-127.
PubMed=360074; DOI=10.1038/275617a0;
Chang A.C.Y., Nunberg J.H., Kaufman R.J., Erlich H.A., Schimke R.T.,
Cohen S.N.;
"Phenotypic expression in E. coli of a DNA sequence coding for mouse
dihydrofolate reductase.";
Nature 275:617-624(1978).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-187.
PubMed=6121807;
Setzer D.R., McGrogan M., Schimke R.T.;
"Nucleotide sequence surrounding multiple polyadenylation sites in the
mouse dihydrofolate reductase gene.";
J. Biol. Chem. 257:5143-5147(1982).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=25980602; DOI=10.1016/j.febslet.2015.05.017;
Hughes L., Carton R., Minguzzi S., McEntee G., Deinum E.E.,
O'Connell M.J., Parle-McDermott A.;
"An active second dihydrofolate reductase enzyme is not a feature of
rat and mouse, but they do have activity in their mitochondria.";
FEBS Lett. 589:1855-1862(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-187 IN COMPLEX WITH NADP
AND METHOTREXATE, AND CHARACTERIZATION OF METHOTREXATE-RESISTANT
VARIANT ARG-23.
PubMed=15681865; DOI=10.1107/S0907444904030422;
Cody V., Luft J.R., Pangborn W.;
"Understanding the role of Leu22 variants in methotrexate resistance:
comparison of wild-type and Leu22Arg variant mouse and human
dihydrofolate reductase ternary crystal complexes with methotrexate
and NADPH.";
Acta Crystallogr. D 61:147-155(2005).
[14]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-187 IN COMPLEX WITH NADP
AND SYNTHETIC INHIBITOR.
PubMed=17019704; DOI=10.1002/prot.21131;
Cody V., Pace J., Chisum K., Rosowsky A.;
"New insights into DHFR interactions: analysis of Pneumocystis carinii
and mouse DHFR complexes with NADPH and two highly potent 5-(omega-
carboxy(alkyloxy) trimethoprim derivatives reveals conformational
correlations with activity and novel parallel ring stacking
interactions.";
Proteins 65:959-969(2006).
[15]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEXES WITH NADP AND
SYNTHETIC INHIBITOR.
PubMed=18703847; DOI=10.1107/S0907444908022348;
Cody V., Pace J., Rosowsky A.;
"Structural analysis of a holoenzyme complex of mouse dihydrofolate
reductase with NADPH and a ternary complex with the potent and
selective inhibitor 2,4-diamino-6-(2'-hydroxydibenz[b,f]azepin-5-
yl)methylpteridine.";
Acta Crystallogr. D 64:977-984(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-187 IN COMPLEXES WITH NADP
AND SYNTHETIC INHIBITOR, AND CATALYTIC ACTIVITY.
PubMed=19748785; DOI=10.1016/j.bmc.2009.08.044;
Gangjee A., Li W., Lin L., Zeng Y., Ihnat M., Warnke L.A., Green D.W.,
Cody V., Pace J., Queener S.F.;
"Design, synthesis, and X-ray crystal structures of 2,4-
diaminofuro[2,3-d]pyrimidines as multireceptor tyrosine kinase and
dihydrofolate reductase inhibitors.";
Bioorg. Med. Chem. 17:7324-7336(2009).
-!- FUNCTION: Key enzyme in folate metabolism. Contributes to the de
novo mitochondrial thymidylate biosynthesis pathway
(PubMed:25980602). Catalyzes an essential reaction for de novo
glycine and purine synthesis, and for DNA precursor synthesis
(PubMed:25980602). Binds its own mRNA.
{ECO:0000250|UniProtKB:P00374, ECO:0000269|PubMed:25980602}.
-!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-
dihydrofolate + NADPH. {ECO:0000255|PROSITE-ProRule:PRU00660,
ECO:0000269|PubMed:19748785, ECO:0000269|PubMed:25980602}.
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00374}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25980602}.
Cytoplasm {ECO:0000269|PubMed:25980602}.
-!- SIMILARITY: Belongs to the dihydrofolate reductase family.
{ECO:0000305}.
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EMBL; V00734; CAA24112.1; -; mRNA.
EMBL; X56066; CAA39544.1; -; mRNA.
EMBL; BC005796; AAH05796.1; -; mRNA.
EMBL; M10071; AAA37637.1; -; Genomic_DNA.
EMBL; L26316; AAA37523.1; -; mRNA.
EMBL; J00387; AAA37638.1; -; Genomic_DNA.
EMBL; J00382; AAA37638.1; JOINED; Genomic_DNA.
EMBL; J00383; AAA37638.1; JOINED; Genomic_DNA.
EMBL; J00384; AAA37638.1; JOINED; Genomic_DNA.
EMBL; J00385; AAA37638.1; JOINED; Genomic_DNA.
EMBL; J00386; AAA37638.1; JOINED; Genomic_DNA.
EMBL; V00731; CAB43539.2; -; mRNA.
EMBL; M10722; AAA37524.1; -; mRNA.
EMBL; M10811; AAA37525.1; -; mRNA.
EMBL; V00733; CAA24111.1; -; Genomic_DNA.
CCDS; CCDS26680.1; -.
PIR; S13096; RDMSD.
RefSeq; NP_034179.1; NM_010049.3.
UniGene; Mm.23695; -.
PDB; 1U70; X-ray; 2.50 A; A=2-187.
PDB; 2FZJ; X-ray; 2.00 A; A=2-187.
PDB; 3D80; X-ray; 1.40 A; A=2-187.
PDB; 3D84; X-ray; 1.90 A; X=2-187.
PDB; 3K45; X-ray; 1.60 A; A=2-187.
PDB; 3K47; X-ray; 2.05 A; A=2-187.
PDBsum; 1U70; -.
PDBsum; 2FZJ; -.
PDBsum; 3D80; -.
PDBsum; 3D84; -.
PDBsum; 3K45; -.
PDBsum; 3K47; -.
ProteinModelPortal; P00375; -.
SMR; P00375; -.
IntAct; P00375; 2.
MINT; P00375; -.
STRING; 10090.ENSMUSP00000022218; -.
BindingDB; P00375; -.
ChEMBL; CHEMBL4564; -.
iPTMnet; P00375; -.
PhosphoSitePlus; P00375; -.
EPD; P00375; -.
PaxDb; P00375; -.
PeptideAtlas; P00375; -.
PRIDE; P00375; -.
Ensembl; ENSMUST00000022218; ENSMUSP00000022218; ENSMUSG00000021707.
GeneID; 13361; -.
KEGG; mmu:13361; -.
UCSC; uc007rkl.1; mouse.
CTD; 1719; -.
MGI; MGI:94890; Dhfr.
eggNOG; KOG1324; Eukaryota.
eggNOG; COG0262; LUCA.
GeneTree; ENSGT00390000010283; -.
HOGENOM; HOG000040235; -.
HOVERGEN; HBG000773; -.
InParanoid; P00375; -.
KO; K00287; -.
OMA; RDNQLPW; -.
OrthoDB; EOG091G0PRK; -.
PhylomeDB; P00375; -.
TreeFam; TF317636; -.
BRENDA; 1.5.1.3; 3474.
Reactome; R-MMU-196757; Metabolism of folate and pterines.
SABIO-RK; P00375; -.
UniPathway; UPA00077; UER00158.
ChiTaRS; Dhfr; mouse.
EvolutionaryTrace; P00375; -.
PRO; PR:P00375; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021707; -.
CleanEx; MM_DHFR; -.
ExpressionAtlas; P00375; baseline and differential.
Genevisible; P00375; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0004146; F:dihydrofolate reductase activity; IDA:UniProtKB.
GO; GO:0051871; F:dihydrofolic acid binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0005542; F:folic acid binding; ISO:MGI.
GO; GO:0051870; F:methotrexate binding; ISO:MGI.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0070402; F:NADPH binding; ISO:MGI.
GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
GO; GO:0000900; F:translation repressor activity, mRNA regulatory element binding; ISO:MGI.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0046452; P:dihydrofolate metabolic process; ISO:MGI.
GO; GO:0046655; P:folic acid metabolic process; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:BHF-UCL.
GO; GO:2000121; P:regulation of removal of superoxide radicals; IMP:BHF-UCL.
GO; GO:0031427; P:response to methotrexate; IEA:UniProtKB-KW.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IMP:BHF-UCL.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; ISO:MGI.
GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
CDD; cd00209; DHFR; 1.
Gene3D; 3.40.430.10; -; 1.
InterPro; IPR024072; DHFR-like_dom_sf.
InterPro; IPR017925; DHFR_CS.
InterPro; IPR001796; DHFR_dom.
Pfam; PF00186; DHFR_1; 1.
SUPFAM; SSF53597; SSF53597; 1.
PROSITE; PS00075; DHFR_1; 1.
PROSITE; PS51330; DHFR_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Methotrexate resistance; Mitochondrion;
NADP; One-carbon metabolism; Oxidoreductase; Reference proteome;
RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:762074}.
CHAIN 2 187 Dihydrofolate reductase.
/FTId=PRO_0000186364.
DOMAIN 4 185 DHFR. {ECO:0000255|PROSITE-
ProRule:PRU00660}.
NP_BIND 16 22 NADP. {ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:17019704}.
NP_BIND 55 57 NADP. {ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:17019704}.
NP_BIND 77 79 NADP. {ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:17019704}.
NP_BIND 117 124 NADP. {ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:17019704}.
REGION 31 36 Substrate binding.
{ECO:0000305|PubMed:15681865}.
BINDING 10 10 NADP; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:15681865,
ECO:0000269|PubMed:17019704}.
BINDING 65 65 Substrate. {ECO:0000305|PubMed:15681865}.
BINDING 71 71 Substrate. {ECO:0000305|PubMed:15681865}.
MOD_RES 33 33 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 33 33 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
VARIANT 23 23 L -> R (in a form with an abnormally low
affinity for methotrexate).
{ECO:0000269|PubMed:15681865}.
VARIANT 32 32 F -> W (in L-5178-Y cell line;
methotrexate-resistant, requires 2
nucleotide substitutions).
CONFLICT 4 4 P -> A (in Ref. 6; AAA37637).
{ECO:0000305}.
CONFLICT 14 14 N -> D (in Ref. 3; CAA39544).
{ECO:0000305}.
CONFLICT 123 123 Q -> E (in Ref. 5; AA sequence and 8;
AAA37525). {ECO:0000305}.
CONFLICT 124 124 E -> Q (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 128 128 Q -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 174 174 K -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
STRAND 4 11 {ECO:0000244|PDB:3D80}.
STRAND 15 19 {ECO:0000244|PDB:3D80}.
STRAND 24 26 {ECO:0000244|PDB:3D80}.
HELIX 29 40 {ECO:0000244|PDB:3D80}.
STRAND 43 46 {ECO:0000244|PDB:1U70}.
STRAND 50 54 {ECO:0000244|PDB:3D80}.
HELIX 55 60 {ECO:0000244|PDB:3D80}.
HELIX 63 65 {ECO:0000244|PDB:3D80}.
STRAND 71 76 {ECO:0000244|PDB:3D80}.
STRAND 88 93 {ECO:0000244|PDB:3D80}.
HELIX 94 101 {ECO:0000244|PDB:3D80}.
HELIX 104 109 {ECO:0000244|PDB:3D80}.
STRAND 113 115 {ECO:0000244|PDB:3D80}.
HELIX 119 126 {ECO:0000244|PDB:3D80}.
STRAND 128 130 {ECO:0000244|PDB:3D80}.
STRAND 132 139 {ECO:0000244|PDB:3D80}.
STRAND 146 148 {ECO:0000244|PDB:3D80}.
TURN 154 156 {ECO:0000244|PDB:3D80}.
STRAND 157 159 {ECO:0000244|PDB:2FZJ}.
STRAND 171 173 {ECO:0000244|PDB:3D80}.
STRAND 176 185 {ECO:0000244|PDB:3D80}.
SEQUENCE 187 AA; 21606 MW; 47AEF15F879B119C CRC64;
MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS
IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS
VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF
EVYEKKD


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