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UniProtKB/Swiss-Prot entry P00375


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DYR_MOUSE
Primary accession number P00375
Secondary accession numbers P70693 Q61485 Q61487 Q61579
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: Dhfr
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6282858 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1093/nar/18.23.7025; PubMed=2263462 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0092-8674(80)90510-3; PubMed=6244105 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1038/275617a0; PubMed=360074 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V00734; CAA24112.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56066; CAA39544.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005796; AAH05796.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10071; AAA37637.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L26316; AAA37523.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00387; AAA37638.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00382; AAA37638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00383; AAA37638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00384; AAA37638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00385; AAA37638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00386; AAA37638.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00731; CAB43539.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10722; AAA37524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10811; AAA37525.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00733; CAA24111.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S13096; RDMSD.
RefSeq NP_034179.1; -.
UniGene Mm.23695
3D structure databases
PDB
1U70; X-ray; 2.50 A; A=1-187.[ExPASy / RCSB / EBI]
2FZJ; X-ray; 2.00 A; A=2-187.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1U70; -.
2FZJ; -.
ModBase P00375.
Organism-specific databases
MGI MGI:94890; Dhfr.
Gene expression databases
ArrayExpress P00375; -.
CleanEx MM_DHFR; -.
GermOnline ENSMUSG00000021707; Mus musculus.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR001796; DHFR_reg.
Graphical view of domain structure.
Pfam PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00375.
ProtoNet P00375.
Genome annotation databases
Ensembl ENSMUSG00000021707; Mus musculus. [Contig view]
GeneID 13361; -.
KEGG mmu:13361; -.
Phylogenomic databases
HOGENOM P00375; -.
HOVERGEN P00375; -.
Other
NextBio 283696; -.
SOURCE Dhfr; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   187  186     Dihydrofolate reductase. PRO_0000186364
DOMAIN   4   185  182     DHFR. 
VARIANT   23    23  1     L -> R (in a form with an abnormally low affinity for methotrexate). 
VARIANT   32    32  1     F -> W (in L5178Y cell line; methotrexate-resistant). 
CONFLICT   4     4        P -> A (in Ref. 6). 
CONFLICT   14    14        N -> D (in Ref. 3; CAA39544). 
CONFLICT   123   123        Q -> E (in Ref. 5, 7 and 8). 
CONFLICT   124   124        E -> Q (in Ref. 5; AA sequence). 
CONFLICT   128   128        Q -> E (in Ref. 5; AA sequence). 
CONFLICT   174   174        K -> D (in Ref. 5; AA sequence). 
STRAND   4    12  9      
HELIX   29    40  12      
STRAND   48    54  7      
HELIX   55    60  6      
HELIX   63    65  3      
STRAND   71    76  6      
STRAND   88    93  6      
HELIX   94   101  8      
HELIX   104   107  4      
STRAND   110   117  8      
HELIX   119   126  8      
STRAND   127   130  4      
STRAND   132   139  8      
STRAND   146   148  3      
TURN   154   156  3      
STRAND   157   159  3      
STRAND   171   173  3      
STRAND   176   185  10      
Sequence information
Length: 187 AA [This is the length of the unprocessed precursor] Molecular weight: 21606 Da [This is the MW of the unprocessed precursor] CRC64: 47AEF15F879B119C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS 

        70         80         90        100        110        120 
IPEKNRPLKD RINIVLSREL KEPPRGAHFL AKSLDDALRL IEQPELASKV DMVWIVGGSS 

       130        140        150        160        170        180 
VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLGKYKLL PEYPGVLSEV QEEKGIKYKF 


EVYEKKD 

P00375 in FASTA format

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