NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
DOI=10.1128/AAC.45.9.2517-2523.2001; PubMed=11502523 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Bruenn J.A., Queener S.F., Cody V.;
"Isolation of rat dihydrofolate reductase gene and characterization of recombinant enzyme.";
Antimicrob. Agents Chemother. 45:2517-2523(2001).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
MISCELLANEOUS: The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
SIMILARITY: Belongs to the dihydrofolate reductase family.
SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.

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

AF318150; AAL11500.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_569084.1; -.

UniGene

Rn.24681

3D structure databases

HSSP

P00374; 1KMS. [HSSP ENTRY / PDB]

SMR

Q920D2; 1-186, 2-187.

ModBase

Q920D2.

Organism-specific databases

RGD

2500; Dhfr.

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

Q920D2.

Genome annotation databases

Ensembl

ENSRNOG00000013521; Rattus norvegicus. [Contig view]

GeneID

24312; -.

KEGG

rno:24312; -.

NMPDR

fig|10116.3.peg.15341; -.

Phylogenomic databases

HOVERGEN

Q920D2; -.

Other

Q920D2; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 187`	`186`	`Dihydrofolate reductase.`	`PRO_0000186366`
`DOMAIN`	`4 185`	`182`	`DHFR.`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 21638 Da [This is the MW of the unprocessed precursor]

CRC64: FE1DB4F3515F8B26 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVRPLNCIVA VSQNMGIGKN GDLPWPLLRN EFKYFQRMTT TSSVEGKQNL VIMGRKTWFS 

        70         80         90        100        110        120 
IPEKNRPLKD RINIVLSREL KEPPQGAHFL AKSLDDALKL IEQPELASKV DMVWVVGGSS 

       130        140        150        160        170        180 
VYQEAMNQPG HLRLFVTRIM QEFESDTFFP EIDLEKYKLL PEYPGVLSEI QEEKGIKYKF 


EVYEKKD

Q920D2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools