P00377 (DYR_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrofolate reductase
EC=1.5.1.3

Gene names

Name:

DHFR

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	186 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1 By similarity.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	Methotrexate resistance One-carbon metabolism
Ligand	NADP RNA-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to methotrexate Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from sequence or structural similarity. Source: UniProtKB drug binding Inferred from sequence or structural similarity. Source: UniProtKB mRNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 186	186	Dihydrofolate reductase		PRO_0000186365
Regions
	Domain	3 – 184	182	DHFR
	Nucleotide binding	15 – 21	7	NADP By similarity
	Nucleotide binding	54 – 56	3	NADP By similarity
	Nucleotide binding	76 – 78	3	NADP By similarity
	Nucleotide binding	116 – 123	8	NADP By similarity
	Region	30 – 35	6	Substrate binding By similarity
Sites
	Binding site	9	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	70	1	Substrate By similarity
Amino acid modifications
	Modified residue	162	1	Cysteine derivative; partial

Sequences

	Sequence		Length	Mass (Da)
	P00377 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D05DB526FE5C12CE	FASTA	186	21,455
	10 20 30 40 50 60 VRPLNCIVAV SQNMGIGKNG DLPWPPLRNE YKYFQRMTTT SSVEGKQNLV IMGRKTWFSI 70 80 90 100 110 120 PEKNRPLKDR INIVLSRELK EPPQGAHFLA KSLDDALKLT EQPELKDKVD MVWIVGGSSV 130 140 150 160 170 180 YKEAMNKPGH IRLFVTRIMK EFESDTFFPE IDLEKYKLLS ECSGVPSDVQ EEKGIKYKFE VYEKNN

References

[1]	"Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence." Smith S.L., Patrick P., Stone D., Phillips A.W., Burchall J.J. J. Biol. Chem. 254:11475-11484(1979) [PubMed: 500653] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	RDPGD. A00389.
3D structure databases
ProteinModelPortal	P00377.
SMR	P00377. Positions 1-186.
ModBase	Search...
Protein-protein interaction databases
STRING	P00377.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
GeneTree	ENSGT00390000010283.
HOVERGEN	HBG000773.
OrthoDB	EOG4QJRPF.
Family and domain databases
InterPro	IPR012259. DHFR. IPR024072. DHFR-like_dom. IPR017925. DHFR_CS. IPR001796. DHFR_dom. [Graphical view]
Gene3D	G3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
SUPFAM	SSF53597. SSF53597. 1 hit.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_PIG

Accession

Primary (citable) accession number: P00377

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program