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P00376

- DYR_BOVIN

UniProt

P00376 - DYR_BOVIN

Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei71 – 711SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 227NADPBy similarity
    Nucleotide bindingi55 – 573NADPBy similarity
    Nucleotide bindingi77 – 793NADPBy similarity
    Nucleotide bindingi117 – 1248NADPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB
    2. drug binding Source: UniProtKB
    3. mRNA binding Source: UniProtKB
    4. NADP binding Source: InterPro

    GO - Biological processi

    1. glycine biosynthetic process Source: InterPro
    2. nucleotide biosynthetic process Source: InterPro
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. response to methotrexate Source: UniProtKB-KW
    5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
    6. tetrahydrofolate metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Methotrexate resistance, One-carbon metabolism

    Keywords - Ligandi

    NADP, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_201998. E2F mediated regulation of DNA replication.
    REACT_217517. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_222884. Metabolism of folate and pterines.
    REACT_225533. G1/S-Specific Transcription.
    SABIO-RKP00376.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:DHFR
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 7

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 187186Dihydrofolate reductasePRO_0000186361Add
    BLAST

    Proteomic databases

    PaxDbiP00376.
    PRIDEiP00376.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000010103.

    Structurei

    3D structure databases

    ProteinModelPortaliP00376.
    SMRiP00376. Positions 2-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 185182DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 366Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the dihydrofolate reductase family.Curated
    Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0262.
    GeneTreeiENSGT00390000010283.
    HOGENOMiHOG000040235.
    HOVERGENiHBG000773.
    InParanoidiP00376.
    KOiK00287.
    OrthoDBiEOG7V1FS3.
    TreeFamiTF317636.

    Family and domain databases

    Gene3Di3.40.430.10. 1 hit.
    InterProiIPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view]
    PfamiPF00186. DHFR_1. 1 hit.
    [Graphical view]
    PRINTSiPR00070. DHFR.
    SUPFAMiSSF53597. SSF53597. 1 hit.
    PROSITEiPS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00376-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFQYFQRMTT VSSVEGKQNL    50
    VIMGRKTWFS IPEKNRPLKD RINIVLSREL KEPPKGAHFL AKSLDDALEL 100
    IEDPELTNKV DVVWIVGGSS VYKEAMNKPG HVRLFVTRIM QEFESDAFFP 150
    EIDFEKYKLL PEYPGVPLDV QEEKGIKYKF EVYEKNN 187
    Length:187
    Mass (Da):21,604
    Last modified:January 23, 2007 - v3
    Checksum:i0727DD855C8A7CD8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221D → N in AAI14163. 1 PublicationCurated
    Sequence conflicti102 – 1021E → Q AA sequence (PubMed:7115669)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC114162 mRNA. Translation: AAI14163.1.
    PIRiA00388. RDBOD.
    RefSeqiNP_001071351.1. NM_001077883.1.
    UniGeneiBt.18730.

    Genome annotation databases

    EnsembliENSBTAT00000010103; ENSBTAP00000010103; ENSBTAG00000007681.
    GeneIDi508809.
    KEGGibta:508809.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC114162 mRNA. Translation: AAI14163.1 .
    PIRi A00388. RDBOD.
    RefSeqi NP_001071351.1. NM_001077883.1.
    UniGenei Bt.18730.

    3D structure databases

    ProteinModelPortali P00376.
    SMRi P00376. Positions 2-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000010103.

    Chemistry

    BindingDBi P00376.
    ChEMBLi CHEMBL1075051.

    Proteomic databases

    PaxDbi P00376.
    PRIDEi P00376.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000010103 ; ENSBTAP00000010103 ; ENSBTAG00000007681 .
    GeneIDi 508809.
    KEGGi bta:508809.

    Organism-specific databases

    CTDi 1719.

    Phylogenomic databases

    eggNOGi COG0262.
    GeneTreei ENSGT00390000010283.
    HOGENOMi HOG000040235.
    HOVERGENi HBG000773.
    InParanoidi P00376.
    KOi K00287.
    OrthoDBi EOG7V1FS3.
    TreeFami TF317636.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    Reactomei REACT_201998. E2F mediated regulation of DNA replication.
    REACT_217517. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_222884. Metabolism of folate and pterines.
    REACT_225533. G1/S-Specific Transcription.
    SABIO-RK P00376.

    Miscellaneous databases

    NextBioi 20868689.

    Family and domain databases

    Gene3Di 3.40.430.10. 1 hit.
    InterProi IPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view ]
    Pfami PF00186. DHFR_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00070. DHFR.
    SUPFAMi SSF53597. SSF53597. 1 hit.
    PROSITEi PS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Heart ventricle.
    2. "Structure of dihydrofolate reductase: primary sequence of the bovine liver enzyme."
      Lai P.-H., Pan Y.-C.E., Gleisner J.M., Peterson D.L., Williams K.R., Blakley R.L.
      Biochemistry 21:3284-3294(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-187.
      Tissue: Liver.

    Entry informationi

    Entry nameiDYR_BOVIN
    AccessioniPrimary (citable) accession number: P00376
    Secondary accession number(s): Q29RI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3