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UniProtKB/Swiss-Prot entry P17719


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

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Entry information
Entry name DYR_DROME
Primary accession number P17719
Secondary accession number Q9VEU4
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on June 1, 2001 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: Dhfr
ORFNames: CG14887
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 155-176.
STRAIN=Canton-S;
PubMed=8195153 [NCBI, ExPASy, EBI, Israel, Japan]
Hao H., Tyshenko M.G., Walker V.K.;
"Dihydrofolate reductase of Drosophila. Cloning and expression of a gene with a rare transcript.";
J. Biol. Chem. 269:15179-15185(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
PROTEIN SEQUENCE OF 1-23.
STRAIN=Canton-S;
DOI=10.1016/0167-4838(90)90258-H; PubMed=2116172 [NCBI, ExPASy, EBI, Israel, Japan]
Rancourt S.L., Walker V.K.;
"The purification of dihydrofolate reductase from Drosophila melanogaster.";
Biochim. Biophys. Acta 1039:261-268(1990).
[5]
INTERACTION WITH VG, AND INVOLVEMENT IN DNA REPLICATION.
DOI=10.1038/sj.cdd.4401321; PubMed=14526388 [NCBI, ExPASy, EBI, Israel, Japan]
Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A., Vaudin P., Becker J.L., Silber J.;
"The Drosophila wing differentiation factor vestigial-scalloped is required for cell proliferation and cell survival at the dorso-ventral boundary of the wing imaginal disc.";
Cell Death Differ. 11:110-122(2004).
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
U06861; AAA19051.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF55324.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A53803; A53803.
S10759; A33105.
RefSeq NP_001036720.1; -.
NP_732147.1; -.
UniGene Dm.8025
3D structure databases
HSSP P00374; 1KMV. [HSSP ENTRY / PDB]
ModBase P17719.
Protein-protein interaction databases
DIP DIP:20310N; -.
IntAct P17719; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-011944-MON; -.
Organism-specific databases
FlyBase FBgn0004087; Dhfr.
Gene expression databases
GermOnline CG14887; Drosophila melanogaster.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from direct assay from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
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 P17719.
Genome annotation databases
Ensembl CG14887; Drosophila melanogaster. [Contig view]
GeneID 42003; -.
KEGG dme:Dmel_CG14887; -.
NMPDR fig|7227.3.peg.13160; -.
Phylogenomic databases
HOGENOM P17719; -.
Other
ProtoNet P17719.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; DNA replication; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   182  182     Dihydrofolate reductase. PRO_0000186370
DOMAIN   3   180  178     DHFR. 
CONFLICT   3     3        R -> T (in Ref. 4; AA sequence). 
CONFLICT   11    11        C -> S (in Ref. 4; AA sequence). 
CONFLICT   134   134        K -> Q (in Ref. 1; AAA19051). 
Sequence information
Length: 182 AA [This is the length of the unprocessed precursor] Molecular weight: 20775 Da [This is the MW of the unprocessed precursor] CRC64: D2C9198F1D2CE430 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLRFNLIVAV CENFGIGIRG DLPWRIKSEL KYFSRTTKRT SDPTKQNAVV MGRKTYFGVP 

        70         80         90        100        110        120 
ESKRPLPDRL NIVLSTTLQE SDLPKGVLLC PNLETAMKIL EEQNEVENIW IVGGSGVYEE 

       130        140        150        160        170        180 
AMASPRCHRL YITKIMQKFD CDTFFPAIPD SFREVAPDSD MPLGVQEENG IKFEYKILEK 


HS 

P17719 in FASTA format

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