PDR3/YBL005W Protein Information

Standard Name	Pdr3p
Systematic Name	Ybl005wp
Alias	Amy2p , Tpe2p
ORF Classification	Verified
Description	Transcriptional activator of the pleiotropic drug resistance network; regulates expression of ATP-binding cassette (ABC) transporters through binding to cis-acting sites known as PDREs (PDR responsive elements); post-translationally up-regulated in cells lacking a functional mitochondrial genome; PDR3 has a paralog, PDR1, that arose from the whole genome duplication; relative distribution to the nucleus increases upon DNA replication stress (1, 2, 3, 4, 5, 6, 7, 8)
Name Description	Pleiotropic Drug Resistance 9

Experimental Data
Molecules/cell	166 10

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	976
Molecular Weight (Da)	112,570
Isoelectric Point (pI)	6.55

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Pdr3p (InterPro)
Physical Interactions	There are 13 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00001314D8 \| P33200 MIPS: YBL005W NCBI: 506478 \| 51013699 \| 535984 \| 585651 \| 6319466 \| 7580487 \| NP_009548.1 GenBank/EMBL/DDBJ: DAA07115.1 \| AY693124 \| S47695 \| X79803 \| Z35766

Amino Acid Sequence (or in FASTA format)
1 MKVKKSTRSK VSTACVNCRK RKIKCTGKYP CTNCISYDCT CVFLKKHLPQ 51 KEDSSQSLPT TAVAPPSSHA NVEASADVQH LDTAIKLDNQ YYFKLMNDLI 101 QTPVSPSATH APDTSNNPTN DNNILFKDDS KYQNQLVTYQ NILTNLYALP 151 PCDDTQLLID KTKSQLNNLI NSWNPEINYP KLSSFSPRPQ RSIETYLLTN 201 KYRNKIHMTR FSFWTDQMVK SQSPDSFLAT TPLVDEVFGL FSPIQAFSLR 251 GIGYLIKKNI ENTGSSMLID TKETIYLILR LFDLCYEHLI QGCISISNPL 301 ENYLQKIKQT PTTTASASLP TSPAPLSNDL VISVIHQLPQ PFIQSITGFT 351 TTQLIENLHD SFSMFRIVTQ MYAQHRKRFA EFLNQAFSLP HQEKSVLFSS 401 FCSSEYLLST LCYAYYNVTL YHMLDINTLD YLEILVSLLE IQNEIDERFG 451 FEKMLEVAVT CSTKMGLSRW EYYVGIDENT AERRRKIWWK IYSLEKRFLT 501 DLGDLSLINE HQMNCLLPKD FRDMGFINHK EFLTKIGTSS LSPSSPKLKN 551 LSLSRLIEYG ELAIAQIVGD FFSETLYNEK FTSLEVSVKP TIIRQKLLEK 601 VFEDIESFRL KLAKIKLHTS RVFQVAHCKY PEYPKNDLIE AAKFVSYHKN 651 TWFSILGAVN NLIARLSEDP EVITEQSMKY ANEMFQEWRE INQFLIQVDT 701 DFIVWACLDF YELIFFVMAS KFYVEDPHIT LEDVINTLKV FKRITNIISF 751 FNNNLDEKDY DCQTFREFSR SSSLVAISIR IIFLKYCYAE QIDRAEFIER 801 LKEVEPGLSD LLREFFDTRS FIYRYMLKSV EKSGFHLIIR KMLESDYKFL 851 YRDKLATGNI PDQGNSSQIS QLYDSTAPSY NNASASAANS PLKLSSLLNS 901 GEESYTQDAS ENVPCNLRHQ DRSLQQTKRQ HSAPSQISAN ENNIYNLGTL 951 EEFVSSGDLT DLYHTLWNDN TSYPFL*

Amino Acid Sequence (or in FASTA format)

       1  MKVKKSTRSK VSTACVNCRK RKIKCTGKYP CTNCISYDCT CVFLKKHLPQ
      51  KEDSSQSLPT TAVAPPSSHA NVEASADVQH LDTAIKLDNQ YYFKLMNDLI
     101  QTPVSPSATH APDTSNNPTN DNNILFKDDS KYQNQLVTYQ NILTNLYALP
     151  PCDDTQLLID KTKSQLNNLI NSWNPEINYP KLSSFSPRPQ RSIETYLLTN
     201  KYRNKIHMTR FSFWTDQMVK SQSPDSFLAT TPLVDEVFGL FSPIQAFSLR
     251  GIGYLIKKNI ENTGSSMLID TKETIYLILR LFDLCYEHLI QGCISISNPL
     301  ENYLQKIKQT PTTTASASLP TSPAPLSNDL VISVIHQLPQ PFIQSITGFT
     351  TTQLIENLHD SFSMFRIVTQ MYAQHRKRFA EFLNQAFSLP HQEKSVLFSS
     401  FCSSEYLLST LCYAYYNVTL YHMLDINTLD YLEILVSLLE IQNEIDERFG
     451  FEKMLEVAVT CSTKMGLSRW EYYVGIDENT AERRRKIWWK IYSLEKRFLT
     501  DLGDLSLINE HQMNCLLPKD FRDMGFINHK EFLTKIGTSS LSPSSPKLKN
     551  LSLSRLIEYG ELAIAQIVGD FFSETLYNEK FTSLEVSVKP TIIRQKLLEK
     601  VFEDIESFRL KLAKIKLHTS RVFQVAHCKY PEYPKNDLIE AAKFVSYHKN
     651  TWFSILGAVN NLIARLSEDP EVITEQSMKY ANEMFQEWRE INQFLIQVDT
     701  DFIVWACLDF YELIFFVMAS KFYVEDPHIT LEDVINTLKV FKRITNIISF
     751  FNNNLDEKDY DCQTFREFSR SSSLVAISIR IIFLKYCYAE QIDRAEFIER
     801  LKEVEPGLSD LLREFFDTRS FIYRYMLKSV EKSGFHLIIR KMLESDYKFL
     851  YRDKLATGNI PDQGNSSQIS QLYDSTAPSY NNASASAANS PLKLSSLLNS
     901  GEESYTQDAS ENVPCNLRHQ DRSLQQTKRQ HSAPSQISAN ENNIYNLGTL
     951  EEFVSSGDLT DLYHTLWNDN TSYPFL*

external links for Pdr3p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
YGOB	BioPIXIE	MIPS	YeastGFP
YOGY	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
	Complexome	YeastRC Structure Prediction (Seattle)
	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Pdr3p

1)	Wolfger H, et al. (1997) The yeast ATP binding cassette (ABC) protein genes PDR10 and PDR15 are novel targets for the Pdr1 and Pdr3 transcriptional regulators. FEBS Lett 418(3):269-74
2)	Delaveau T, et al. (1994) PDR3, a new yeast regulatory gene, is homologous to PDR1 and controls the multidrug resistance phenomenon. Mol Gen Genet 244(5):501-11
3)	Balzi E and Goffeau A (1995) Yeast multidrug resistance: the PDR network. J Bioenerg Biomembr 27(1):71-6
4)	Kean LS, et al. (1997) Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. J Cell Biol 138(2):255-70
5)	Zhang X and Moye-Rowley WS (2001) Saccharomyces cerevisiae multidrug resistance gene expression inversely correlates with the status of the F(0) component of the mitochondrial ATPase. J Biol Chem 276(51):47844-52
6)	Devaux F, et al. (2002) Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. FEBS Lett 515(1-3):25-8
7)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
8)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
9)	Subik J, et al. (1986) Genetic mapping of nuclear mucidin resistance mutations in Saccharomyces cerevisiae. A new pdr locus on chromosome II. Curr Genet 10(9):665-70
10)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41