Basic Information
Name | ABC transporter ATP-binding protein/permease PDR18 (Pleiotropic drug resistance protein 18) |
Uniprot ID | P53756 |
Systematic gene name | YNR070W |
Standard gene name | PDR18 |
Gene names | PDR18 YNR070W N3568 |
Description from SGD | YNR070W PDR18 SGDID:S000005353, Chr XIV from 765375-769376, Genome Release 64-3-1, Verified ORF, "Putative transporter of the ATP-binding cassette (ABC) family; role in plasma membrane sterol incorporation; implicated in pleiotropic drug resistance; provides resistance to ethanol stress and contributes to a decreased intracellular accumulation of ethanol; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies" |
Protein length | 1333 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MECVSVEGLD SSFLEGQTFG DILCLPWTII KGIRERKNRN KMKIILKNVS
LLAKSGEMVL VLGRPGAGCT SFLKSAAGET SQFAGGVTTG HISYDGIPQK
EMMQHYKPDV IYNGEQDVHF PHLTVKQTLD FAISCKMPAK RVNNVTKEEY
ITANREFYAK IFGLTHTFDT KVGNDFISGV SGGERKRVSI AEALAAKGSI
YCWDNATRGL DSSTALEFAR AIRTMTNLLG TTALVTVYQA SENIYETFDK
VTVLYAGRQI FCGKTTEAKD YFENMGYLCP PRQSTAEYLT AITDPNGLHE
IKPGFEYQVP HTADEFEKYW LDSPEYARLK GEIQKYKHEV NTEWTKKTYN
ESMAQEKSKG TRKKSYYTVS YWEQIRLCTI RGFLRIYGDK SYTVINTCAA
IAQAFITGSL FYQAPSSTLG AFSRSGVLFF SLLYYSLMGL ANISFEHRPI
LQKHKVYSLY HPSAEALAST ISSFPFRMIG LTFFIIILYF LAGLHRSAGA
FFTMYLLLTM CSEAITSLFQ MVSSLCDTLS QANSIAGVVM LSIAMYSTYM
IQLPSMHPWF KWISYILPIR YAFESMLNAE FHGRHMDCGG TLVPSGPGFE
NILPENQVCA FVGSRPGQSW VLGDDYLRAQ YQYEYKNTWR NFGIMWCFLI
GYIVLRAVFT EYKSPVKSGG DALVVKKGTK NAIQRSWSSK NDEENLNASI
ATQDMKEIAS SNDDSTSADF EGLESTGVFI WKNVSFTIPH SSGQRKLLDS
VSGYCVPGTL TALIGESGAG KTTLLNTLAQ RNVGTITGDM LVDGLPMDAS
FKRRTGYVQQ QDLHVAELTV KESLQFSARM RRPQSIPDAE KMEYVEKIIS
ILEMQEFSEA LVGEIGYGLN VEQRKKLSIG VELVGKPDLL LFLDEPTSGL
DSQSAWAVVK MLKRLALAGQ SILCTIHQPS ATLFEQFDRL LLLGKGGQTI
YFGEIGKNSS SVIKYFEKNG ARKCQQNENP AEYILEAIGA GATASVQQNW
PDIWQKSHEY ANINEKINDM IKDLSSTTLH KTATRASKYA TSYSYQFHHV
LKRSSLTFWR NLNYIMAKMM LLMISGLFIG FTFFHVGVNA IGLQNSLFAC
FMAIVISAPA TNQIQERATV AKELYEVRES KSNMFHWSLL LITHYLNELP
YHLLFSTIFF VSSYFPLGVF TEASRSSVFY LNYAILFQLY YIGLALMILY
MSPNLQSANV IVGFILSFLL SFCGAVQPAS LMPGFWTFMW KLSPYTYFLQ
NLVGLLMHDK PVRCSKKELS LFNPPVGQTC GEFTKPFFEF GTGYIANPDA
TADCAYCQYK VGDEYLARIN ASFSYLWRNF GFI
LLAKSGEMVL VLGRPGAGCT SFLKSAAGET SQFAGGVTTG HISYDGIPQK
EMMQHYKPDV IYNGEQDVHF PHLTVKQTLD FAISCKMPAK RVNNVTKEEY
ITANREFYAK IFGLTHTFDT KVGNDFISGV SGGERKRVSI AEALAAKGSI
YCWDNATRGL DSSTALEFAR AIRTMTNLLG TTALVTVYQA SENIYETFDK
VTVLYAGRQI FCGKTTEAKD YFENMGYLCP PRQSTAEYLT AITDPNGLHE
IKPGFEYQVP HTADEFEKYW LDSPEYARLK GEIQKYKHEV NTEWTKKTYN
ESMAQEKSKG TRKKSYYTVS YWEQIRLCTI RGFLRIYGDK SYTVINTCAA
IAQAFITGSL FYQAPSSTLG AFSRSGVLFF SLLYYSLMGL ANISFEHRPI
LQKHKVYSLY HPSAEALAST ISSFPFRMIG LTFFIIILYF LAGLHRSAGA
FFTMYLLLTM CSEAITSLFQ MVSSLCDTLS QANSIAGVVM LSIAMYSTYM
IQLPSMHPWF KWISYILPIR YAFESMLNAE FHGRHMDCGG TLVPSGPGFE
NILPENQVCA FVGSRPGQSW VLGDDYLRAQ YQYEYKNTWR NFGIMWCFLI
GYIVLRAVFT EYKSPVKSGG DALVVKKGTK NAIQRSWSSK NDEENLNASI
ATQDMKEIAS SNDDSTSADF EGLESTGVFI WKNVSFTIPH SSGQRKLLDS
VSGYCVPGTL TALIGESGAG KTTLLNTLAQ RNVGTITGDM LVDGLPMDAS
FKRRTGYVQQ QDLHVAELTV KESLQFSARM RRPQSIPDAE KMEYVEKIIS
ILEMQEFSEA LVGEIGYGLN VEQRKKLSIG VELVGKPDLL LFLDEPTSGL
DSQSAWAVVK MLKRLALAGQ SILCTIHQPS ATLFEQFDRL LLLGKGGQTI
YFGEIGKNSS SVIKYFEKNG ARKCQQNENP AEYILEAIGA GATASVQQNW
PDIWQKSHEY ANINEKINDM IKDLSSTTLH KTATRASKYA TSYSYQFHHV
LKRSSLTFWR NLNYIMAKMM LLMISGLFIG FTFFHVGVNA IGLQNSLFAC
FMAIVISAPA TNQIQERATV AKELYEVRES KSNMFHWSLL LITHYLNELP
YHLLFSTIFF VSSYFPLGVF TEASRSSVFY LNYAILFQLY YIGLALMILY
MSPNLQSANV IVGFILSFLL SFCGAVQPAS LMPGFWTFMW KLSPYTYFLQ
NLVGLLMHDK PVRCSKKELS LFNPPVGQTC GEFTKPFFEF GTGYIANPDA
TADCAYCQYK VGDEYLARIN ASFSYLWRNF GFI
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[835, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[1245, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1245, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1246, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1246, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1247, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[1247, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |