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Protein

Phospholipid-transporting ATPase DNF1

Gene

DNF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids.Curated

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei667 – 66714-aspartylphosphate intermediateBy similarity

GO - Molecular functioni

  1. ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Source: SGD
  2. ATP binding Source: UniProtKB-KW
  3. magnesium ion binding Source: InterPro
  4. phospholipid-translocating ATPase activity Source: SGD

GO - Biological processi

  1. endocytosis Source: SGD
  2. establishment or maintenance of cell polarity Source: SGD
  3. intracellular protein transport Source: SGD
  4. ion transmembrane transport Source: GOC
  5. phospholipid translocation Source: SGD
  6. response to pheromone involved in conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30327-MONOMER.
BRENDAi3.6.3.1. 984.
ReactomeiREACT_271569. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.8.4. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase DNF1 (EC:3.6.3.1)
Alternative name(s):
Flippase DNF1
Gene namesi
Name:DNF1
Ordered Locus Names:YER166W
ORF Names:SYGP-ORF7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYER166w.
EuPathDBiFungiDB:YER166W.
SGDiS000000968. DNF1.

Subcellular locationi

  1. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
  2. Endosome membrane 1 Publication; Multi-pass membrane protein 1 Publication
  3. Golgi apparatustrans-Golgi network membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 214214CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 2394ExtracellularSequence Analysis
Transmembranei240 – 26021HelicalSequence AnalysisAdd
BLAST
Topological domaini261 – 553293CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei554 – 57421HelicalSequence AnalysisAdd
BLAST
Topological domaini575 – 59420ExtracellularSequence AnalysisAdd
BLAST
Transmembranei595 – 61521HelicalSequence AnalysisAdd
BLAST
Topological domaini616 – 1188573CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1189 – 120921HelicalSequence AnalysisAdd
BLAST
Topological domaini1210 – 121910ExtracellularSequence Analysis
Transmembranei1220 – 124021HelicalSequence AnalysisAdd
BLAST
Topological domaini1241 – 127030CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1271 – 129121HelicalSequence AnalysisAdd
BLAST
Topological domaini1292 – 130716ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1308 – 132821HelicalSequence AnalysisAdd
BLAST
Topological domaini1329 – 13346CytoplasmicSequence Analysis
Transmembranei1335 – 135521HelicalSequence AnalysisAdd
BLAST
Topological domaini1356 – 137520ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1376 – 139621HelicalSequence AnalysisAdd
BLAST
Topological domaini1397 – 1571175CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endosome membrane Source: UniProtKB-SubCell
  2. Golgi apparatus Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. Lem3p-Dnf1p complex Source: SGD
  5. mating projection tip membrane Source: SGD
  6. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15711571Phospholipid-transporting ATPase DNF1PRO_0000046235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Phosphoserine3 Publications
Modified residuei70 – 701Phosphothreonine1 Publication
Modified residuei81 – 811Phosphoserine2 Publications
Modified residuei85 – 851Phosphothreonine2 Publications
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei94 – 941Phosphothreonine1 Publication
Modified residuei104 – 1041Phosphoserine1 Publication
Modified residuei109 – 1091Phosphothreonine1 Publication
Modified residuei351 – 3511Phosphoserine1 Publication
Modified residuei365 – 3651Phosphoserine1 Publication
Modified residuei1506 – 15061Phosphoserine3 Publications
Modified residuei1551 – 15511Phosphothreonine1 Publication
Modified residuei1552 – 15521Phosphoserine1 Publication
Modified residuei1563 – 15631Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by FPK1 and KIN82.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32660.
PaxDbiP32660.
PeptideAtlasiP32660.

Expressioni

Gene expression databases

GenevestigatoriP32660.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LEM3P428384EBI-3121,EBI-28396

Protein-protein interaction databases

BioGridi36919. 36 interactions.
DIPiDIP-7949N.
IntActiP32660. 16 interactions.
MINTiMINT-1364907.
STRINGi4932.YER166W.

Structurei

3D structure databases

ProteinModelPortaliP32660.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00780000122861.
HOGENOMiHOG000202528.
InParanoidiP32660.
KOiK01530.
OMAiTHILEGV.
OrthoDBiEOG7FR7QR.

Family and domain databases

Gene3Di2.70.150.10. 3 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR001757. P_typ_ATPase.
IPR026871. PLip_transp_ATPase.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PTHR24092:SF7. PTHR24092:SF7. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32660-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTFHGDGH APMSPFEDTF QFEDNSSNED THIAPTHFDD GATSNKYSRP
60 70 80 90 100
QVSFNDETPK NKREDAEEFT FNDDTEYDNH SFQPTPKLNN GSGTFDDVEL
110 120 130 140 150
DNDSGEPHTN YDGMKRFRMG TKRNKKGNPI MGRSKTLKWA RKNIPNPFED
160 170 180 190 200
FTKDDIDPGA INRAQELRTV YYNMPLPKDM IDEEGNPIMQ YPRNKIRTTK
210 220 230 240 250
YTPLTFLPKN ILFQFHNFAN VYFLVLIILG AFQIFGVTNP GLSAVPLVVI
260 270 280 290 300
VIITAIKDAI EDSRRTVLDL EVNNTKTHIL EGVENENVST DNISLWRRFK
310 320 330 340 350
KANSRLLFKF IQYCKEHLTE EGKKKRMQRK RHELRVQKTV GTSGPRSSLD
360 370 380 390 400
SIDSYRVSAD YGRPSLDYDN LEQGAGEANI VDRSLPPRTD CKFAKNYWKG
410 420 430 440 450
VKVGDIVRIH NNDEIPADII LLSTSDTDGA CYVETKNLDG ETNLKVRQSL
460 470 480 490 500
KCTNTIRTSK DIARTKFWIE SEGPHSNLYT YQGNMKWRNL ADGEIRNEPI
510 520 530 540 550
TINNVLLRGC TLRNTKWAMG VVMFTGGDTK IMLNSGITPT KKSRISRELN
560 570 580 590 600
FSVVINFVLL FILCFVSGIA NGVYYDKKGR SRFSYEFGTI AGSAATNGFV
610 620 630 640 650
SFWVAVILYQ SLVPISLYIS VEIIKTAQAA FIYGDVLLYN AKLDYPCTPK
660 670 680 690 700
SWNISDDLGQ VEYIFSDKTG TLTQNVMEFK KCTINGVSYG RAYTEALAGL
710 720 730 740 750
RKRQGIDVET EGRREKAEIA KDRDTMIDEL RALSGNSQFY PEEVTFVSKE
760 770 780 790 800
FVRDLKGASG EVQQRCCEHF MLALALCHSV LVEANPDNPK KLDLKAQSPD
810 820 830 840 850
EAALVATARD VGFSFVGKTK KGLIIEMQGI QKEFEILNIL EFNSSRKRMS
860 870 880 890 900
CIVKIPGLNP GDEPRALLIC KGADSIIYSR LSRQSGSNSE AILEKTALHL
910 920 930 940 950
EQYATEGLRT LCIAQRELSW SEYEKWNEKY DIAAASLANR EDELEVVADS
960 970 980 990 1000
IERELILLGG TAIEDRLQDG VPDCIELLAE AGIKLWVLTG DKVETAINIG
1010 1020 1030 1040 1050
FSCNLLNNEM ELLVIKTTGD DVKEFGSEPS EIVDALLSKY LKEYFNLTGS
1060 1070 1080 1090 1100
EEEIFEAKKD HEFPKGNYAI VIDGDALKLA LYGEDIRRKF LLLCKNCRAV
1110 1120 1130 1140 1150
LCCRVSPSQK AAVVKLVKDS LDVMTLAIGD GSNDVAMIQS ADVGIGIAGE
1160 1170 1180 1190 1200
EGRQAVMCSD YAIGQFRYLA RLVLVHGRWS YKRLAEMIPE FFYKNMIFAL
1210 1220 1230 1240 1250
ALFWYGIYND FDGSYLYEYT YMMFYNLAFT SLPVIFLGIL DQDVNDTISL
1260 1270 1280 1290 1300
VVPQLYRVGI LRKEWNQRKF LWYMLDGLYQ SIICFFFPYL VYHKNMIVTS
1310 1320 1330 1340 1350
NGLGLDHRYF VGVYVTTIAV ISCNTYVLLH QYRWDWFSGL FIALSCLVVF
1360 1370 1380 1390 1400
AWTGIWSSAI ASREFFKAAA RIYGAPSFWA VFFVAVLFCL LPRFTYDSFQ
1410 1420 1430 1440 1450
KFFYPTDVEI VREMWQHGHF DHYPPGYDPT DPNRPKVTKA GQHGEKIIEG
1460 1470 1480 1490 1500
IALSDNLGGS NYSRDSVVTE EIPMTFMHGE DGSPSGYQKQ ETWMTSPKET
1510 1520 1530 1540 1550
QDLLQSPQFQ QAQTFGRGPS TNVRSSLDRT REQMIATNQL DNRYSVERAR
1560 1570
TSLDLPGVTN AASLIGTQQN N
Length:1,571
Mass (Da):177,798
Last modified:February 1, 1995 - v2
Checksum:i3CC3FBA8ADDE8960
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA. Translation: AAB64693.1.
BK006939 Genomic DNA. Translation: DAA07828.1.
PIRiS50669.
RefSeqiNP_011093.3. NM_001179056.3.

Genome annotation databases

EnsemblFungiiYER166W; YER166W; YER166W.
GeneIDi856913.
KEGGisce:YER166W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18922 Genomic DNA. Translation: AAB64693.1.
BK006939 Genomic DNA. Translation: DAA07828.1.
PIRiS50669.
RefSeqiNP_011093.3. NM_001179056.3.

3D structure databases

ProteinModelPortaliP32660.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36919. 36 interactions.
DIPiDIP-7949N.
IntActiP32660. 16 interactions.
MINTiMINT-1364907.
STRINGi4932.YER166W.

Protein family/group databases

TCDBi3.A.3.8.4. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBiP32660.
PaxDbiP32660.
PeptideAtlasiP32660.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER166W; YER166W; YER166W.
GeneIDi856913.
KEGGisce:YER166W.

Organism-specific databases

CYGDiYER166w.
EuPathDBiFungiDB:YER166W.
SGDiS000000968. DNF1.

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00780000122861.
HOGENOMiHOG000202528.
InParanoidiP32660.
KOiK01530.
OMAiTHILEGV.
OrthoDBiEOG7FR7QR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30327-MONOMER.
BRENDAi3.6.3.1. 984.
ReactomeiREACT_271569. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi983359.
PROiP32660.

Gene expression databases

GenevestigatoriP32660.

Family and domain databases

Gene3Di2.70.150.10. 3 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR001757. P_typ_ATPase.
IPR026871. PLip_transp_ATPase.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PTHR24092:SF7. PTHR24092:SF7. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  4. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; THR-85 AND SER-1506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
    Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
    Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY FPK1 AND KIN82.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-351 AND SER-1506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; THR-70; SER-81; THR-85; SER-92; THR-94; SER-104; THR-109; SER-365; SER-1506; THR-1551; SER-1552 AND SER-1563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATC5_YEAST
AccessioniPrimary (citable) accession number: P32660
Secondary accession number(s): D3DM74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: April 29, 2015
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.