Phospholipid-transporting ATPase DNF1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32660 (ATC5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phospholipid-transporting ATPase DNF1
EC=3.6.3.1

Alternative name(s):
Flippase DNF1

Gene names

Name:	DNF1
Ordered Locus Names:	YER166W
ORF Names:	SYGP-ORF7

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1571 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids Potential.
Catalytic activity	ATP + H₂O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Golgi apparatus › trans-Golgi network membrane; Multi-pass membrane protein Ref.7.
Post-translational modification	Phosphorylated by FPK1 and KIN82. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cell membrane Endosome Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro endocytosis Inferred from mutant phenotype. Source: SGD establishment or maintenance of cell polarity Inferred from genetic interaction. Source: SGD phospholipid translocation Inferred from mutant phenotype. Source: SGD
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: SGD plasma membrane Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phospholipid-translocating ATPase activity Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LEM3	P42838	4	EBI-3121,EBI-28396

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1571

1571

Phospholipid-transporting ATPase DNF1

PRO_0000046235

Regions

Topological domain

1 – 214

214

Cytoplasmic Potential

Transmembrane

215 – 235

Helical; Potential

Topological domain

236 – 239

Extracellular Potential

Transmembrane

240 – 260

Helical; Potential

Topological domain

261 – 553

293

Cytoplasmic Potential

Transmembrane

554 – 574

Helical; Potential

Topological domain

575 – 594

Extracellular Potential

Transmembrane

595 – 615

Helical; Potential

Topological domain

616 – 1188

573

Cytoplasmic Potential

Transmembrane

1189 – 1209

Helical; Potential

Topological domain

1210 – 1219

Extracellular Potential

Transmembrane

1220 – 1240

Helical; Potential

Topological domain

1241 – 1270

Cytoplasmic Potential

Transmembrane

1271 – 1291

Helical; Potential

Topological domain

1292 – 1307

Extracellular Potential

Transmembrane

1308 – 1328

Helical; Potential

Topological domain

1329 – 1334

Cytoplasmic Potential

Transmembrane

1335 – 1355

Helical; Potential

Topological domain

1356 – 1375

Extracellular Potential

Transmembrane

1376 – 1396

Helical; Potential

Topological domain

1397 – 1571

175

Cytoplasmic Potential

Sites

Active site

667

4-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.5 Ref.6 Ref.8

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphotyrosine Ref.8

Modified residue

Phosphoserine Ref.4 Ref.8

Modified residue

Phosphothreonine Ref.4

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphothreonine Ref.8

Modified residue

347

Phosphoserine Ref.8

Modified residue

351

Phosphoserine Ref.8

Modified residue

365

Phosphoserine Ref.6 Ref.8

Modified residue

1460

Phosphoserine Ref.8

Modified residue

1483

Phosphoserine Ref.8

Modified residue

1506

Phosphoserine Ref.4 Ref.8

Modified residue

1545

Phosphoserine Ref.8

Modified residue

1551

Phosphothreonine Ref.8

Modified residue

1552

Phosphoserine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P32660 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 3CC3FBA8ADDE8960
Show »

FASTA

1,571

177,798

        10         20         30         40         50         60 
MSGTFHGDGH APMSPFEDTF QFEDNSSNED THIAPTHFDD GATSNKYSRP QVSFNDETPK 

        70         80         90        100        110        120 
NKREDAEEFT FNDDTEYDNH SFQPTPKLNN GSGTFDDVEL DNDSGEPHTN YDGMKRFRMG 

       130        140        150        160        170        180 
TKRNKKGNPI MGRSKTLKWA RKNIPNPFED FTKDDIDPGA INRAQELRTV YYNMPLPKDM 

       190        200        210        220        230        240 
IDEEGNPIMQ YPRNKIRTTK YTPLTFLPKN ILFQFHNFAN VYFLVLIILG AFQIFGVTNP 

       250        260        270        280        290        300 
GLSAVPLVVI VIITAIKDAI EDSRRTVLDL EVNNTKTHIL EGVENENVST DNISLWRRFK 

       310        320        330        340        350        360 
KANSRLLFKF IQYCKEHLTE EGKKKRMQRK RHELRVQKTV GTSGPRSSLD SIDSYRVSAD 

       370        380        390        400        410        420 
YGRPSLDYDN LEQGAGEANI VDRSLPPRTD CKFAKNYWKG VKVGDIVRIH NNDEIPADII 

       430        440        450        460        470        480 
LLSTSDTDGA CYVETKNLDG ETNLKVRQSL KCTNTIRTSK DIARTKFWIE SEGPHSNLYT 

       490        500        510        520        530        540 
YQGNMKWRNL ADGEIRNEPI TINNVLLRGC TLRNTKWAMG VVMFTGGDTK IMLNSGITPT 

       550        560        570        580        590        600 
KKSRISRELN FSVVINFVLL FILCFVSGIA NGVYYDKKGR SRFSYEFGTI AGSAATNGFV 

       610        620        630        640        650        660 
SFWVAVILYQ SLVPISLYIS VEIIKTAQAA FIYGDVLLYN AKLDYPCTPK SWNISDDLGQ 

       670        680        690        700        710        720 
VEYIFSDKTG TLTQNVMEFK KCTINGVSYG RAYTEALAGL RKRQGIDVET EGRREKAEIA 

       730        740        750        760        770        780 
KDRDTMIDEL RALSGNSQFY PEEVTFVSKE FVRDLKGASG EVQQRCCEHF MLALALCHSV 

       790        800        810        820        830        840 
LVEANPDNPK KLDLKAQSPD EAALVATARD VGFSFVGKTK KGLIIEMQGI QKEFEILNIL 

       850        860        870        880        890        900 
EFNSSRKRMS CIVKIPGLNP GDEPRALLIC KGADSIIYSR LSRQSGSNSE AILEKTALHL 

       910        920        930        940        950        960 
EQYATEGLRT LCIAQRELSW SEYEKWNEKY DIAAASLANR EDELEVVADS IERELILLGG 

       970        980        990       1000       1010       1020 
TAIEDRLQDG VPDCIELLAE AGIKLWVLTG DKVETAINIG FSCNLLNNEM ELLVIKTTGD 

      1030       1040       1050       1060       1070       1080 
DVKEFGSEPS EIVDALLSKY LKEYFNLTGS EEEIFEAKKD HEFPKGNYAI VIDGDALKLA 

      1090       1100       1110       1120       1130       1140 
LYGEDIRRKF LLLCKNCRAV LCCRVSPSQK AAVVKLVKDS LDVMTLAIGD GSNDVAMIQS 

      1150       1160       1170       1180       1190       1200 
ADVGIGIAGE EGRQAVMCSD YAIGQFRYLA RLVLVHGRWS YKRLAEMIPE FFYKNMIFAL 

      1210       1220       1230       1240       1250       1260 
ALFWYGIYND FDGSYLYEYT YMMFYNLAFT SLPVIFLGIL DQDVNDTISL VVPQLYRVGI 

      1270       1280       1290       1300       1310       1320 
LRKEWNQRKF LWYMLDGLYQ SIICFFFPYL VYHKNMIVTS NGLGLDHRYF VGVYVTTIAV 

      1330       1340       1350       1360       1370       1380 
ISCNTYVLLH QYRWDWFSGL FIALSCLVVF AWTGIWSSAI ASREFFKAAA RIYGAPSFWA 

      1390       1400       1410       1420       1430       1440 
VFFVAVLFCL LPRFTYDSFQ KFFYPTDVEI VREMWQHGHF DHYPPGYDPT DPNRPKVTKA 

      1450       1460       1470       1480       1490       1500 
GQHGEKIIEG IALSDNLGGS NYSRDSVVTE EIPMTFMHGE DGSPSGYQKQ ETWMTSPKET 

      1510       1520       1530       1540       1550       1560 
QDLLQSPQFQ QAQTFGRGPS TNVRSSLDRT REQMIATNQL DNRYSVERAR TSLDLPGVTN 

      1570 
AASLIGTQQN N

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 16847258] [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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; THR-85 AND SER-1506, MASS SPECTROMETRY. 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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, MASS SPECTROMETRY.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-92 AND SER-365, MASS SPECTROMETRY.
[7]	"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: 18199685] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY FPK1 AND KIN82.
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; THR-58; TYR-77; SER-81; THR-94; SER-347; SER-351; SER-365; SER-1460; SER-1483; SER-1506; SER-1545; THR-1551 AND SER-1552, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18922 Genomic DNA. Translation: AAB64693.1. BK006939 Genomic DNA. Translation: DAA07828.1.
PIR	S50669.
RefSeq	NP_011093.1. NM_001179056.1.
3D structure databases
ProteinModelPortal	P32660.
SMR	P32660. Positions 1109-1164.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-7949N.
IntAct	P32660. 18 interactions.
MINT	MINT-1364907.
STRING	P32660.
Protein family/group databases
TCDB	3.A.3.8.4. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PeptideAtlas	P32660.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER166W; YER166W; YER166W.
GeneID	856913.
KEGG	sce:YER166W.
NMPDR	fig\|4932.3.peg.2179.
Organism-specific databases
CYGD	YER166w.
SGD	S000000968. DNF1.
Phylogenomic databases
eggNOG	fuNOG04167.
GeneTree	EFGT00050000000755.
HOGENOM	HBG745019.
OMA	ALFWYGI.
OrthoDB	EOG44BF99.
Gene expression databases
ArrayExpress	P32660.
Genevestigator	P32660.
GermOnline	YER166W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 3 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01530.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983359.

Entry information

Entry name

ATC5_YEAST

Accession

Primary (citable) accession number: P32660
Secondary accession number(s): D3DM74

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents