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P32660 (ATC5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1571 AA.
Sequence statusComplete.
Protein existenceEvidence 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(Side 1) = ADP + phosphate + phospholipid(Side 2).

Subcellular location

Cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein Ref.6.

Post-translational modification

Phosphorylated by FPK1 and KIN82. Ref.6

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell membrane
Endosome
Golgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from mutant phenotype PubMed 12631737. Source: SGD

establishment or maintenance of cell polarity

Inferred from genetic interaction PubMed 15461661. Source: SGD

intracellular protein transport

Inferred from genetic interaction PubMed 12221123. Source: SGD

ion transmembrane transport

Inferred from sequence or structural similarity PubMed 9224683. Source: GOC

phospholipid translocation

Inferred from mutant phenotype PubMed 17015438. Source: SGD

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 12221123PubMed 12631737. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

Inferred from sequence or structural similarity PubMed 9224683. Source: SGD

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Inferred from mutant phenotype PubMed 17015438. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LEM3P428384EBI-3121,EBI-28396

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15711571Phospholipid-transporting ATPase DNF1
PRO_0000046235

Regions

Topological domain1 – 214214Cytoplasmic Potential
Transmembrane215 – 23521Helical; Potential
Topological domain236 – 2394Extracellular Potential
Transmembrane240 – 26021Helical; Potential
Topological domain261 – 553293Cytoplasmic Potential
Transmembrane554 – 57421Helical; Potential
Topological domain575 – 59420Extracellular Potential
Transmembrane595 – 61521Helical; Potential
Topological domain616 – 1188573Cytoplasmic Potential
Transmembrane1189 – 120921Helical; Potential
Topological domain1210 – 121910Extracellular Potential
Transmembrane1220 – 124021Helical; Potential
Topological domain1241 – 127030Cytoplasmic Potential
Transmembrane1271 – 129121Helical; Potential
Topological domain1292 – 130716Extracellular Potential
Transmembrane1308 – 132821Helical; Potential
Topological domain1329 – 13346Cytoplasmic Potential
Transmembrane1335 – 135521Helical; Potential
Topological domain1356 – 137520Extracellular Potential
Transmembrane1376 – 139621Helical; Potential
Topological domain1397 – 1571175Cytoplasmic Potential

Sites

Active site66714-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue531Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue701Phosphothreonine Ref.8
Modified residue811Phosphoserine Ref.4 Ref.8
Modified residue851Phosphothreonine Ref.4 Ref.8
Modified residue921Phosphoserine Ref.8
Modified residue941Phosphothreonine Ref.8
Modified residue1041Phosphoserine Ref.8
Modified residue1091Phosphothreonine Ref.8
Modified residue3511Phosphoserine Ref.7
Modified residue3651Phosphoserine Ref.8
Modified residue15061Phosphoserine Ref.4 Ref.7 Ref.8
Modified residue15511Phosphothreonine Ref.8
Modified residue15521Phosphoserine Ref.8
Modified residue15631Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P32660 [UniParc].

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

FASTA1,571177,798
        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' 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. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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] [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18922 Genomic DNA. Translation: AAB64693.1.
BK006939 Genomic DNA. Translation: DAA07828.1.
PIRS50669.
RefSeqNP_011093.3. NM_001179056.3.

3D structure databases

ProteinModelPortalP32660.
SMRP32660. Positions 1107-1174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36919. 35 interactions.
DIPDIP-7949N.
IntActP32660. 16 interactions.
MINTMINT-1364907.
STRING4932.YER166W.

Protein family/group databases

TCDB3.A.3.8.4. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbP32660.
PeptideAtlasP32660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER166W; YER166W; YER166W.
GeneID856913.
KEGGsce:YER166W.

Organism-specific databases

CYGDYER166w.
SGDS000000968. DNF1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00740000115303.
HOGENOMHOG000202528.
KOK01530.
OMATHILEGV.
OrthoDBEOG7FR7QR.

Enzyme and pathway databases

BioCycYEAST:G3O-30327-MONOMER.

Gene expression databases

GenevestigatorP32660.

Family and domain databases

Gene3D2.70.150.10. 3 hits.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
IPR026871. PLip_transp_ATPase_fungal.
[Graphical view]
PANTHERPTHR24092. PTHR24092. 1 hit.
PTHR24092:SF14. PTHR24092:SF14. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983359.

Entry information

Entry nameATC5_YEAST
AccessionPrimary (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: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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

SIMILARITY comments

Index of protein domains and families