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Reviewed, UniProtKB/Swiss-Prot P32660 (ATC5_YEAST)

Last modified February 9, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable phospholipid-transporting ATPase DNF1
    EC=3.6.3.1
Gene names
Name: DNF1
Ordered Locus Names: YER166W
ORF Names: SYGP-ORF7
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length1571 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15711571Probable phospholipid-transporting ATPase DNF1
PRO_0000046235

Regions

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

Sites

Active site66714-aspartylphosphate intermediate By similarity

Amino acid modifications

Modified residue531Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue581Phosphothreonine Ref.6
Modified residue771Phosphotyrosine Ref.6
Modified residue811Phosphoserine Ref.6 Ref.3
Modified residue851Phosphothreonine Ref.3
Modified residue921Phosphoserine Ref.5
Modified residue941Phosphothreonine Ref.6
Modified residue3471Phosphoserine Ref.6
Modified residue3511Phosphoserine Ref.6
Modified residue3651Phosphoserine Ref.5 Ref.6
Modified residue14601Phosphoserine Ref.6
Modified residue14831Phosphoserine Ref.6
Modified residue15061Phosphoserine Ref.6 Ref.3
Modified residue15451Phosphoserine Ref.6
Modified residue15511Phosphothreonine Ref.6
Modified residue15521Phosphoserine Ref.6

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Sequences

Sequence LengthMass (Da)Tools
P32660-1 [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

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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: 9169868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"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].
[3]"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.
[4]"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.
[5]"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.
[6]"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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U18922 Genomic DNA. Translation: AAB64693.1.
PIRS50669.
RefSeqNP_011093.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-7949N.
IntActP32660. 22 interactions.
STRINGP32660.

Protein family/group databases

TCDB3.A.3.8.4. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PeptideAtlasP32660.

Genome annotation databases

EnsemblYER166W; YER166W; YER166W; Saccharomyces cerevisiae. [Genome view]
GeneID856913.
KEGGsce:YER166W.
NMPDRfig|4932.3.peg.2179.

Organism-specific databases

CYGDYER166w.
SGDS000000968. DNF1.

Phylogenomic databases

eggNOGfuNOG04167.
HOGENOMHBG745019.
OMAALFWYGI.
OrthoDBEOG9C898R.
PhylomeDBP32660.

Enzyme and pathway databases

BRENDA3.6.3.1. 250.

Gene expression databases

ArrayExpressP32660.
GenevestigatorP32660.
GermOnlineYER166W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transl.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio983359.

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Entry information

Entry nameATC5_YEAST
AccessionPrimary (citable) accession number: P32660
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome V

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents