Reviewed, UniProtKB/Swiss-Prot Q12675 (ATC4_YEAST)

Names and origin

Protein names

Recommended name:
    Probable phospholipid-transporting ATPase DNF2
    EC=3.6.3.1

Gene names

Name:	DNF2
Ordered Locus Names:	YDR093W
ORF Names:	YD8557.01

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Required for protein transport from Golgi to vacuoles. Ref.2
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein. Ref.2
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IV subfamily.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro endocytosis Inferred from genetic interaction. Source: SGD establishment or maintenance of cell polarity Inferred from genetic interaction. Source: SGD intracellular protein transport Ref.2 Inferred from genetic interaction. Source: SGD phospholipid translocation Inferred from mutant phenotype. Source: SGD transmembrane transport Inferred from mutant phenotype. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: SGD plasma membrane Ref.2 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: UniProtKB-KW phospholipid-translocating ATPase activity Inferred from genetic interaction. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DNF1	P32660	1	EBI-3114,EBI-3121
LEM3	P42838	1	EBI-3114,EBI-28396
MID2	P36027	1	EBI-3114,EBI-10901

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1612	1612	Probable phospholipid-transporting ATPase DNF2		PRO_0000046234
Regions
	Topological domain	1 – 252	252	Cytoplasmic Potential
	Transmembrane	253 – 273	21	Potential
	Topological domain	274 – 277	4	Extracellular Potential
	Transmembrane	278 – 298	21	Potential
	Topological domain	299 – 598	300	Cytoplasmic Potential
	Transmembrane	599 – 619	21	Potential
	Topological domain	620 – 639	20	Extracellular Potential
	Transmembrane	640 – 660	21	Potential
	Topological domain	661 – 1231	571	Cytoplasmic Potential
	Transmembrane	1232 – 1252	21	Potential
	Topological domain	1253 – 1262	10	Extracellular Potential
	Transmembrane	1263 – 1283	21	Potential
	Topological domain	1284 – 1313	30	Cytoplasmic Potential
	Transmembrane	1314 – 1334	21	Potential
	Topological domain	1335 – 1350	16	Extracellular Potential
	Transmembrane	1351 – 1371	21	Potential
	Topological domain	1372 – 1377	6	Cytoplasmic Potential
	Transmembrane	1378 – 1398	21	Potential
	Topological domain	1399 – 1418	20	Extracellular Potential
	Transmembrane	1419 – 1439	21	Potential
	Topological domain	1440 – 1612	173	Cytoplasmic Potential
Sites
	Active site	712	1	4-aspartylphosphate intermediate Probable
Amino acid modifications
	Modified residue	70	1	Phosphothreonine Ref.5
	Modified residue	386	1	Phosphoserine Ref.6
	Modified residue	389	1	Phosphoserine Ref.5
	Modified residue	392	1	Phosphoserine Ref.5 Ref.6
	Modified residue	396	1	Phosphoserine Ref.6
	Modified residue	403	1	Phosphoserine Ref.6
	Modified residue	1532	1	Phosphoserine Ref.6
	Modified residue	1542	1	Phosphoserine Ref.5 Ref.6 Ref.3
	Modified residue	1592	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q12675-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 09719DF264256BEC	FASTA	1,612	182,619
	10 20 30 40 50 60 MSSPSKPTSP FVDDIEHESG SASNGLSSMS PFDDSFQFEK PSSAHGNIEV AKTGGSVLKR 70 80 90 100 110 120 QSKPMKDIST PDLSKVTFDG IDDYSNDNDI NDDDELNGKK TEIHEHENEV DDDLHSFQAT 130 140 150 160 170 180 PMPNTGGFED VELDNNEGSN NDSQADHKLK RVRFGTRRNK SGRIDINRSK TLKWAKKNFH 190 200 210 220 230 240 NAIDEFSTKE DSLENSALQN RSDELRTVYY NLPLPEDMLD EDGLPLAVYP RNKIRTTKYT 250 260 270 280 290 300 PLTFFPKNIL FQFHNFANIY FLILLILGAF QIFGVTNPGF ASVPLIVIVI ITAIKDGIED 310 320 330 340 350 360 SRRTVLDLEV NNTRTHILSG VKNENVAVDN VSLWRRFKKA NTRALIKIFE YFSENLTAAG 370 380 390 400 410 420 REKKLQKKRE ELRRKRNSRS FGPRGSLDSI GSYRMSADFG RPSLDYENLN QTMSQANRYN 430 440 450 460 470 480 DGENLVDRTL QPNPECRFAK DYWKNVKVGD IVRVHNNDEI PADMILLSTS DVDGACYVET 490 500 510 520 530 540 KNLDGETNLK VRQSLKCSKI IKSSRDITRT KFWVESEGPH ANLYSYQGNF KWQDTQNGNI 550 560 570 580 590 600 RNEPVNINNL LLRGCTLRNT KWAMGMVIFT GDDTKIMINA GVTPTKKSRI SRELNFSVIL 610 620 630 640 650 660 NFVLLFILCF TAGIVNGVYY KQKPRSRDYF EFGTIGGSAS TNGFVSFWVA VILYQSLVPI 670 680 690 700 710 720 SLYISVEIIK TAQAIFIYTD VLLYNAKLDY PCTPKSWNIS DDLGQIEYIF SDKTGTLTQN 730 740 750 760 770 780 VMEFKKCTIN GVSYGRAYTE ALAGLRKRQG VDVESEGRRE KEEIAKDRET MIDELRSMSD 790 800 810 820 830 840 NTQFCPEDLT FVSKEIVEDL KGSSGDHQQK CCEHFLLALA LCHSVLVEPN KDDPKKLDIK 850 860 870 880 890 900 AQSPDESALV STARQLGYSF VGSSKSGLIV EIQGVQKEFQ VLNVLEFNSS RKRMSCIIKI 910 920 930 940 950 960 PGSTPKDEPK ALLICKGADS VIYSRLDRTQ NDATLLEKTA LHLEEYATEG LRTLCLAQRE 970 980 990 1000 1010 1020 LTWSEYERWV KTYDVAAASV TNREEELDKV TDVIERELIL LGGTAIEDRL QDGVPDSIAL 1030 1040 1050 1060 1070 1080 LAEAGIKLWV LTGDKVETAI NIGFSCNVLN NDMELLVVKA SGEDVEEFGS DPIQVVNNLV 1090 1100 1110 1120 1130 1140 TKYLREKFGM SGSEEELKEA KREHGLPQGN FAVIIDGDAL KVALNGEEMR RKFLLLCKNC 1150 1160 1170 1180 1190 1200 KAVLCCRVSP AQKAAVVKLV KKTLDVMTLA IGDGSNDVAM IQSADVGVGI AGEEGRQAVM 1210 1220 1230 1240 1250 1260 CSDYAIGQFR YVTRLVLVHG KWCYKRLAEM IPQFFYKNVI FTLSLFWYGI YNNFDGSYLF 1270 1280 1290 1300 1310 1320 EYTYLTFYNL AFTSVPVILL AVLDQDVSDT VSMLVPQLYR VGILRKEWNQ TKFLWYMLDG 1330 1340 1350 1360 1370 1380 VYQSVICFFF PYLAYHKNMV VTENGLGLDH RYFVGVFVTA IAVTSCNFYV FMEQYRWDWF 1390 1400 1410 1420 1430 1440 CGLFICLSLA VFYGWTGIWT SSSSSNEFYK GAARVFAQPA YWAVLFVGVL FCLLPRFTID 1450 1460 1470 1480 1490 1500 CIRKIFYPKD IEIVREMWLR GDFDLYPQGY DPTDPSRPRI NEIRPLTDFK EPISLDTHFD 1510 1520 1530 1540 1550 1560 GVSHSQETIV TEEIPMSILN GEQGSRKGYR VSTTLERRDQ LSPVTTTNNL PRRSMASARG 1570 1580 1590 1600 1610 NKLRTSLDRT REEMLANHQL DTRYSVERAR ASLDLPGINH AETLLSQRSR DR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system." Hua Z., Fatheddin P., Graham T.R. Mol. Biol. Cell 13:3162-3177(2002) [PubMed: 12221123] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[3]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542, MASS SPECTROMETRY.
[4]	"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].
[5]	"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 THR-70; SER-389; SER-392 AND SER-1542, 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-386; SER-392; SER-396; SER-403; SER-1532; SER-1542 AND SER-1592, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z47746 Genomic DNA. Translation: CAA87668.1.
PIR	S51243.
RefSeq	NP_010378.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:8055N.
IntAct	Q12675. 4 interactions.
Protein family/group databases
TCDB	3.A.3.8.5. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PeptideAtlas	Q12675.
Genome annotation databases
Ensembl	YDR093W. Saccharomyces cerevisiae. [Contig view]
GeneID	851667.
GenomeReviews	Gene locus YDR093W in contig Z71256_GR.
KEGG	sce:YDR093W.
NMPDR	fig|4932.3.peg.1124.
Organism-specific databases
CYGD	YDR093w.
SGD	S000002500. DNF2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q12675.
OMA	Q12675. NEEIPAD.
Enzyme and pathway databases
BRENDA	3.6.3.1. 250.
Gene expression databases
ArrayExpress	Q12675.
GermOnline	YDR093W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR013200. HAD-SF_hydro-like_3. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF08282. Hydrolase_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969286.

Entry information

Entry name

ATC4_YEAST

Accession

Primary (citable) accession number: Q12675

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)