Reviewed, UniProtKB/Swiss-Prot Q12674 (ATC8_YEAST)

Names and origin

Protein names

Recommended name:
    Probable phospholipid-transporting ATPase DNF3
    EC=3.6.3.1

Gene names

Name:	DNF3
Ordered Locus Names:	YMR162C
ORF Names:	YM8520.11C

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	1656 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 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.

Ontologies

Keywords
Cellular component	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 intracellular protein transport Inferred from genetic interaction. Source: SGD phospholipid translocation Inferred from mutant phenotype. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW trans-Golgi network transport vesicle 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1656	1656	Probable phospholipid-transporting ATPase DNF3		PRO_0000046237
Regions
	Topological domain	1 – 164	164	Extracellular Potential
	Transmembrane	165 – 185	21	Potential
	Topological domain	186 – 451	266	Cytoplasmic Potential
	Transmembrane	452 – 472	21	Potential
	Topological domain	473 – 495	23	Extracellular Potential
	Transmembrane	496 – 516	21	Potential
	Topological domain	517 – 1157	641	Cytoplasmic Potential
	Transmembrane	1158 – 1178	21	Potential
	Topological domain	1179 – 1318	140	Extracellular Potential
	Transmembrane	1319 – 1339	21	Potential
	Topological domain	1340 – 1365	26	Cytoplasmic Potential
	Transmembrane	1366 – 1386	21	Potential
	Topological domain	1387 – 1395	9	Extracellular Potential
	Transmembrane	1396 – 1416	21	Potential
	Topological domain	1417 – 1432	16	Cytoplasmic Potential
	Transmembrane	1433 – 1453	21	Potential
	Topological domain	1454 – 1473	20	Extracellular Potential
	Transmembrane	1474 – 1494	21	Potential
	Topological domain	1495 – 1656	162	Cytoplasmic Potential
Sites
	Active site	566	1	4-aspartylphosphate intermediate Probable
Amino acid modifications
	Modified residue	621	1	Phosphoserine Ref.4
	Modified residue	622	1	Phosphoserine Ref.4
	Modified residue	651	1	Phosphoserine Ref.3
	Modified residue	699	1	Phosphoserine Ref.4
	Modified residue	703	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q12674-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: A20A823BEB401184	FASTA	1,656	188,319
	10 20 30 40 50 60 MGIADGQRRR SSSLRTQMFN KHLYDKYRGR TDDEIELEDI NESKTFSGSD NNDKDDRDET 70 80 90 100 110 120 SGNYAAEEDY EMEEYGSPDV SYSIITKILD TILDRRRTFH SKDGRHIPII LDHNAIEYKQ 130 140 150 160 170 180 AATKRDGHLI DERFNKPYCD NRITSSRYTF YSFLPRQLYA QFSKLANTYF FIVAVLQMIP 190 200 210 220 230 240 GWSTTGTYTT IIPLCVFMGI SMTREAWDDF RRHRLDKEEN NKPVGVLVKD GNNDAQEVYT 250 260 270 280 290 300 LPSSVVSSTA YLTKSAAAEN NPPLNDDRNS SQGHFLDTHF NNFELLKNKY NVHIHQKKWE 310 320 330 340 350 360 KLRVGDFVLL TQDDWVPADL LLLTCDGENS ECFVETMALD GETNLKSKQP HPELNKLTKA 370 380 390 400 410 420 ASGLANINAQ VTVEDPNIDL YNFEGNLELK NHRNDTIMKY PLGPDNVIYR GSILRNTQNV 430 440 450 460 470 480 VGMVIFSGEE TKIRMNALKN PRTKAPKLQR KINMIIVFMV FVVATISLFS YLGHVLHKKK 490 500 510 520 530 540 YIDQNKAWYL FQADAGVAPT IMSFIIMYNT VIPLSLYVTM EIIKVVQSKM MEWDIDMYHA 550 560 570 580 590 600 ETNTPCESRT ATILEELGQV SYIFSDKTGT LTDNKMIFRK FSLCGSSWLH NVDLGNSEDN 610 620 630 640 650 660 FEDNRDNTNS LRLPPKAHNG SSIDVVSIGD QNVLDRLGFS DAPIEKGHRP SLDNFPKSRN 670 680 690 700 710 720 SIEYKGNSSA IYTGRPSMRS LFGKDNSHLS KQASVISPSE TFSENIKSSF DLIQFIQRYP 730 740 750 760 770 780 TALFSQKAKF FFLSLALCHS CLPKKTHNES IGEDSIEYQS SSPDELALVT AARDLGYIVL 790 800 810 820 830 840 NRNAQILTIK TFPDGFDGEA KLENYEILNY IDFNSQRKRM SVLVRMPNQP NQVLLICKGA 850 860 870 880 890 900 DNVIMERLHD RELAAKKMAD ICTSTKERKD AEAELVLQQR KSLERMVDEE AMARTSLRNS 910 920 930 940 950 960 LSSVPRASLS LQAVRKSLSM KNSRTRDPEK QIDSIDQFLE TVKKSDQEIG SVVNKSRKSL 970 980 990 1000 1010 1020 HKQQIEKYGP RISIDGTHFP NNNVPIDTRK EGLQHDYDTE ILEHIGSDEL ILNEEYVIER 1030 1040 1050 1060 1070 1080 TLQAIDEFST EGLRTLVYAY KWIDIGQYEN WNKRYHQAKT SLTDRKIKVD EAGAEIEDGL 1090 1100 1110 1120 1130 1140 NLLGVTAIED KLQDGVSEAI EKIRRAGIKM WMLTGDKRET AINIGYSCML IKDYSTVVIL 1150 1160 1170 1180 1190 1200 TTTDENIISK MNAVSQEVDS GNIAHCVVVI DGATMAMFEG NPTYMSVFVE LCTKTDSVIC 1210 1220 1230 1240 1250 1260 CRASPSQKAL MVSNIRNTDP NLVTLAIGDG ANDIAMIQSA DIGVGIAGKE GLQASRVSDY 1270 1280 1290 1300 1310 1320 SIGQFRFLLK LLFVHGRYNY IRTSKFMLCT FYKEITFYFT QLIYQRYTMF SGSSLYEPWS 1330 1340 1350 1360 1370 1380 LSMFNTLFTS LPVLCIGMFE KDLKPMTLLT VPELYSYGRL SQGFNWLIFM EWVILATTNS 1390 1400 1410 1420 1430 1440 LIITFLNVVM WGMSSLSDNT MYPLGLINFT AIVALINVKS QFVEMHNRNW LAFTSVVLSC 1450 1460 1470 1480 1490 1500 GGWLVWCCAL PILNNTDQIY DVAYGFYNHF GKDITFWCTS LVLALLPITL DIVYKTFKVM 1510 1520 1530 1540 1550 1560 IWPSDSDIFA ELEQKSDIRK KLELGAYSEM RQGWTWDKDP STFTRYTDKV LSRPRTNSRA 1570 1580 1590 1600 1610 1620 SAKTHNSSIY SMSNGNVDHS SKKNFFGNSS KKSSERYEVL PSGKLIKRPS LKTQSSKDSI 1630 1640 1650 GGNITTKLTK KLKLPSRNVE DEDVNQIIQA RLKDLE

References

[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [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]	"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-651, MASS SPECTROMETRY.
[4]	"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-621; SER-622; SER-699 AND SER-703, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49705 Genomic DNA. Translation: CAA89798.1.
PIR	S54520.
RefSeq	NP_013885.1.
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	YMR162C. Saccharomyces cerevisiae. [Contig view]
GeneID	855197.
GenomeReviews	Gene locus YMR162C in contig Z71257_GR.
KEGG	sce:YMR162C.
NMPDR	fig|4932.3.peg.4935.
Organism-specific databases
CYGD	YMR162c.
SGD	S000004772. DNF3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q12674.
OMA	Q12674. MSISIAR.
Enzyme and pathway databases
BRENDA	3.6.3.1. 250.
Gene expression databases
ArrayExpress	Q12674.
GermOnline	YMR162C. 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. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	978676.

Entry information

Entry name

ATC8_YEAST

Accession

Primary (citable) accession number: Q12674

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)