Reviewed, UniProtKB/Swiss-Prot P40527 (ATC7_YEAST)

Names and origin

Protein names

Recommended name:
    Probable phospholipid-transporting ATPase NEO1
    EC=3.6.3.1

Gene names

Name:	NEO1
Ordered Locus Names:	YIL048W

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	1151 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. Leads to neomycin-resistance when overexpressed. Required for traffic between late Golgi and early endosomes. Ref.2
Catalytic activity	ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subunit structure	Interacts with MON2. Ref.2
Subcellular location	Endosome membrane; Multi-pass membrane protein. Golgi apparatus 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	Endosome Golgi apparatus 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 Ref.2 Inferred from mutant phenotype. Source: SGD phospholipid transport Inferred from electronic annotation. Source: InterPro protein transport Inferred from electronic annotation. Source: UniProtKB-KW retrograde vesicle-mediated transport, Golgi to ER Inferred from mutant phenotype. Source: SGD vacuole organization Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	Golgi membrane Inferred from direct assay. Source: SGD endosome Ref.2 Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SFT2	P38166	1	EBI-3137,EBI-17046
SSA2	P10592	1	EBI-3137,EBI-8603

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1151	1151	Probable phospholipid-transporting ATPase NEO1		PRO_0000046236
Regions
	Topological domain	1 – 184	184	Extracellular Potential
	Transmembrane	185 – 205	21	Potential
	Topological domain	206 – 209	4	Cytoplasmic Potential
	Transmembrane	210 – 230	21	Potential
	Topological domain	231 – 367	137	Extracellular Potential
	Transmembrane	368 – 388	21	Potential
	Topological domain	389 – 416	28	Cytoplasmic Potential
	Transmembrane	417 – 437	21	Potential
	Topological domain	438	1	Extracellular Potential
	Transmembrane	439 – 459	21	Potential
	Topological domain	460 – 947	488	Cytoplasmic Potential
	Transmembrane	948 – 968	21	Potential
	Topological domain	969 – 970	2	Extracellular Potential
	Transmembrane	971 – 991	21	Potential
	Topological domain	992 – 1020	29	Cytoplasmic Potential
	Transmembrane	1021 – 1041	21	Potential
	Topological domain	1042 – 1052	11	Extracellular Potential
	Transmembrane	1053 – 1073	21	Potential
	Topological domain	1074 – 1078	5	Cytoplasmic Potential
	Transmembrane	1079 – 1099	21	Potential
	Topological domain	1100 – 1109	10	Extracellular Potential
	Transmembrane	1110 – 1130	21	Potential
	Topological domain	1131 – 1151	21	Cytoplasmic Potential
	Region	1131 – 1151	21	Required for endosomal targeting
Sites
	Active site	503	1	4-aspartylphosphate intermediate Probable
Amino acid modifications
	Modified residue	64	1	Phosphoserine Ref.6
	Modified residue	102	1	Phosphoserine Ref.6 Ref.4
	Modified residue	115	1	Phosphoserine Ref.6
	Modified residue	551	1	Phosphoserine Ref.6 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P40527-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: DC7225CC9577DBE6	FASTA	1,151	130,218
	10 20 30 40 50 60 MPNPPSFKSH KQNLFNSNNN QHANSVDSFD LHLDDSFDAA LDSLQINNNP EPLSKHNTVG 70 80 90 100 110 120 DRESFEMRTV DDLDNFSNHS SDSHRKSSNT DTHPLMYDNR LSQDDNFKFT NIASSPPSSS 130 140 150 160 170 180 NNIFSKALSY LKVSNTKNWS KFGSPIELSD QHIEREIHPD TTPVYDRNRY VSNELSNAKY 190 200 210 220 230 240 NAVTFVPTLL YEQFKFFYNL YFLVVALSQA VPALRIGYLS SYIVPLAFVL TVTMAKEAID 250 260 270 280 290 300 DIQRRRRDRE SNNELYHVIT RNRSIPSKDL KVGDLIKVHK GDRIPADLVL LQSSEPSGES 310 320 330 340 350 360 FIKTDQLDGE TDWKLRVACP LTQNLSENDL INRISITASA PEKSIHKFLG KVTYKDSTSN 370 380 390 400 410 420 PLSVDNTLWA NTVLASSGFC IACVVYTGRD TRQAMNTTTA KVKTGLLELE INSISKILCA 430 440 450 460 470 480 CVFALSILLV AFAGFHNDDW YIDILRYLIL FSTIIPVSLR VNLDLAKSVY AHQIEHDKTI 490 500 510 520 530 540 PETIVRTSTI PEDLGRIEYL LSDKTGTLTQ NDMQLKKIHL GTVSYTSETL DIVSDYVQSL 550 560 570 580 590 600 VSSKNDSLNN SKVALSTTRK DMSFRVRDMI LTLAICHNVT PTFEDDELTY QAASPDEIAI 610 620 630 640 650 660 VKFTESVGLS LFKRDRHSIS LLHEHSGKTL NYEILQVFPF NSDSKRMGII VRDEQLDEYW 670 680 690 700 710 720 FMQKGADTVM SKIVESNDWL EEETGNMARE GLRTLVIGRK KLNKKIYEQF QKEYNDASLS 730 740 750 760 770 780 MLNRDQQMSQ VITKYLEHDL ELLGLTGVED KLQKDVKSSI ELLRNAGIKI WMLTGDKVET 790 800 810 820 830 840 ARCVSISAKL ISRGQYVHTI TKVTRPEGAF NQLEYLKINR NACLLIDGES LGMFLKHYEQ 850 860 870 880 890 900 EFFDVVVHLP TVIACRCTPQ QKADVALVIR KMTGKRVCCI GDGGNDVSMI QCADVGVGIV 910 920 930 940 950 960 GKEGKQASLA ADFSITQFCH LTELLLWHGR NSYKRSAKLA QFVMHRGLII AICQAVYSIC 970 980 990 1000 1010 1020 SLFEPIALYQ GWLMVGYATC YTMAPVFSLT LDHDIEESLT KIYPELYKEL TEGKSLSYKT 1030 1040 1050 1060 1070 1080 FFVWVLLSLF QGSVIQLFSQ AFTSLLDTDF TRMVAISFTA LVVNELIMVA LEIYTWNKTM 1090 1100 1110 1120 1130 1140 LVTEIATLLF YIVSVPFLGD YFDLGYMTTV NYYAGLLVIL LISIFPVWTA KAIYRRLHPP 1150 SYAKVQEFAT P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Molecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system." Wicky S., Schwarz H., Singer-Krueger B. Mol. Cell. Biol. 24:7402-7418(2004) [PubMed: 15314152] [Abstract] Cited for: INTERACTION WITH MON2, SUBCELLULAR LOCATION, FUNCTION.
[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].
[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-102, 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-551, 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-64; SER-102; SER-115 AND SER-551, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38060 Genomic DNA. Translation: CAA86174.1.
PIR	S48431.
RefSeq	NP_012216.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2548N.
IntAct	P40527. 4 interactions.
STRING	P40527.
Genome annotation databases
Ensembl	YIL048W; YIL048W; YIL048W; Saccharomyces cerevisiae. [Genome view]
GeneID	854763.
KEGG	sce:YIL048W.
NMPDR	fig|4932.3.peg.1747.
Organism-specific databases
CYGD	YIL048w.
SGD	S000001310. NEO1.
Phylogenomic databases
eggNOG	fuNOG05222.
HOGENOM	HBG720821.
OMA	KDENIPG.
OrthoDB	EOG9S4QZD.
PhylomeDB	P40527.
Enzyme and pathway databases
BRENDA	3.6.3.1. 250.
Gene expression databases
ArrayExpress	P40527.
Genevestigator	P40527.
GermOnline	YIL048W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR005834. Dehalogen-like_hydro. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 4 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	977511.

Entry information

Entry name

ATC7_YEAST

Accession

Primary (citable) accession number: P40527

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)