Probable phospholipid-transporting ATPase NEO1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40527 (ATC7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [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.3
Catalytic activity	ATP + H₂O + phospholipid(In) = ADP + phosphate + phospholipid(Out).
Subunit structure	Interacts with MON2. Ref.3
Subcellular location	Endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Ref.3.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cation transport Inferred from electronic annotation. Source: InterPro endocytosis Inferred from mutant phenotype Ref.3. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW retrograde vesicle-mediated transport, Golgi to ER Inferred from mutant phenotype. Source: SGD vacuole organization Inferred from mutant phenotype Ref.3. Source: SGD
Cellular component	Golgi membrane Inferred from direct assay. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro phospholipid-translocating ATPase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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

Helical; Potential

Topological domain

206 – 209

Cytoplasmic Potential

Transmembrane

210 – 230

Helical; Potential

Topological domain

231 – 367

137

Extracellular Potential

Transmembrane

368 – 388

Helical; Potential

Topological domain

389 – 416

Cytoplasmic Potential

Transmembrane

417 – 437

Helical; Potential

Topological domain

438

Extracellular Potential

Transmembrane

439 – 459

Helical; Potential

Topological domain

460 – 947

488

Cytoplasmic Potential

Transmembrane

948 – 968

Helical; Potential

Topological domain

969 – 970

Extracellular Potential

Transmembrane

971 – 991

Helical; Potential

Topological domain

992 – 1020

Cytoplasmic Potential

Transmembrane

1021 – 1041

Helical; Potential

Topological domain

1042 – 1052

Extracellular Potential

Transmembrane

1053 – 1073

Helical; Potential

Topological domain

1074 – 1078

Cytoplasmic Potential

Transmembrane

1079 – 1099

Helical; Potential

Topological domain

1100 – 1109

Extracellular Potential

Transmembrane

1110 – 1130

Helical; Potential

Topological domain

1131 – 1151

Cytoplasmic Potential

Region

1131 – 1151

Required for endosomal targeting

Sites

Active site

503

4-aspartylphosphate intermediate Probable

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Modified residue

102

Phosphoserine Ref.5 Ref.7

Modified residue

115

Phosphoserine Ref.7

Modified residue

551

Phosphoserine Ref.6 Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P40527 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: DC7225CC9577DBE6
Show »

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

« Hide

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. 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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.
[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]. Strain: ATCC 208353 / W303-1A.
[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 SER-102, MASS SPECTROMETRY. Strain: ADR376.
[6]	"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.
[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: 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. BK006942 Genomic DNA. Translation: DAA08499.1.
PIR	S48431.
RefSeq	NP_012216.1. NM_001179398.1.
3D structure databases
ProteinModelPortal	P40527.
SMR	P40527. Positions 854-917.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2548N.
IntAct	P40527. 2 interactions.
MINT	MINT-422616.
STRING	P40527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL048W; YIL048W; YIL048W.
GeneID	854763.
KEGG	sce:YIL048W.
NMPDR	fig\|4932.3.peg.1747.
Organism-specific databases
CYGD	YIL048w.
SGD	S000001310. NEO1.
Phylogenomic databases
eggNOG	fuNOG05222.
GeneTree	EFGT00050000000755.
HOGENOM	HBG720821.
OMA	RRTCAIG.
OrthoDB	EOG49KJZN.
Gene expression databases
ArrayExpress	P40527.
Genevestigator	P40527.
GermOnline	YIL048W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01530.
Pfam	PF00122. E1-E2_ATPase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977511.

Entry information

Entry name

ATC7_YEAST

Accession

Primary (citable) accession number: P40527
Secondary accession number(s): D6VVN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IX

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents