Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40527 (ATC7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable phospholipid-transporting ATPase NEO1

EC=3.6.3.1
Gene names
Name:NEO1
Ordered Locus Names:YIL048W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1151 AA.
Sequence statusComplete.
Protein existenceEvidence 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(Side 1) = ADP + phosphate + phospholipid(Side 2).

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 processProtein transport
Transport
   Cellular componentEndosome
Golgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from mutant phenotype Ref.3. Source: SGD

ion transmembrane transport

Inferred from sequence or structural similarity PubMed 9224683. Source: GOC

phospholipid translocation

Inferred from sequence or structural similarity PubMed 12221123. Source: GOC

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

retrograde vesicle-mediated transport, Golgi to ER

Inferred from mutant phenotype PubMed 12960419. Source: SGD

vacuole organization

Inferred from mutant phenotype Ref.3. Source: SGD

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.3. Source: SGD

Golgi membrane

Inferred from direct assay PubMed 12960419. Source: SGD

endosome

Inferred from direct assay Ref.3. Source: SGD

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

Inferred from sequence or structural similarity PubMed 9224683. Source: SGD

cation-transporting ATPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid-translocating ATPase activity

Inferred from sequence or structural similarity PubMed 12221123. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11511151Probable phospholipid-transporting ATPase NEO1
PRO_0000046236

Regions

Topological domain1 – 184184Extracellular Potential
Transmembrane185 – 20521Helical; Potential
Topological domain206 – 2094Cytoplasmic Potential
Transmembrane210 – 23021Helical; Potential
Topological domain231 – 367137Extracellular Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 41628Cytoplasmic Potential
Transmembrane417 – 43721Helical; Potential
Topological domain4381Extracellular Potential
Transmembrane439 – 45921Helical; Potential
Topological domain460 – 947488Cytoplasmic Potential
Transmembrane948 – 96821Helical; Potential
Topological domain969 – 9702Extracellular Potential
Transmembrane971 – 99121Helical; Potential
Topological domain992 – 102029Cytoplasmic Potential
Transmembrane1021 – 104121Helical; Potential
Topological domain1042 – 105211Extracellular Potential
Transmembrane1053 – 107321Helical; Potential
Topological domain1074 – 10785Cytoplasmic Potential
Transmembrane1079 – 109921Helical; Potential
Topological domain1100 – 110910Extracellular Potential
Transmembrane1110 – 113021Helical; Potential
Topological domain1131 – 115121Cytoplasmic Potential
Region1131 – 115121Required for endosomal targeting

Sites

Active site50314-aspartylphosphate intermediate Probable

Amino acid modifications

Modified residue1021Phosphoserine Ref.5 Ref.6 Ref.7
Modified residue5511Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P40527 [UniParc].

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

FASTA1,151130,218
        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' 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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38060 Genomic DNA. Translation: CAA86174.1.
BK006942 Genomic DNA. Translation: DAA08499.1.
PIRS48431.
RefSeqNP_012216.1. NM_001179398.1.

3D structure databases

ProteinModelPortalP40527.
SMRP40527. Positions 265-917.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34942. 79 interactions.
DIPDIP-2548N.
IntActP40527. 6 interactions.
MINTMINT-422616.
STRING4932.YIL048W.

Proteomic databases

PaxDbP40527.
PRIDEP40527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL048W; YIL048W; YIL048W.
GeneID854763.
KEGGsce:YIL048W.

Organism-specific databases

CYGDYIL048w.
SGDS000001310. NEO1.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00550000074723.
HOGENOMHOG000201571.
KOK01530.
OMASYANEAM.
OrthoDBEOG7FR7QR.

Enzyme and pathway databases

BioCycYEAST:G3O-31319-MONOMER.

Gene expression databases

GenevestigatorP40527.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977511.
PROP40527.

Entry information

Entry nameATC7_YEAST
AccessionPrimary (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: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families