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Q12697 (YPK9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar cation-transporting ATPase YPK9
EC=3.6.3.-
Alternative name(s):
PARK9 homolog;
Gene names
Name:YPK9
Ordered Locus Names:YOR291W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vacuolar transporter which plays a role in sequestration of divalent heavy metal ions. Ref.5

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Vacuole membrane; Multi-pass membrane protein Ref.5.

Disruption phenotype

Confers sensitivity for growth for cadmium, manganese, nickel or selenium. Ref.5

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14721472Vacuolar cation-transporting ATPase YPK9
PRO_0000046351

Regions

Topological domain1 – 293293Cytoplasmic Potential
Transmembrane294 – 31522Helical; Potential
Topological domain316 – 3216Vacuolar Potential
Transmembrane322 – 34423Helical; Potential
Topological domain345 – 488144Cytoplasmic Potential
Transmembrane489 – 51123Helical; Potential
Topological domain512 – 5143Vacuolar Potential
Transmembrane515 – 53319Helical; Potential
Topological domain534 – 693160Cytoplasmic Potential
Transmembrane694 – 71320Helical; Potential
Topological domain714 – 72613Vacuolar Potential
Transmembrane727 – 74822Helical; Potential
Topological domain749 – 1244496Cytoplasmic Potential
Transmembrane1245 – 126420Helical; Potential
Topological domain1265 – 12717Vacuolar Potential
Transmembrane1272 – 128918Helical; Potential
Topological domain1290 – 130718Cytoplasmic Potential
Transmembrane1308 – 133124Helical; Potential
Topological domain1332 – 135120Vacuolar Potential
Transmembrane1352 – 137423Helical; Potential
Topological domain1375 – 138713Cytoplasmic Potential
Transmembrane1388 – 140720Helical; Potential
Topological domain1408 – 142316Vacuolar Potential
Transmembrane1424 – 144623Helical; Potential
Topological domain1447 – 147226Cytoplasmic Potential

Sites

Active site78114-aspartylphosphate intermediate By similarity
Metal binding11871Magnesium By similarity
Metal binding11911Magnesium By similarity

Amino acid modifications

Modified residue951Phosphothreonine Ref.3
Modified residue2181Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q12697 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 6738AC22E561A4A9

FASTA1,472166,750
        10         20         30         40         50         60 
MDIPSSNQIQ HGQRSERNRR MPRASFSSTA TTSTAATLTS AMVLDQNNSE PYAGATFEAV 

        70         80         90        100        110        120 
PSSIVSFHHP HSFQSSNLPS PHSSGNLEQR GRRLTESEPL VLSSAEQSRS SSRNPSHFRF 

       130        140        150        160        170        180 
FTQEQISNAE GASTLENTDY DMAWDATPAY EQDRIYGTGL SSRRSSIRSF SRASSLSNAK 

       190        200        210        220        230        240 
SYGSFSKRGR SGSRAPQRLG ENSDTGFVYH SATHSSSSLS RYTTRERIPI ELESQTDEIL 

       250        260        270        280        290        300 
EDESSTHSLE SSDSRRSASE NNRGSFSGHD DVHNQHSEYL KPDYHEKFYP QYAPNLHYQR 

       310        320        330        340        350        360 
FYIAEEDLVI GIAAYQTSKF WYIIYNLCCF LTFGLVYLLT RWLPHLKVKL YGVKVPLAKA 

       370        380        390        400        410        420 
EWVVIENEFG EFVIQPIDRQ WYNRPLSTVL PFENYPNPSY EPNDINLSHH HANEINPNVP 

       430        440        450        460        470        480 
ILITFEYRYI KFIYSPLDDL FKTNNNWIDP DWVDLSTVSN GLTKGVQEDR ELAFGKNQIN 

       490        500        510        520        530        540 
LRMKTTSEIL FNEVLHPFYV FQVFSIILWG IDEYYYYAAC IFLISVLSIF DSLNEQKKVS 

       550        560        570        580        590        600 
RNLAEMSHFH CDVRVLRDKF WTTISSSELV PGDIYEVSDP NITILPCDSI LLSSDCIVNE 

       610        620        630        640        650        660 
SMLTGESVPV SKFPATEETM YQLCDDFQST QISSFVSKSF LYNGTNIIRA RIAPGQTAAL 

       670        680        690        700        710        720 
AMVVRTGFST TKGSLVRSMV FPKPTGFKFY RDSFKYIGFM SLIAIFGFCV SCVQFIKLGL 

       730        740        750        760        770        780 
DKKTMILRAL DIITIVVPPA LPATLTIGTN FALSRLKEKG IFCISPTRLN ISGKIDVMCF 

       790        800        810        820        830        840 
DKTGTLTEDG LDVLGVQISE PNGVRGQKFG ELLSDIRQVF PKFSLNDCSS PLDFKSRNFF 

       850        860        870        880        890        900 
MSLLTCHSLR SVDGNLLGDP LDFKMFQFTG WSFEEDFQKR AFHSLYEGRH EDDVFPENSE 

       910        920        930        940        950        960 
IIPAVVHPDS NNRENTFTDN DPHNFLGVVR SFEFLSELRR MSVIVKTNND DVYWSFTKGA 

       970        980        990       1000       1010       1020 
PEVISEICNK STLPADFEEV LRCYTHNGYR VIACAGKTLP KRTWLYSQKV SREEVESNLE 

      1030       1040       1050       1060       1070       1080 
FLGFIIFQNK LKKETSETLK SLQDANIRTI MCTGDNILTA ISVGREAGLI QCSRVYVPSI 

      1090       1100       1110       1120       1130       1140 
NDTPLHGEPV IVWRDVNEPD KILDTKTLKP VKLGNNSVES LRECNYTLAV SGDVFRLLFR 

      1150       1160       1170       1180       1190       1200 
DENEIPEEYL NEILLNSSIY ARMSPDEKHE LMIQLQKLDY TVGFCGDGAN DCGALKAADV 

      1210       1220       1230       1240       1250       1260 
GISLSEAEAS VAAPFTSKIF NISCVLDVIR EGRAALVTSF ACFQYMSLYS AIQFITITIL 

      1270       1280       1290       1300       1310       1320 
YSRGSNLGDF QFLYIDLLLI VPIAICMSWS KSYEKIDKKR PSANLVSPKI LVPLLISVFL 

      1330       1340       1350       1360       1370       1380 
VFLFQFIPWI IVQKMSWYIK PIVGGDDAVQ SSDNTVLFFV SNFQYILTAI VLSVGPPYRE 

      1390       1400       1410       1420       1430       1440 
PMSKNFEFIV DITVSIGASL LLMTLDTESY LGKMLQLTPI SNSFTMFIIV WVILNYYAQL 

      1450       1460       1470 
YIPPSIKGWL KKKKSSKKYK LLIQEEMKLK EV

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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-95, MASS SPECTROMETRY.
Strain: ADR376.
[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-218, MASS SPECTROMETRY.
[5]"Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2."
Schmidt K., Wolfe D.M., Stiller B., Pearce D.A.
Biochem. Biophys. Res. Commun. 383:198-202(2009) [PubMed: 19345671] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z75199 Genomic DNA. Translation: CAA99518.1.
BK006948 Genomic DNA. Translation: DAA11055.1.
PIRS67195.
RefSeqNP_014934.1. NM_001183710.1.

3D structure databases

ProteinModelPortalQ12697.
SMRQ12697. Positions 924-1029, 1167-1211.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12697.

Protein family/group databases

TCDB3.A.3.14.1. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR291W; YOR291W; YOR291W.
GeneID854466.
KEGGsce:YOR291W.
NMPDRfig|4932.3.peg.6046.

Organism-specific databases

CYGDYOR291w.
SGDS000005817. YPK9.

Phylogenomic databases

eggNOGfuNOG05761.
GeneTreeEFGT00050000000742.
HOGENOMHBG735026.
OMALIIAFTM.
OrthoDBEOG4SBJ60.

Gene expression databases

ArrayExpressQ12697.
GenevestigatorQ12697.
GermOnlineYOR291W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR023306. 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.
IPR006544. ATPase_P-typ_unknown-pump-sp.
IPR023214. HAD-like_dom.
IPR000150. Hypothet_cof.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK14951.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976753.

Entry information

Entry nameYPK9_YEAST
AccessionPrimary (citable) accession number: Q12697
Secondary accession number(s): D6W2Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents