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Protein

Vacuolar cation-transporting ATPase YPK9

Gene

YPK9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Vacuolar transporter which plays a role in sequestration of divalent heavy metal ions.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei781 – 78114-aspartylphosphate intermediateBy similarity
Metal bindingi1187 – 11871MagnesiumBy similarity
Metal bindingi1191 – 11911MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33776-MONOMER.
ReactomeiR-SCE-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.10.8. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar cation-transporting ATPase YPK9 (EC:3.6.3.-)
Alternative name(s):
PARK9 homolog
Gene namesi
Name:YPK9
Ordered Locus Names:YOR291W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR291W.
SGDiS000005817. YPK9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 293293CytoplasmicSequence analysisAdd
BLAST
Transmembranei294 – 31522HelicalSequence analysisAdd
BLAST
Topological domaini316 – 3216VacuolarSequence analysis
Transmembranei322 – 34423HelicalSequence analysisAdd
BLAST
Topological domaini345 – 488144CytoplasmicSequence analysisAdd
BLAST
Transmembranei489 – 51123HelicalSequence analysisAdd
BLAST
Topological domaini512 – 5143VacuolarSequence analysis
Transmembranei515 – 53319HelicalSequence analysisAdd
BLAST
Topological domaini534 – 693160CytoplasmicSequence analysisAdd
BLAST
Transmembranei694 – 71320HelicalSequence analysisAdd
BLAST
Topological domaini714 – 72613VacuolarSequence analysisAdd
BLAST
Transmembranei727 – 74822HelicalSequence analysisAdd
BLAST
Topological domaini749 – 1244496CytoplasmicSequence analysisAdd
BLAST
Transmembranei1245 – 126420HelicalSequence analysisAdd
BLAST
Topological domaini1265 – 12717VacuolarSequence analysis
Transmembranei1272 – 128918HelicalSequence analysisAdd
BLAST
Topological domaini1290 – 130718CytoplasmicSequence analysisAdd
BLAST
Transmembranei1308 – 133124HelicalSequence analysisAdd
BLAST
Topological domaini1332 – 135120VacuolarSequence analysisAdd
BLAST
Transmembranei1352 – 137423HelicalSequence analysisAdd
BLAST
Topological domaini1375 – 138713CytoplasmicSequence analysisAdd
BLAST
Transmembranei1388 – 140720HelicalSequence analysisAdd
BLAST
Topological domaini1408 – 142316VacuolarSequence analysisAdd
BLAST
Transmembranei1424 – 144623HelicalSequence analysisAdd
BLAST
Topological domaini1447 – 147226CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • vacuole-mitochondrion membrane contact site Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

Confers sensitivity for growth for cadmium, manganese, nickel or selenium.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14721472Vacuolar cation-transporting ATPase YPK9PRO_0000046351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei95 – 951PhosphothreonineCombined sources
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei1117 – 11171PhosphoserineCombined sources
Modified residuei1120 – 11201PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12697.

PTM databases

iPTMnetiQ12697.

Interactioni

Protein-protein interaction databases

BioGridi34679. 76 interactions.
MINTiMINT-4503690.

Structurei

3D structure databases

ProteinModelPortaliQ12697.
SMRiQ12697. Positions 512-793, 931-1302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000063001.
InParanoidiQ12697.
KOiK14951.
OMAiDERDYRE.
OrthoDBiEOG74R1ZZ.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIPSSNQIQ HGQRSERNRR MPRASFSSTA TTSTAATLTS AMVLDQNNSE
60 70 80 90 100
PYAGATFEAV PSSIVSFHHP HSFQSSNLPS PHSSGNLEQR GRRLTESEPL
110 120 130 140 150
VLSSAEQSRS SSRNPSHFRF FTQEQISNAE GASTLENTDY DMAWDATPAY
160 170 180 190 200
EQDRIYGTGL SSRRSSIRSF SRASSLSNAK SYGSFSKRGR SGSRAPQRLG
210 220 230 240 250
ENSDTGFVYH SATHSSSSLS RYTTRERIPI ELESQTDEIL EDESSTHSLE
260 270 280 290 300
SSDSRRSASE NNRGSFSGHD DVHNQHSEYL KPDYHEKFYP QYAPNLHYQR
310 320 330 340 350
FYIAEEDLVI GIAAYQTSKF WYIIYNLCCF LTFGLVYLLT RWLPHLKVKL
360 370 380 390 400
YGVKVPLAKA EWVVIENEFG EFVIQPIDRQ WYNRPLSTVL PFENYPNPSY
410 420 430 440 450
EPNDINLSHH HANEINPNVP ILITFEYRYI KFIYSPLDDL FKTNNNWIDP
460 470 480 490 500
DWVDLSTVSN GLTKGVQEDR ELAFGKNQIN LRMKTTSEIL FNEVLHPFYV
510 520 530 540 550
FQVFSIILWG IDEYYYYAAC IFLISVLSIF DSLNEQKKVS RNLAEMSHFH
560 570 580 590 600
CDVRVLRDKF WTTISSSELV PGDIYEVSDP NITILPCDSI LLSSDCIVNE
610 620 630 640 650
SMLTGESVPV SKFPATEETM YQLCDDFQST QISSFVSKSF LYNGTNIIRA
660 670 680 690 700
RIAPGQTAAL AMVVRTGFST TKGSLVRSMV FPKPTGFKFY RDSFKYIGFM
710 720 730 740 750
SLIAIFGFCV SCVQFIKLGL DKKTMILRAL DIITIVVPPA LPATLTIGTN
760 770 780 790 800
FALSRLKEKG IFCISPTRLN ISGKIDVMCF DKTGTLTEDG LDVLGVQISE
810 820 830 840 850
PNGVRGQKFG ELLSDIRQVF PKFSLNDCSS PLDFKSRNFF MSLLTCHSLR
860 870 880 890 900
SVDGNLLGDP LDFKMFQFTG WSFEEDFQKR AFHSLYEGRH EDDVFPENSE
910 920 930 940 950
IIPAVVHPDS NNRENTFTDN DPHNFLGVVR SFEFLSELRR MSVIVKTNND
960 970 980 990 1000
DVYWSFTKGA PEVISEICNK STLPADFEEV LRCYTHNGYR VIACAGKTLP
1010 1020 1030 1040 1050
KRTWLYSQKV SREEVESNLE FLGFIIFQNK LKKETSETLK SLQDANIRTI
1060 1070 1080 1090 1100
MCTGDNILTA ISVGREAGLI QCSRVYVPSI NDTPLHGEPV IVWRDVNEPD
1110 1120 1130 1140 1150
KILDTKTLKP VKLGNNSVES LRECNYTLAV SGDVFRLLFR DENEIPEEYL
1160 1170 1180 1190 1200
NEILLNSSIY ARMSPDEKHE LMIQLQKLDY TVGFCGDGAN DCGALKAADV
1210 1220 1230 1240 1250
GISLSEAEAS VAAPFTSKIF NISCVLDVIR EGRAALVTSF ACFQYMSLYS
1260 1270 1280 1290 1300
AIQFITITIL YSRGSNLGDF QFLYIDLLLI VPIAICMSWS KSYEKIDKKR
1310 1320 1330 1340 1350
PSANLVSPKI LVPLLISVFL VFLFQFIPWI IVQKMSWYIK PIVGGDDAVQ
1360 1370 1380 1390 1400
SSDNTVLFFV SNFQYILTAI VLSVGPPYRE PMSKNFEFIV DITVSIGASL
1410 1420 1430 1440 1450
LLMTLDTESY LGKMLQLTPI SNSFTMFIIV WVILNYYAQL YIPPSIKGWL
1460 1470
KKKKSSKKYK LLIQEEMKLK EV
Length:1,472
Mass (Da):166,750
Last modified:November 1, 1997 - v1
Checksum:i6738AC22E561A4A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75199 Genomic DNA. Translation: CAA99518.1.
BK006948 Genomic DNA. Translation: DAA11055.1.
PIRiS67195.
RefSeqiNP_014934.1. NM_001183710.1.

Genome annotation databases

EnsemblFungiiYOR291W; YOR291W; YOR291W.
GeneIDi854466.
KEGGisce:YOR291W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75199 Genomic DNA. Translation: CAA99518.1.
BK006948 Genomic DNA. Translation: DAA11055.1.
PIRiS67195.
RefSeqiNP_014934.1. NM_001183710.1.

3D structure databases

ProteinModelPortaliQ12697.
SMRiQ12697. Positions 512-793, 931-1302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34679. 76 interactions.
MINTiMINT-4503690.

Protein family/group databases

TCDBi3.A.3.10.8. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiQ12697.

Proteomic databases

MaxQBiQ12697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR291W; YOR291W; YOR291W.
GeneIDi854466.
KEGGisce:YOR291W.

Organism-specific databases

EuPathDBiFungiDB:YOR291W.
SGDiS000005817. YPK9.

Phylogenomic databases

GeneTreeiENSGT00530000063001.
InParanoidiQ12697.
KOiK14951.
OMAiDERDYRE.
OrthoDBiEOG74R1ZZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33776-MONOMER.
ReactomeiR-SCE-936837. Ion transport by P-type ATPases.

Miscellaneous databases

NextBioi976753.
PROiQ12697.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006544. P-type_TPase_V.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF12409. P5-ATPase. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  4. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION.
  5. "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 THR-95; SER-108; SER-1117 AND SER-1120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYPK9_YEAST
AccessioniPrimary (citable) accession number: Q12697
Secondary accession number(s): D6W2Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.