YPK9_YEAST
ID YPK9_YEAST Reviewed; 1472 AA.
AC Q12697; D6W2Y9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Vacuolar cation-transporting ATPase YPK9;
DE EC=7.2.2.-;
DE AltName: Full=PARK9 homolog;
GN Name=YPK9; OrderedLocusNames=YOR291W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [4]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19345671; DOI=10.1016/j.bbrc.2009.03.151;
RA Schmidt K., Wolfe D.M., Stiller B., Pearce D.A.;
RT "Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking
RT YPK9p the orthologue of human ATP13A2.";
RL Biochem. Biophys. Res. Commun. 383:198-202(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-108; SER-1117 AND
RP SER-1120, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24603074; DOI=10.1093/hmg/ddu099;
RA Kong S.M., Chan B.K., Park J.S., Hill K.J., Aitken J.B., Cottle L.,
RA Farghaian H., Cole A.R., Lay P.A., Sue C.M., Cooper A.A.;
RT "Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis
RT and promotes alpha-Synuclein externalization via exosomes.";
RL Hum. Mol. Genet. 23:2816-2833(2014).
CC -!- FUNCTION: Vacuolar transporter which plays a role in sequestration of
CC divalent heavy metal ions. {ECO:0000269|PubMed:19345671,
CC ECO:0000269|PubMed:24603074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19345671};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19345671}.
CC -!- DISRUPTION PHENOTYPE: Confers sensitivity for growth for cadmium,
CC manganese, nickel, selenium and iron. {ECO:0000269|PubMed:19345671,
CC ECO:0000269|PubMed:24603074}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
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DR EMBL; Z75199; CAA99518.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11055.1; -; Genomic_DNA.
DR PIR; S67195; S67195.
DR RefSeq; NP_014934.1; NM_001183710.1.
DR AlphaFoldDB; Q12697; -.
DR SMR; Q12697; -.
DR BioGRID; 34679; 141.
DR STRING; 4932.YOR291W; -.
DR TCDB; 3.A.3.10.8; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q12697; -.
DR MaxQB; Q12697; -.
DR PaxDb; Q12697; -.
DR PRIDE; Q12697; -.
DR EnsemblFungi; YOR291W_mRNA; YOR291W; YOR291W.
DR GeneID; 854466; -.
DR KEGG; sce:YOR291W; -.
DR SGD; S000005817; YPK9.
DR VEuPathDB; FungiDB:YOR291W; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000168207; -.
DR HOGENOM; CLU_001828_1_0_1; -.
DR InParanoid; Q12697; -.
DR OMA; GFKFYED; -.
DR BioCyc; YEAST:G3O-33776-MON; -.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q12697; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12697; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1903135; F:cupric ion binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030145; F:manganese ion binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0015662; F:P-type ion transporter activity; ISS:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; ISS:SGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF12409; P5-ATPase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..1472
FT /note="Vacuolar cation-transporting ATPase YPK9"
FT /id="PRO_0000046351"
FT TOPO_DOM 1..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..321
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..514
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..726
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..1244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1265..1271
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1290..1307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1308..1331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1332..1351
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1352..1374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1375..1387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1388..1407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1408..1423
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1424..1446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1447..1472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1472 AA; 166750 MW; 6738AC22E561A4A9 CRC64;
MDIPSSNQIQ HGQRSERNRR MPRASFSSTA TTSTAATLTS AMVLDQNNSE PYAGATFEAV
PSSIVSFHHP HSFQSSNLPS PHSSGNLEQR GRRLTESEPL VLSSAEQSRS SSRNPSHFRF
FTQEQISNAE GASTLENTDY DMAWDATPAY EQDRIYGTGL SSRRSSIRSF SRASSLSNAK
SYGSFSKRGR SGSRAPQRLG ENSDTGFVYH SATHSSSSLS RYTTRERIPI ELESQTDEIL
EDESSTHSLE SSDSRRSASE NNRGSFSGHD DVHNQHSEYL KPDYHEKFYP QYAPNLHYQR
FYIAEEDLVI GIAAYQTSKF WYIIYNLCCF LTFGLVYLLT RWLPHLKVKL YGVKVPLAKA
EWVVIENEFG EFVIQPIDRQ WYNRPLSTVL PFENYPNPSY EPNDINLSHH HANEINPNVP
ILITFEYRYI KFIYSPLDDL FKTNNNWIDP DWVDLSTVSN GLTKGVQEDR ELAFGKNQIN
LRMKTTSEIL FNEVLHPFYV FQVFSIILWG IDEYYYYAAC IFLISVLSIF DSLNEQKKVS
RNLAEMSHFH CDVRVLRDKF WTTISSSELV PGDIYEVSDP NITILPCDSI LLSSDCIVNE
SMLTGESVPV SKFPATEETM YQLCDDFQST QISSFVSKSF LYNGTNIIRA RIAPGQTAAL
AMVVRTGFST TKGSLVRSMV FPKPTGFKFY RDSFKYIGFM SLIAIFGFCV SCVQFIKLGL
DKKTMILRAL DIITIVVPPA LPATLTIGTN FALSRLKEKG IFCISPTRLN ISGKIDVMCF
DKTGTLTEDG LDVLGVQISE PNGVRGQKFG ELLSDIRQVF PKFSLNDCSS PLDFKSRNFF
MSLLTCHSLR SVDGNLLGDP LDFKMFQFTG WSFEEDFQKR AFHSLYEGRH EDDVFPENSE
IIPAVVHPDS NNRENTFTDN DPHNFLGVVR SFEFLSELRR MSVIVKTNND DVYWSFTKGA
PEVISEICNK STLPADFEEV LRCYTHNGYR VIACAGKTLP KRTWLYSQKV SREEVESNLE
FLGFIIFQNK LKKETSETLK SLQDANIRTI MCTGDNILTA ISVGREAGLI QCSRVYVPSI
NDTPLHGEPV IVWRDVNEPD KILDTKTLKP VKLGNNSVES LRECNYTLAV SGDVFRLLFR
DENEIPEEYL NEILLNSSIY ARMSPDEKHE LMIQLQKLDY TVGFCGDGAN DCGALKAADV
GISLSEAEAS VAAPFTSKIF NISCVLDVIR EGRAALVTSF ACFQYMSLYS AIQFITITIL
YSRGSNLGDF QFLYIDLLLI VPIAICMSWS KSYEKIDKKR PSANLVSPKI LVPLLISVFL
VFLFQFIPWI IVQKMSWYIK PIVGGDDAVQ SSDNTVLFFV SNFQYILTAI VLSVGPPYRE
PMSKNFEFIV DITVSIGASL LLMTLDTESY LGKMLQLTPI SNSFTMFIIV WVILNYYAQL
YIPPSIKGWL KKKKSSKKYK LLIQEEMKLK EV
