VNX1_YEAST
ID VNX1_YEAST Reviewed; 908 AA.
AC P42839; D6W0M5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Low affinity vacuolar monovalent cation/H(+) antiporter;
DE AltName: Full=Vacuolar Na(+)/H(+) exchanger;
GN Name=VNX1; OrderedLocusNames=YNL321W; ORFNames=N0339;
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 [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7502583; DOI=10.1002/yea.320111109;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT identifies six known genes, a new member of the hexose transporter family
RT and ten new open reading frames.";
RL Yeast 11:1077-1085(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=17588950; DOI=10.1074/jbc.m703116200;
RA Cagnac O., Leterrier M., Yeager M., Blumwald E.;
RT "Identification and characterization of Vnx1p, a novel type of vacuolar
RT monovalent cation/H+ antiporter of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:24284-24293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26 AND SER-110, AND
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-32; THR-33; SER-110;
RP THR-118 AND SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Has a role in promoting intracellular monovalent cation
CC sequestration via the exchange of monovalent cations and especially
CC Na(+) for hydrogen ions across the vacuolar membrane.
CC {ECO:0000269|PubMed:17588950}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 mM for Na(+) transport {ECO:0000269|PubMed:17588950};
CC KM=82.2 mM for K(+) transport {ECO:0000269|PubMed:17588950};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17588950};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17588950}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. {ECO:0000305}.
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DR EMBL; Z46259; CAA86376.1; -; Genomic_DNA.
DR EMBL; Z71597; CAA96252.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10241.1; -; Genomic_DNA.
DR PIR; S51293; S51293.
DR RefSeq; NP_014078.1; NM_001183159.1.
DR AlphaFoldDB; P42839; -.
DR SMR; P42839; -.
DR BioGRID; 35519; 59.
DR DIP; DIP-4268N; -.
DR STRING; 4932.YNL321W; -.
DR TCDB; 2.A.19.7.1; the ca(2+):cation antiporter (caca) family.
DR iPTMnet; P42839; -.
DR MaxQB; P42839; -.
DR PaxDb; P42839; -.
DR PRIDE; P42839; -.
DR EnsemblFungi; YNL321W_mRNA; YNL321W; YNL321W.
DR GeneID; 855395; -.
DR KEGG; sce:YNL321W; -.
DR SGD; S000005265; VNX1.
DR VEuPathDB; FungiDB:YNL321W; -.
DR eggNOG; KOG1397; Eukaryota.
DR GeneTree; ENSGT00390000016897; -.
DR HOGENOM; CLU_001583_0_0_1; -.
DR InParanoid; P42839; -.
DR OMA; YQIYGSH; -.
DR BioCyc; YEAST:G3O-33306-MON; -.
DR SABIO-RK; P42839; -.
DR PRO; PR:P42839; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42839; protein.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
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:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IMP:SGD.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IMP:SGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:SGD.
DR GO; GO:0006814; P:sodium ion transport; IMP:SGD.
DR Gene3D; 1.20.1420.30; -; 1.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR005185; YccF.
DR PANTHER; PTHR31503; PTHR31503; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR Pfam; PF03733; YccF; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..908
FT /note="Low affinity vacuolar monovalent cation/H(+)
FT antiporter"
FT /id="PRO_0000209505"
FT TOPO_DOM 1..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..408
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..530
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..587
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..686
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..783
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..851
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 907..908
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 908 AA; 102499 MW; 180E0EEC77DC111E CRC64;
MAKNNHISAS GNSTSGDHRL KEEVLTPTTS ASTPHRIFSV DDDPKEIQND IRYLEGLHEG
LKFALHANKS KRSVSSQSPI VHSSNNTLHH HEHQQHLPPT LESLSSKSHS VPDLNTATPS
SPKRMHSSIR ELPHDDNDDE DANDDSRFII HDSHGHDLLI DEINCQSPSH LENNDQASNA
SSTESFTLRE RQDAINETHP FGIRIWKPAL YKKHRSVQRT AAQDIHETQL KTITWEVTCS
NVLWFILFGF PIAILFYSAA IVVFLLGGGG LVTNSAKEYS KCLYKLANYF LWPFGKMVYL
LQDEQYLQED KDEGISMQQF YNWVTSYSNR LVFHQSQAKF QQREDHPAPA TESSSLMPPA
NTTATPLNSN HPSYNSIRHE IPHAAAQRRY FGRGKWSWGR VLFYTIFHLV LQPILAVLSL
CLWLLVFTIP MSNVLWQIMY HCRRHPLALG FKYVENSSQS HENEITQQQL NKNILLCTFR
AAGWHYYKYT VDGTNVIVVN LISIVFFTIF DFYVLKNFLH WKTWFTYESS IFILCLTSTI
PLAFYIGQAV ASISAQTSMG VGAVINAFFS TIVEIFLYCV ALQQKKGLLV EGSMIGSILG
AVLLLPGLSM CGGALNRKTQ RYNPASAGVS SALLIFSMIV MFVPTVLYEI YGGYSVNCAD
GANDRDCTFS HPPLKFNRLF THVIQPMSIS CAIVLFCAYI IGLWFTLRTH AKMIWQLPIA
DPTSTAPEQQ EQNSHDAPNW SRSKSTCILL MSTLLYAIIA EILVSCVDAV LEDIPSLNPK
FLGLTIFALI PNTTEFLNAI SFAIHGNVAL SMEIGSAYAL QVCLLQIPSL VIYSIFYTWN
VKKSMINIRT QMFPLVFPRW DIFGAMTSVF MFTYLYAEGK SNYFKGSMLI LLYIIIVVGF
YFQGALSE
