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Vacuolar calcium ion transporter (High copy number undoes manganese protein 1) (Manganese resistance 1 protein) (Vacuolar Ca(2 )/H( ) exchanger)

 VCX1_YEAST              Reviewed;         411 AA.
Q99385; D6VRM2; O13580; O13581;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 129.
RecName: Full=Vacuolar calcium ion transporter;
AltName: Full=High copy number undoes manganese protein 1;
AltName: Full=Manganese resistance 1 protein;
AltName: Full=Vacuolar Ca(2+)/H(+) exchanger;
Name=VCX1; Synonyms=HUM1, MNR1; OrderedLocusNames=YDL128W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=S288c / YPH1;
PubMed=8668190; DOI=10.1128/MCB.16.7.3730;
Pozos T.C., Sekler I., Cyert M.S.;
"The product of HUM1, a novel yeast gene, is required for vacuolar
Ca2+/H+ exchange and is related to mammalian Na+/Ca2+ exchangers.";
Mol. Cell. Biol. 16:3730-3741(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANT VCX1-D1
ILE-383.
PubMed=8628289; DOI=10.1128/MCB.16.5.2226;
Cunningham K.W., Fink G.R.;
"Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+
ATPases in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:2226-2237(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS MANGANESE-RESISTANT.
STRAIN=ATCC 201238 / W303-1B;
PubMed=10219995;
DOI=10.1002/(SICI)1097-0061(19990330)15:5<371::AID-YEA380>3.3.CO;2-G;
Del Pozo L., Osaba L., Corchero J., Jimenez A.;
"A single nucleotide change in the MNR1 (VCX1/HUM1) gene determines
resistance to Manganese in Saccharomyces cerevisae.";
Yeast 15:371-375(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Has a role in promoting intracellular calcium ion
sequestration via the exchange of calcium ions for hydrogen ions
across the vacuolar membrane. Involved also in manganese ion
homeostasis via its uptake into the vacuole.
{ECO:0000269|PubMed:8628289, ECO:0000269|PubMed:8668190}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:8668190}; Multi-pass membrane protein
{ECO:0000269|PubMed:8668190}.
-!- MISCELLANEOUS: Present with 7770 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC
2.A.19) family. {ECO:0000305}.
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EMBL; U18944; AAC49550.1; -; Genomic_DNA.
EMBL; U36603; AAB60313.1; -; Genomic_DNA.
EMBL; AJ001272; CAA04645.1; -; Genomic_DNA.
EMBL; AJ001273; CAA04646.1; -; Genomic_DNA.
EMBL; Z74176; CAA98696.1; -; Genomic_DNA.
EMBL; BK006938; DAA11732.1; -; Genomic_DNA.
PIR; S61933; S61933.
RefSeq; NP_010155.1; NM_001180187.1.
PDB; 4K1C; X-ray; 2.30 A; A/B=1-411.
PDBsum; 4K1C; -.
ProteinModelPortal; Q99385; -.
SMR; Q99385; -.
BioGrid; 31935; 40.
DIP; DIP-5039N; -.
IntAct; Q99385; 1.
STRING; 4932.YDL128W; -.
TCDB; 2.A.19.2.2; the ca(2+):cation antiporter (caca) family.
iPTMnet; Q99385; -.
MaxQB; Q99385; -.
PaxDb; Q99385; -.
PRIDE; Q99385; -.
EnsemblFungi; YDL128W_mRNA; YDL128W_mRNA; YDL128W.
GeneID; 851429; -.
KEGG; sce:YDL128W; -.
SGD; S000002286; VCX1.
GeneTree; ENSGT00390000016897; -.
HOGENOM; HOG000083011; -.
InParanoid; Q99385; -.
KO; K07300; -.
OMA; SNWLEGT; -.
OrthoDB; EOG092C2NQI; -.
BioCyc; YEAST:G3O-29527-MONOMER; -.
PRO; PR:Q99385; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015369; F:calcium:proton antiporter activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
GO; GO:0006816; P:calcium ion transport; IDA:SGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
GO; GO:0055085; P:transmembrane transport; IDA:SGD.
InterPro; IPR004713; CaH_exchang.
InterPro; IPR004798; CAX.
InterPro; IPR004837; NaCa_Exmemb.
Pfam; PF01699; Na_Ca_ex; 2.
TIGRFAMs; TIGR00846; caca2; 1.
TIGRFAMs; TIGR00378; cax; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Calcium transport;
Complete proteome; Ion transport; Manganese; Membrane; Metal-binding;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Vacuole.
CHAIN 1 411 Vacuolar calcium ion transporter.
/FTId=PRO_0000209504.
TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.
TRANSMEM 31 53 Helical. {ECO:0000255}.
TOPO_DOM 54 59 Vacuolar. {ECO:0000255}.
TRANSMEM 60 82 Helical. {ECO:0000255}.
TOPO_DOM 83 91 Cytoplasmic. {ECO:0000255}.
TRANSMEM 92 114 Helical. {ECO:0000255}.
TOPO_DOM 115 126 Vacuolar. {ECO:0000255}.
TRANSMEM 127 146 Helical. {ECO:0000255}.
TOPO_DOM 147 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 183 Helical. {ECO:0000255}.
TOPO_DOM 184 203 Vacuolar. {ECO:0000255}.
TRANSMEM 204 226 Helical. {ECO:0000255}.
TOPO_DOM 227 252 Cytoplasmic. {ECO:0000255}.
TRANSMEM 253 275 Helical. {ECO:0000255}.
TOPO_DOM 276 287 Vacuolar. {ECO:0000255}.
TRANSMEM 288 310 Helical. {ECO:0000255}.
TOPO_DOM 311 319 Cytoplasmic. {ECO:0000255}.
TRANSMEM 320 342 Helical. {ECO:0000255}.
TOPO_DOM 343 348 Vacuolar. {ECO:0000255}.
TRANSMEM 349 371 Helical. {ECO:0000255}.
TOPO_DOM 372 380 Cytoplasmic. {ECO:0000255}.
TRANSMEM 381 398 Helical. {ECO:0000255}.
TOPO_DOM 399 411 Vacuolar. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:15665377}.
VARIANT 204 204 S -> A (in manganese-resistant mutant 2).
VARIANT 208 208 L -> P (in manganese-resistant mutant 1).
VARIANT 383 383 M -> I (in VCX1-D1).
{ECO:0000269|PubMed:8628289}.
HELIX 25 36 {ECO:0000244|PDB:4K1C}.
HELIX 41 45 {ECO:0000244|PDB:4K1C}.
HELIX 46 56 {ECO:0000244|PDB:4K1C}.
HELIX 60 87 {ECO:0000244|PDB:4K1C}.
HELIX 91 100 {ECO:0000244|PDB:4K1C}.
HELIX 101 103 {ECO:0000244|PDB:4K1C}.
HELIX 104 114 {ECO:0000244|PDB:4K1C}.
TURN 115 117 {ECO:0000244|PDB:4K1C}.
HELIX 119 134 {ECO:0000244|PDB:4K1C}.
HELIX 136 146 {ECO:0000244|PDB:4K1C}.
HELIX 158 181 {ECO:0000244|PDB:4K1C}.
HELIX 193 219 {ECO:0000244|PDB:4K1C}.
TURN 220 222 {ECO:0000244|PDB:4K1C}.
HELIX 223 241 {ECO:0000244|PDB:4K1C}.
HELIX 250 273 {ECO:0000244|PDB:4K1C}.
HELIX 275 281 {ECO:0000244|PDB:4K1C}.
HELIX 286 292 {ECO:0000244|PDB:4K1C}.
HELIX 294 311 {ECO:0000244|PDB:4K1C}.
HELIX 315 331 {ECO:0000244|PDB:4K1C}.
HELIX 333 343 {ECO:0000244|PDB:4K1C}.
HELIX 354 373 {ECO:0000244|PDB:4K1C}.
HELIX 378 396 {ECO:0000244|PDB:4K1C}.
SEQUENCE 411 AA; 44646 MW; 4A946818A02E8078 CRC64;
MDATTPLLTV ANSHPARNPK HTAWRAAVYD LQYILKASPL NFLLVFVPLG LIWGHFQLSH
TLTFLFNFLA IIPLAAILAN ATEELADKAG NTIGGLLNAT FGNAVELIVS IIALKKGQVR
IVQASMLGSL LSNLLLVLGL CFIFGGYNRV QQTFNQTAAQ TMSSLLAIAC ASLLIPAAFR
ATLPHGKEDH FIDGKILELS RGTSIVILIV YVLFLYFQLG SHHALFEQQE EETDEVMSTI
SRNPHHSLSV KSSLVILLGT TVIISFCADF LVGTIDNVVE STGLSKTFIG LIVIPIVGNA
AEHVTSVLVA MKDKMDLALG VAIGSSLQVA LFVTPFMVLV GWMIDVPMTL NFSTFETATL
FIAVFLSNYL ILDGESNWLE GVMSLAMYIL IAMAFFYYPD EKTLDSIGNS L


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