VCX1_YEAST
ID VCX1_YEAST Reviewed; 411 AA.
AC Q99385; D6VRM2; O13580; O13581;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Vacuolar calcium ion transporter;
DE AltName: Full=High copy number undoes manganese protein 1;
DE AltName: Full=Manganese resistance 1 protein;
DE AltName: Full=Vacuolar Ca(2+)/H(+) exchanger;
GN Name=VCX1; Synonyms=HUM1, MNR1; OrderedLocusNames=YDL128W;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=S288c / YPH1;
RX PubMed=8668190; DOI=10.1128/mcb.16.7.3730;
RA Pozos T.C., Sekler I., Cyert M.S.;
RT "The product of HUM1, a novel yeast gene, is required for vacuolar Ca2+/H+
RT exchange and is related to mammalian Na+/Ca2+ exchangers.";
RL Mol. Cell. Biol. 16:3730-3741(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANT VCX1-D1 ILE-383.
RX PubMed=8628289; DOI=10.1128/mcb.16.5.2226;
RA Cunningham K.W., Fink G.R.;
RT "Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+
RT ATPases in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:2226-2237(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS MANGANESE-RESISTANT.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=10219995;
RX DOI=10.1002/(sici)1097-0061(19990330)15:5<371::aid-yea380>3.3.co;2-g;
RA Del Pozo L., Osaba L., Corchero J., Jimenez A.;
RT "A single nucleotide change in the MNR1 (VCX1/HUM1) gene determines
RT resistance to Manganese in Saccharomyces cerevisae.";
RL Yeast 15:371-375(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-13, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
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 [9]
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).
CC -!- FUNCTION: Has a role in promoting intracellular calcium ion
CC sequestration via the exchange of calcium ions for hydrogen ions across
CC the vacuolar membrane. Involved also in manganese ion homeostasis via
CC its uptake into the vacuole. {ECO:0000269|PubMed:8628289,
CC ECO:0000269|PubMed:8668190}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:8668190};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8668190}.
CC -!- MISCELLANEOUS: Present with 7770 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; U18944; AAC49550.1; -; Genomic_DNA.
DR EMBL; U36603; AAB60313.1; -; Genomic_DNA.
DR EMBL; AJ001272; CAA04645.1; -; Genomic_DNA.
DR EMBL; AJ001273; CAA04646.1; -; Genomic_DNA.
DR EMBL; Z74176; CAA98696.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11732.1; -; Genomic_DNA.
DR PIR; S61933; S61933.
DR RefSeq; NP_010155.1; NM_001180187.1.
DR PDB; 4K1C; X-ray; 2.30 A; A/B=1-411.
DR PDBsum; 4K1C; -.
DR AlphaFoldDB; Q99385; -.
DR SMR; Q99385; -.
DR BioGRID; 31935; 44.
DR DIP; DIP-5039N; -.
DR IntAct; Q99385; 1.
DR STRING; 4932.YDL128W; -.
DR TCDB; 2.A.19.2.2; the ca(2+):cation antiporter (caca) family.
DR iPTMnet; Q99385; -.
DR MaxQB; Q99385; -.
DR PaxDb; Q99385; -.
DR PRIDE; Q99385; -.
DR EnsemblFungi; YDL128W_mRNA; YDL128W; YDL128W.
DR GeneID; 851429; -.
DR KEGG; sce:YDL128W; -.
DR SGD; S000002286; VCX1.
DR VEuPathDB; FungiDB:YDL128W; -.
DR eggNOG; KOG1397; Eukaryota.
DR GeneTree; ENSGT00390000016897; -.
DR HOGENOM; CLU_008721_4_2_1; -.
DR InParanoid; Q99385; -.
DR OMA; AAVMITC; -.
DR BioCyc; YEAST:G3O-29527-MON; -.
DR PRO; PR:Q99385; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q99385; protein.
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:0015369; F:calcium:proton antiporter activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IMP:SGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:SGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR Gene3D; 1.20.1420.30; -; 1.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR004798; CAX-like.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR PANTHER; PTHR31503; PTHR31503; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00378; cax; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Calcium transport; Ion transport;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..411
FT /note="Vacuolar calcium ion transporter"
FT /id="PRO_0000209504"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..59
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 60..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..126
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..203
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..287
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..348
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 381..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..411
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:16847258"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT VARIANT 204
FT /note="S -> A (in manganese-resistant mutant 2)"
FT VARIANT 208
FT /note="L -> P (in manganese-resistant mutant 1)"
FT VARIANT 383
FT /note="M -> I (in VCX1-D1)"
FT /evidence="ECO:0000269|PubMed:8628289"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 60..87
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4K1C"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 158..181
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 193..219
FT /evidence="ECO:0007829|PDB:4K1C"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 223..241
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 250..273
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 315..331
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 354..373
FT /evidence="ECO:0007829|PDB:4K1C"
FT HELIX 378..396
FT /evidence="ECO:0007829|PDB:4K1C"
SQ 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
