VHC1_YEAST
ID VHC1_YEAST Reviewed; 1120 AA.
AC P38329; D6VQN1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vacuolar cation-chloride cotransporter 1 {ECO:0000305|PubMed:23022132};
DE AltName: Full=Vacuolar homolog of CCC family protein 1 {ECO:0000303|PubMed:23022132};
GN Name=VHC1 {ECO:0000303|PubMed:23022132};
GN OrderedLocusNames=YBR235W {ECO:0000312|SGD:S000000439}; ORFNames=YBR1601;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 GENE FAMILY.
RX PubMed=8526903; DOI=10.1006/bbrc.1995.2757;
RA Andre B., Scherens B.;
RT "The yeast YBR235w gene encodes a homolog of the mammalian electroneutral
RT Na(+)-(K(+))-Cl(-) cotransporter family.";
RL Biochem. Biophys. Res. Commun. 217:150-153(1995).
RN [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-915 AND SER-918, AND
RP 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23022132; DOI=10.1016/j.bbamem.2012.09.019;
RA Petrezselyova S., Kinclova-Zimmermannova O., Sychrova H.;
RT "Vhc1, a novel transporter belonging to the family of electroneutral
RT cation-Cl(-) cotransporters, participates in the regulation of cation
RT content and morphology of Saccharomyces cerevisiae vacuoles.";
RL Biochim. Biophys. Acta 1828:623-631(2013).
CC -!- FUNCTION: Catalyzes the coordinated symport of chloride with potassium
CC ions across the vacuolar membrane. Involved in vacuolar osmoregulation.
CC {ECO:0000305|PubMed:23022132}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:23022132};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Affects vacuolar morphology and decreases
CC survival upon hyperosmotic stress. {ECO:0000269|PubMed:23022132}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; Z36104; CAA85198.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07351.1; -; Genomic_DNA.
DR PIR; S46111; S46111.
DR RefSeq; NP_009794.3; NM_001178583.3.
DR AlphaFoldDB; P38329; -.
DR SMR; P38329; -.
DR BioGRID; 32930; 80.
DR DIP; DIP-2969N; -.
DR MINT; P38329; -.
DR STRING; 4932.YBR235W; -.
DR CarbonylDB; P38329; -.
DR iPTMnet; P38329; -.
DR MaxQB; P38329; -.
DR PaxDb; P38329; -.
DR PRIDE; P38329; -.
DR EnsemblFungi; YBR235W_mRNA; YBR235W; YBR235W.
DR GeneID; 852537; -.
DR KEGG; sce:YBR235W; -.
DR SGD; S000000439; VHC1.
DR VEuPathDB; FungiDB:YBR235W; -.
DR eggNOG; KOG1288; Eukaryota.
DR GeneTree; ENSGT00940000171884; -.
DR HOGENOM; CLU_001883_4_0_1; -.
DR InParanoid; P38329; -.
DR OMA; NAGLYVT; -.
DR BioCyc; YEAST:G3O-29166-MON; -.
DR Reactome; R-SCE-426117; Cation-coupled Chloride cotransporters.
DR PRO; PR:P38329; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38329; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0031166; C:integral component of vacuolar membrane; IDA:SGD.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IMP:SGD.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0055075; P:potassium ion homeostasis; IGI:SGD.
DR GO; GO:0034486; P:vacuolar transmembrane transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF03522; SLC12; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium transport; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1120
FT /note="Vacuolar cation-chloride cotransporter 1"
FT /id="PRO_0000202520"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 63..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..85
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 86..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 146..166
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..193
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 194..214
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..283
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 284..304
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 318..338
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..360
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 361..381
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 394..414
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..430
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 431..451
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 463..482
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..487
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 488..506
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..1120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1120 AA; 123999 MW; 299C99C0CBC3E5CC CRC64;
MVSRFYQIPG THRPSSAISS SNESSSLLSA RRISQTYFNY QATPECQKVS SKYDPDNPNK
DKLGTYDGVF VPTALNVLSI LMFLRFGFIL GQLGIICTIG LLLLSYTINL LTTLSISAIS
TNGTVRGGGA YYMISRSLGP EFGGSIGLVF FLGQVFNAGM NAVGIIEPLL YNLGYSAQGE
PPAALGELLP RGHWHEFTYA TVILFLCFSV AFVGSQTVSR AGNILFLVLA ASIFSIPLSA
LIRSPFTEGG ISYTGPSWQT FHDNLLPHLT KGAAGSLLKG KETFNDLFGV FFPATAGIFA
GAGMSSELRK PSKSIPKGTL WGLLFTFICY AVVVFSMGCS IPRRSLYDEV QIIQTISSVQ
WVIFMGEMAT SLFSIIVGML GAAYVLEAIA KDNIIPGLEI FAHSPLYSLI FTWILTQLCL
FSDVNKIATF ITMTFLMTFV VMNLACFLLG ISSAPNFRPS FKYFNRYTTA IGALLSVVAM
LIVDGISASV LFLAMILLFL FIHYFSPPKS WGDVSQSLIY HQVRKYLLRL RQDNIKYWRP
QILLFVDNPR TSWNLIRFCN HLKKGGLYIL GHVAVTADFP KQLNELKTQQ KAWMKIRDMA
AIKAFVQVGT GPSLIWGIRN VFIGSGLGGM KPNITVVGFF DLESYRKHIP QSRSQNNLQK
QVEIKATVPR STCSDVKINV PLPTDECKNE TKVNVQQWVQ IVEDLSLMQS NIAIAHGFKN
LEIPNKRDSC FPKKTIDLYP IQMCGKVEAK GDQPAAITTN FDTYTLILQL AAILVTVPEW
KRTHSLRVIL FVEQEYHRTN ETQRMKKLLQ VLRIDAEVLV VSLDQFRVYN TIVKGDPIVF
DYVNSKLADN EWWKDLVEAR DTLKPKRRFS TIEPQTIAKQ FTQSRKYTSG VQKLGVSFTM
NTRMPTNRID TPCESEDSDL DTDLTSIRDA FSASTNISVG KDLTTKSKTG SDRTNLLVKN
LQSDVSTQSL RPVFSSNTLP RTRVVEDGTG EQPTLIPIAE PDLSNGNGTG SGIGNGNKLK
KPVLPELSPC CSKDSLVTAM QNLGFNDLPS TAQHLVLNDV MTQMSKSSDL IFSTLPVPAL
GTHEDHDASL QYVEDLDIWL EGLPPCMLIN SQTMTVTTAL
