Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vacuolar calcium ion transporter

Gene

VCX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • calcium:proton antiporter activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • potassium:proton antiporter activity Source: SGD

GO - Biological processi

  • calcium ion transport Source: SGD
  • cellular calcium ion homeostasis Source: SGD
  • transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29527-MONOMER.

Protein family/group databases

TCDBi2.A.19.2.2. the ca(2+):cation antiporter (caca) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar calcium ion transporter
Alternative name(s):
High copy number undoes manganese protein 1
Manganese resistance 1 protein
Vacuolar Ca(2+)/H(+) exchanger
Gene namesi
Name:VCX1
Synonyms:HUM1, MNR1
Ordered Locus Names:YDL128W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL128W.
SGDiS000002286. VCX1.

Subcellular locationi

  • Vacuole membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030CytoplasmicSequence analysisAdd
BLAST
Transmembranei31 – 5323HelicalSequence analysisAdd
BLAST
Topological domaini54 – 596VacuolarSequence analysis
Transmembranei60 – 8223HelicalSequence analysisAdd
BLAST
Topological domaini83 – 919CytoplasmicSequence analysis
Transmembranei92 – 11423HelicalSequence analysisAdd
BLAST
Topological domaini115 – 12612VacuolarSequence analysisAdd
BLAST
Transmembranei127 – 14620HelicalSequence analysisAdd
BLAST
Topological domaini147 – 16014CytoplasmicSequence analysisAdd
BLAST
Transmembranei161 – 18323HelicalSequence analysisAdd
BLAST
Topological domaini184 – 20320VacuolarSequence analysisAdd
BLAST
Transmembranei204 – 22623HelicalSequence analysisAdd
BLAST
Topological domaini227 – 25226CytoplasmicSequence analysisAdd
BLAST
Transmembranei253 – 27523HelicalSequence analysisAdd
BLAST
Topological domaini276 – 28712VacuolarSequence analysisAdd
BLAST
Transmembranei288 – 31023HelicalSequence analysisAdd
BLAST
Topological domaini311 – 3199CytoplasmicSequence analysis
Transmembranei320 – 34223HelicalSequence analysisAdd
BLAST
Topological domaini343 – 3486VacuolarSequence analysis
Transmembranei349 – 37123HelicalSequence analysisAdd
BLAST
Topological domaini372 – 3809CytoplasmicSequence analysis
Transmembranei381 – 39818HelicalSequence analysisAdd
BLAST
Topological domaini399 – 41113VacuolarSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Vacuolar calcium ion transporterPRO_0000209504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99385.
PRIDEiQ99385.

PTM databases

iPTMnetiQ99385.

Interactioni

Protein-protein interaction databases

BioGridi31935. 25 interactions.
DIPiDIP-5039N.
MINTiMINT-523645.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3612Combined sources
Helixi41 – 455Combined sources
Helixi46 – 5611Combined sources
Helixi60 – 8728Combined sources
Helixi91 – 10010Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 11411Combined sources
Turni115 – 1173Combined sources
Helixi119 – 13416Combined sources
Helixi136 – 14611Combined sources
Helixi158 – 18124Combined sources
Helixi193 – 21927Combined sources
Turni220 – 2223Combined sources
Helixi223 – 24119Combined sources
Helixi250 – 27324Combined sources
Helixi275 – 2817Combined sources
Helixi286 – 2927Combined sources
Helixi294 – 31118Combined sources
Helixi315 – 33117Combined sources
Helixi333 – 34311Combined sources
Helixi354 – 37320Combined sources
Helixi378 – 39619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K1CX-ray2.30A/B1-411[»]
ProteinModelPortaliQ99385.
SMRiQ99385. Positions 22-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000083011.
InParanoidiQ99385.
KOiK07300.
OMAiREPNERD.
OrthoDBiEOG76HQ97.

Family and domain databases

InterProiIPR004713. CaH_exchang.
IPR004798. CAX.
IPR004837. NaCa_Exmemb.
IPR030177. Vcx1.
[Graphical view]
PANTHERiPTHR31503:SF5. PTHR31503:SF5. 1 hit.
PfamiPF01699. Na_Ca_ex. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00846. caca2. 1 hit.
TIGR00378. cax. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDATTPLLTV ANSHPARNPK HTAWRAAVYD LQYILKASPL NFLLVFVPLG
60 70 80 90 100
LIWGHFQLSH TLTFLFNFLA IIPLAAILAN ATEELADKAG NTIGGLLNAT
110 120 130 140 150
FGNAVELIVS IIALKKGQVR IVQASMLGSL LSNLLLVLGL CFIFGGYNRV
160 170 180 190 200
QQTFNQTAAQ TMSSLLAIAC ASLLIPAAFR ATLPHGKEDH FIDGKILELS
210 220 230 240 250
RGTSIVILIV YVLFLYFQLG SHHALFEQQE EETDEVMSTI SRNPHHSLSV
260 270 280 290 300
KSSLVILLGT TVIISFCADF LVGTIDNVVE STGLSKTFIG LIVIPIVGNA
310 320 330 340 350
AEHVTSVLVA MKDKMDLALG VAIGSSLQVA LFVTPFMVLV GWMIDVPMTL
360 370 380 390 400
NFSTFETATL FIAVFLSNYL ILDGESNWLE GVMSLAMYIL IAMAFFYYPD
410
EKTLDSIGNS L
Length:411
Mass (Da):44,646
Last modified:November 1, 1996 - v1
Checksum:i4A946818A02E8078
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti204 – 2041S → A in manganese-resistant mutant 2.
Natural varianti208 – 2081L → P in manganese-resistant mutant 1.
Natural varianti383 – 3831M → I in VCX1-D1. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18944 Genomic DNA. Translation: AAC49550.1.
U36603 Genomic DNA. Translation: AAB60313.1.
AJ001272 Genomic DNA. Translation: CAA04645.1.
AJ001273 Genomic DNA. Translation: CAA04646.1.
Z74176 Genomic DNA. Translation: CAA98696.1.
BK006938 Genomic DNA. Translation: DAA11732.1.
PIRiS61933.
RefSeqiNP_010155.1. NM_001180187.1.

Genome annotation databases

EnsemblFungiiYDL128W; YDL128W; YDL128W.
GeneIDi851429.
KEGGisce:YDL128W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18944 Genomic DNA. Translation: AAC49550.1.
U36603 Genomic DNA. Translation: AAB60313.1.
AJ001272 Genomic DNA. Translation: CAA04645.1.
AJ001273 Genomic DNA. Translation: CAA04646.1.
Z74176 Genomic DNA. Translation: CAA98696.1.
BK006938 Genomic DNA. Translation: DAA11732.1.
PIRiS61933.
RefSeqiNP_010155.1. NM_001180187.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K1CX-ray2.30A/B1-411[»]
ProteinModelPortaliQ99385.
SMRiQ99385. Positions 22-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31935. 25 interactions.
DIPiDIP-5039N.
MINTiMINT-523645.

Protein family/group databases

TCDBi2.A.19.2.2. the ca(2+):cation antiporter (caca) family.

PTM databases

iPTMnetiQ99385.

Proteomic databases

MaxQBiQ99385.
PRIDEiQ99385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL128W; YDL128W; YDL128W.
GeneIDi851429.
KEGGisce:YDL128W.

Organism-specific databases

EuPathDBiFungiDB:YDL128W.
SGDiS000002286. VCX1.

Phylogenomic databases

HOGENOMiHOG000083011.
InParanoidiQ99385.
KOiK07300.
OMAiREPNERD.
OrthoDBiEOG76HQ97.

Enzyme and pathway databases

BioCyciYEAST:G3O-29527-MONOMER.

Miscellaneous databases

PROiQ99385.

Family and domain databases

InterProiIPR004713. CaH_exchang.
IPR004798. CAX.
IPR004837. NaCa_Exmemb.
IPR030177. Vcx1.
[Graphical view]
PANTHERiPTHR31503:SF5. PTHR31503:SF5. 1 hit.
PfamiPF01699. Na_Ca_ex. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00846. caca2. 1 hit.
TIGR00378. cax. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The product of HUM1, a novel yeast gene, is required for vacuolar Ca2+/H+ exchange and is related to mammalian Na+/Ca2+ exchangers."
    Pozos T.C., Sekler I., Cyert M.S.
    Mol. Cell. Biol. 16:3730-3741(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: S288c / YPH1.
  2. "Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+ ATPases in Saccharomyces cerevisiae."
    Cunningham K.W., Fink G.R.
    Mol. Cell. Biol. 16:2226-2237(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANT VCX1-D1 ILE-383.
  3. "A single nucleotide change in the MNR1 (VCX1/HUM1) gene determines resistance to Manganese in Saccharomyces cerevisae."
    Del Pozo L., Osaba L., Corchero J., Jimenez A.
    Yeast 15:371-375(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS MANGANESE-RESISTANT.
    Strain: ATCC 201238 / W303-1B.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    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.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVCX1_YEAST
AccessioniPrimary (citable) accession number: Q99385
Secondary accession number(s): D6VRM2, O13580, O13581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7770 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.