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Protein

Endosomal/prevacuolar sodium/hydrogen exchanger

Gene

NHX1

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

Endosomal/prevacuolar electroneutral Na+/H+ exchanger which mediates intracellular sequestration of Na+ cations, regulates vacuolar pH and contributes to osmotolerance following sudden exposure to hyperosmotic media. Contributes also to the postdiauxic/stationary phase resistance to osmotic stress and allows for the continued growth of cells until the acquired osmotolerance response can occur. Involved in hygromycin resistance probably through its influence on the electrochemical proton gradient affecting secondarily the entrance of hygromycin. Mediates pH-dependent vesicle trafficking out of the endosome. Contributes to K+ sequestration and homeostasis.13 Publications

GO - Molecular functioni

  • potassium:proton antiporter activity Source: SGD
  • sodium:proton antiporter activity Source: SGD

GO - Biological processi

  • cellular monovalent inorganic cation homeostasis Source: SGD
  • potassium ion transmembrane transport Source: SGD
  • sodium ion transmembrane transport Source: SGD
  • vacuolar acidification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Potassium transport, Sodium transport, Transport

Keywords - Ligandi

Potassium, Sodium

Enzyme and pathway databases

BioCyciYEAST:G3O-29984-MONOMER.
ReactomeiR-SCE-425986. Sodium/Proton exchangers.

Protein family/group databases

TCDBi2.A.36.1.12. the monovalent cation:proton antiporter-1 (cpa1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Endosomal/prevacuolar sodium/hydrogen exchanger
Alternative name(s):
Endosomal/prevacuolar Na(+)/H(+) exchanger
Vacuolar protein sorting-associated protein 44
Gene namesi
Name:NHX1
Synonyms:NHA2, VPL27, VPS44
Ordered Locus Names:YDR456W
ORF Names:D9461.40
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR456W.
SGDiS000002864. NHX1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 61LumenalSequence analysisAdd BLAST40
Transmembranei62 – 82HelicalSequence analysisAdd BLAST21
Topological domaini83 – 85CytoplasmicSequence analysis3
Transmembranei86 – 106HelicalSequence analysisAdd BLAST21
Topological domaini107 – 117LumenalSequence analysisAdd BLAST11
Transmembranei118 – 138HelicalSequence analysisAdd BLAST21
Topological domaini139 – 152CytoplasmicSequence analysisAdd BLAST14
Transmembranei153 – 173HelicalSequence analysisAdd BLAST21
Topological domaini174 – 189LumenalSequence analysisAdd BLAST16
Transmembranei190 – 211HelicalSequence analysisAdd BLAST22
Topological domaini212 – 217CytoplasmicSequence analysis6
Transmembranei218 – 238HelicalSequence analysisAdd BLAST21
Topological domaini239 – 258LumenalSequence analysisAdd BLAST20
Transmembranei259 – 279HelicalSequence analysisAdd BLAST21
Topological domaini280 – 288CytoplasmicSequence analysis9
Transmembranei289 – 308HelicalSequence analysisAdd BLAST20
Topological domaini309 – 313LumenalSequence analysis5
Transmembranei314 – 333HelicalSequence analysisAdd BLAST20
Topological domaini334 – 344CytoplasmicSequence analysisAdd BLAST11
Transmembranei345 – 364HelicalSequence analysisAdd BLAST20
Topological domaini365 – 376CytoplasmicSequence analysisAdd BLAST12
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 431LumenalSequence analysisAdd BLAST34
Transmembranei432 – 452HelicalSequence analysisAdd BLAST21
Topological domaini453 – 457CytoplasmicSequence analysis5
Transmembranei458 – 478HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • early endosome Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • late endosome Source: SGD
  • late endosome membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi201D → N: Impairs protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi225E → Q: Impairs protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi230D → N: Impairs protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi355E → Q: Impairs partially resistance to osmotic stress and hygromycin. 1 Publication1
Mutagenesisi357F → A, L or I: Impairs resistance to osmotic stress and hygromycin, and blocks protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi357F → V: Impairs partially resistance to osmotic stress and hygromycin. 1 Publication1
Mutagenesisi361Y → A: Impairs resistance to osmotic stress and hygromycin, and blocks protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi365E → A: Impairs resistance to osmotic stress and hygromycin, and blocks protein-trafficking to the vacuole. 1 Publication1
Mutagenesisi369E → A: Impairs partially resistance to osmotic stress and hygromycin. 1 Publication1
Mutagenesisi376P → N: Impairs resistance to osmotic stress and hygromycin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000005238022 – 633Endosomal/prevacuolar sodium/hydrogen exchangerAdd BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi420N-linked (GlcNAc...)Sequence analysis1
Modified residuei490PhosphothreonineCombined sources1
Modified residuei494PhosphoserineCombined sources1
Modified residuei498PhosphothreonineCombined sources1
Modified residuei499PhosphoserineCombined sources1
Glycosylationi515N-linked (GlcNAc...)1 Publication1
Glycosylationi550N-linked (GlcNAc...)1 Publication1
Glycosylationi563N-linked (GlcNAc...)1 Publication1
Modified residuei569PhosphoserineCombined sources1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ04121.
PRIDEiQ04121.
TopDownProteomicsiQ04121.

PTM databases

iPTMnetiQ04121.

Interactioni

Subunit structurei

Interacts with CYP6.1 Publication

Protein-protein interaction databases

BioGridi32510. 167 interactors.
DIPiDIP-4145N.
IntActiQ04121. 16 interactors.
MINTiMINT-494386.

Structurei

3D structure databases

ProteinModelPortaliQ04121.
SMRiQ04121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi124 – 133Amiloride-binding10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi23 – 50Asp-richAdd BLAST28

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
InParanoidiQ04121.
KOiK12041.
OMAiFWHATDS.
OrthoDBiEOG092C1Y19.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 3 hits.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04121-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKVLLNIA FKVLLTTAKR AVDPDDDDEL LPSPDLPGSD DPIAGDPDVD
60 70 80 90 100
LNPVTEEMFS SWALFIMLLL LISALWSSYY LTQKRIRAVH ETVLSIFYGM
110 120 130 140 150
VIGLIIRMSP GHYIQDTVTF NSSYFFNVLL PPIILNSGYE LNQVNFFNNM
160 170 180 190 200
LSILIFAIPG TFISAVVIGI ILYIWTFLGL ESIDISFADA MSVGATLSAT
210 220 230 240 250
DPVTILSIFN AYKVDPKLYT IIFGESLLND AISIVMFETC QKFHGQPATF
260 270 280 290 300
SSVFEGAGLF LMTFSVSLLI GVLIGILVAL LLKHTHIRRY PQIESCLILL
310 320 330 340 350
IAYESYFFSN GCHMSGIVSL LFCGITLKHY AYYNMSRRSQ ITIKYIFQLL
360 370 380 390 400
ARLSENFIFI YLGLELFTEV ELVYKPLLII VAAISICVAR WCAVFPLSQF
410 420 430 440 450
VNWIYRVKTI RSMSGITGEN ISVPDEIPYN YQMMTFWAGL RGAVGVALAL
460 470 480 490 500
GIQGEYKFTL LATVLVVVVL TVIIFGGTTA GMLEVLNIKT GCISEEDTSD
510 520 530 540 550
DEFDIEAPRA INLLNGSSIQ TDLGPYSDNN SPDISIDQFA VSSNKNLPNN
560 570 580 590 600
ISTTGGNTFG GLNETENTSP NPARSSMDKR NLRDKLGTIF NSDSQWFQNF
610 620 630
DEQVLKPVFL DNVSPSLQDS ATQSPADFSS QNH
Length:633
Mass (Da):70,148
Last modified:November 1, 1996 - v1
Checksum:i9B771ABDE41CEB0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64861.1.
BK006938 Genomic DNA. Translation: DAA12290.1.
PIRiS69734.
RefSeqiNP_010744.3. NM_001180764.3.

Genome annotation databases

EnsemblFungiiYDR456W; YDR456W; YDR456W.
GeneIDi852066.
KEGGisce:YDR456W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64861.1.
BK006938 Genomic DNA. Translation: DAA12290.1.
PIRiS69734.
RefSeqiNP_010744.3. NM_001180764.3.

3D structure databases

ProteinModelPortaliQ04121.
SMRiQ04121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32510. 167 interactors.
DIPiDIP-4145N.
IntActiQ04121. 16 interactors.
MINTiMINT-494386.

Protein family/group databases

TCDBi2.A.36.1.12. the monovalent cation:proton antiporter-1 (cpa1) family.

PTM databases

iPTMnetiQ04121.

Proteomic databases

MaxQBiQ04121.
PRIDEiQ04121.
TopDownProteomicsiQ04121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR456W; YDR456W; YDR456W.
GeneIDi852066.
KEGGisce:YDR456W.

Organism-specific databases

EuPathDBiFungiDB:YDR456W.
SGDiS000002864. NHX1.

Phylogenomic databases

GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
InParanoidiQ04121.
KOiK12041.
OMAiFWHATDS.
OrthoDBiEOG092C1Y19.

Enzyme and pathway databases

BioCyciYEAST:G3O-29984-MONOMER.
ReactomeiR-SCE-425986. Sodium/Proton exchangers.

Miscellaneous databases

PROiQ04121.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 3 hits.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNHX1_YEAST
AccessioniPrimary (citable) accession number: Q04121
Secondary accession number(s): D6VT80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 151 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 521 molecules/cell in log phase SD medium.1 Publication

Caution

Numerous studies suggest that the C-terminal tail of the Na+/H+ exchangers assumes a cytosolic orientation and constitutes a regulatory region. This cytosolic localization is confirmed by phosphorylation analysis (PubMed:15665377 and PubMed:18407956). However, residues Asn-515, Asn-550 and Asn-563 have been shown to be glycosylated and localized at the lumenal side (PubMed:11036065). These contradictory results suggest an unusual topology of the C-terminal tail which may contain membrane spans formed by beta-sheets or even may switch from one side to the other of the membrane.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.