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2.A.36.1.12
Na+:H+ antiporter, NHX1; (vacuolar/endosomal Na+ tolerance protein).  Plays roles in ion homeostasis and vesicle trafficing (Mukherjee et al. 2006). The structures and functions of these NHX homologues have been reviewed (Dutta and Fliegel 2018).

Accession Number:Q04121
Protein Name:Endosomal/prevacuolar sodium/hydrogen exchanger
Length:633
Molecular Weight:70148.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Endosome membrane1 / Multi-pass membrane protein2
Substrate Na+, H+

Cross database links:

Genevestigator: Q04121 Q04121
eggNOG: fuNOG04144 fuNOG04144
HEGENOM: HBG734847 HBG734847
DIP: DIP-4145N DIP-4145N
Entrez Gene ID: 852066   
Pfam: PF00999   

Gene Ontology

GO:0000329 C:fungal-type vacuole membrane
GO:0016021 C:integral to membrane
GO:0031902 C:late endosome membrane
GO:0015385 F:sodium:hydrogen antiporter activity
GO:0006813 P:potassium ion transport
GO:0007035 P:vacuolar acidification

References (20)

[1] “Identification of a mitochondrial Na+/H+ exchanger.”  Numata M.et.al.   9507001
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.”  Jacq C.et.al.   9169867
[3] “Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants.”  Raymond C.K.et.al.   1493335
[4] “Intracellular sequestration of sodium by a novel Na+/H+ exchanger in yeast is enhanced by mutations in the plasma membrane H+-ATPase. Insights into mechanisms of sodium tolerance.”  Nass R.et.al.   9334180
[5] “Novel localization of a Na+/H+ exchanger in a late endosomal compartment of yeast. Implications for vacuole biogenesis.”  Nass R.et.al.   9694857
[6] “The yeast endosomal Na+/H+ exchanger, Nhx1, confers osmotolerance following acute hypertonic shock.”  Nass R.et.al.   10589731
[7] “Arabidopsis thaliana and Saccharomyces cerevisiae NHX1 genes encode amiloride sensitive electroneutral Na(+)/H(+) exchangers.”  Darley C.P.et.al.   10998367
[8] “The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae.”  Bowers K.et.al.   11102523
[9] “The yeast Na+/H+ exchanger Nhx1 is an N-linked glycoprotein. Topological implications.”  Wells K.M.et.al.   11036065
[10] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[11] “Inhibition of sodium/proton exchange by a Rab-GTPase-activating protein regulates endosomal traffic in yeast.”  Ali R.et.al.   14610088
[12] “The yeast endosomal Na+K+/H+ exchanger Nhx1 regulates cellular pH to control vesicle trafficking.”  Brett C.L.et.al.   15635088
[13] “Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.”  Gruhler A.et.al.   15665377
[14] “Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants.”  Maresova L.et.al.   15659172
[15] “Mutational analysis of the intramembranous H10 loop of yeast Nhx1 reveals a critical role in ion homoeostasis and vesicle trafficking.”  Mukherjee S.et.al.   16671892
[16] “Prevacuolar compartment morphology in vps mutants of Saccharomyces cerevisiae.”  Hedman J.M.et.al.   17543551
[17] “Identification and characterization of Vnx1p, a novel type of vacuolar monovalent cation/H+ antiporter of Saccharomyces cerevisiae.”  Cagnac O.et.al.   17588950
[18] “Chloride homeostasis in Saccharomyces cerevisiae: high affinity influx, V-ATPase-dependent sequestration, and identification of a candidate Cl-sensor.”  Jennings M.L.et.al.   18378800
[19] “Cardiolipin mediates cross-talk between mitochondria and the vacuole.”  Chen S.et.al.   18799619
[20] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
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  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MLSKVLLNIA FKVLLTTAKR AVDPDDDDEL LPSPDLPGSD DPIAGDPDVD LNPVTEEMFS 
61:	SWALFIMLLL LISALWSSYY LTQKRIRAVH ETVLSIFYGM VIGLIIRMSP GHYIQDTVTF 
121:	NSSYFFNVLL PPIILNSGYE LNQVNFFNNM LSILIFAIPG TFISAVVIGI ILYIWTFLGL 
181:	ESIDISFADA MSVGATLSAT DPVTILSIFN AYKVDPKLYT IIFGESLLND AISIVMFETC 
241:	QKFHGQPATF SSVFEGAGLF LMTFSVSLLI GVLIGILVAL LLKHTHIRRY PQIESCLILL 
301:	IAYESYFFSN GCHMSGIVSL LFCGITLKHY AYYNMSRRSQ ITIKYIFQLL ARLSENFIFI 
361:	YLGLELFTEV ELVYKPLLII VAAISICVAR WCAVFPLSQF VNWIYRVKTI RSMSGITGEN 
421:	ISVPDEIPYN YQMMTFWAGL RGAVGVALAL GIQGEYKFTL LATVLVVVVL TVIIFGGTTA 
481:	GMLEVLNIKT GCISEEDTSD DEFDIEAPRA INLLNGSSIQ TDLGPYSDNN SPDISIDQFA 
541:	VSSNKNLPNN ISTTGGNTFG GLNETENTSP NPARSSMDKR NLRDKLGTIF NSDSQWFQNF 
601:	DEQVLKPVFL DNVSPSLQDS ATQSPADFSS QNH