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Protein

Sodium/hydrogen exchanger 1

Gene

Slc9a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei165 – 1651Channel pore-liningBy similarity

GO - Molecular functioni

  1. calcium-dependent protein binding Source: MGI
  2. protein phosphatase 2B binding Source: MGI
  3. sodium:proton antiporter activity Source: MGI

GO - Biological processi

  1. cardiac muscle cell contraction Source: Ensembl
  2. cardiac muscle cell differentiation Source: MGI
  3. cell growth Source: Ensembl
  4. cellular response to acidic pH Source: UniProtKB
  5. cellular response to antibiotic Source: Ensembl
  6. cellular response to electrical stimulus Source: Ensembl
  7. cellular response to epinephrine stimulus Source: MGI
  8. cellular response to hypoxia Source: Ensembl
  9. cellular response to insulin stimulus Source: Ensembl
  10. cellular sodium ion homeostasis Source: MGI
  11. hydrogen ion transmembrane transport Source: MGI
  12. negative regulation of apoptotic process Source: Ensembl
  13. neuron death Source: Ensembl
  14. positive regulation of action potential Source: Ensembl
  15. positive regulation of calcineurin-NFAT signaling cascade Source: MGI
  16. positive regulation of calcium:sodium antiporter activity Source: MGI
  17. positive regulation of cardiac muscle hypertrophy Source: MGI
  18. positive regulation of cell growth Source: Ensembl
  19. positive regulation of mitochondrial membrane permeability Source: Ensembl
  20. positive regulation of NFAT protein import into nucleus Source: MGI
  21. positive regulation of the force of heart contraction Source: MGI
  22. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  23. protein oligomerization Source: UniProtKB
  24. regulation of cardiac muscle contraction by calcium ion signaling Source: MGI
  25. regulation of intracellular pH Source: MGI
  26. regulation of pH Source: MGI
  27. regulation of sensory perception of pain Source: Ensembl
  28. regulation of the force of heart contraction by cardiac conduction Source: MGI
  29. response to acidic pH Source: MGI
  30. response to drug Source: Ensembl
  31. response to muscle stretch Source: MGI
  32. sodium ion export Source: UniProtKB
  33. sodium ion import across plasma membrane Source: MGI
  34. sodium ion transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Sodium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Sodium

Enzyme and pathway databases

ReactomeiREACT_324002. Sodium/Proton exchangers.
REACT_353590. Hyaluronan uptake and degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/hydrogen exchanger 1
Alternative name(s):
Na(+)/H(+) exchanger 1
Short name:
NHE-1
Solute carrier family 9 member 1
Gene namesi
Name:Slc9a1
Synonyms:Nhe1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:102462. Slc9a1.

Subcellular locationi

  1. Membrane; Multi-pass membrane protein
  2. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  3. Cell membrane; Multi-pass membrane protein

  4. Note: Colocalizes with CHP1 and CHP2 at the reticulum endoplasmic and plasma membrane.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3321Helical; Name=M1Sequence AnalysisAdd
BLAST
Topological domaini34 – 10572ExtracellularSequence AnalysisAdd
BLAST
Transmembranei106 – 12621Helical; Name=M2Sequence AnalysisAdd
BLAST
Topological domaini127 – 1337CytoplasmicSequence Analysis
Transmembranei134 – 15320Helical; Name=M3Sequence AnalysisAdd
BLAST
Topological domaini154 – 1585ExtracellularSequence Analysis
Transmembranei159 – 17820Helical; Name=M4Sequence AnalysisAdd
BLAST
Topological domaini179 – 19517CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei196 – 21520Helical; Name=M5Sequence AnalysisAdd
BLAST
Topological domaini216 – 23116ExtracellularSequence AnalysisAdd
BLAST
Transmembranei232 – 25120Helical; Name=M6Sequence AnalysisAdd
BLAST
Topological domaini252 – 2609CytoplasmicSequence Analysis
Transmembranei261 – 28020Helical; Name=M7Sequence AnalysisAdd
BLAST
Topological domaini281 – 29818ExtracellularSequence AnalysisAdd
BLAST
Transmembranei299 – 31921Helical; Name=M8Sequence AnalysisAdd
BLAST
Topological domaini320 – 34223CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei343 – 36220Helical; Name=M9Sequence AnalysisAdd
BLAST
Topological domaini363 – 38523ExtracellularSequence AnalysisAdd
BLAST
Intramembranei386 – 40621Name=H10By similarityAdd
BLAST
Topological domaini407 – 4148ExtracellularSequence Analysis
Transmembranei415 – 43420Helical; Name=M10Sequence AnalysisAdd
BLAST
Topological domaini435 – 45218CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei453 – 47422Helical; Name=M11Sequence AnalysisAdd
BLAST
Topological domaini475 – 4839ExtracellularSequence Analysis
Transmembranei484 – 50320Helical; Name=M12Sequence AnalysisAdd
BLAST
Topological domaini504 – 820317CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. basolateral plasma membrane Source: MGI
  3. cation-transporting ATPase complex Source: MGI
  4. cell surface Source: Ensembl
  5. cytoplasm Source: UniProtKB
  6. endoplasmic reticulum Source: UniProtKB
  7. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  8. extracellular vesicular exosome Source: MGI
  9. focal adhesion Source: MGI
  10. integral component of plasma membrane Source: MGI
  11. intercalated disc Source: Ensembl
  12. membrane Source: MGI
  13. membrane raft Source: MGI
  14. mitochondrion Source: Ensembl
  15. nucleoplasm Source: MGI
  16. perinuclear region of cytoplasm Source: Ensembl
  17. plasma membrane Source: UniProtKB
  18. T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 820820Sodium/hydrogen exchanger 1PRO_0000052348Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Modified residuei603 – 6031Phosphoserine1 Publication
Modified residuei606 – 6061PhosphoserineBy similarity
Modified residuei609 – 6091Phosphoserine1 Publication
Modified residuei697 – 6971Phosphoserine2 Publications
Modified residuei701 – 7011PhosphoserineBy similarity
Modified residuei707 – 7071Phosphoserine2 Publications
Modified residuei727 – 7271PhosphoserineBy similarity
Modified residuei730 – 7301PhosphoserineBy similarity
Modified residuei733 – 7331PhosphoserineBy similarity
Modified residuei790 – 7901PhosphoserineBy similarity

Post-translational modificationi

O-glycosylated.By similarity
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1 (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61165.
PaxDbiQ61165.
PRIDEiQ61165.

PTM databases

PhosphoSiteiQ61165.

Expressioni

Gene expression databases

BgeeiQ61165.
ExpressionAtlasiQ61165. baseline and differential.
GenevestigatoriQ61165.

Interactioni

Subunit structurei

Oligomer. Interacts with calmodulin and TESC. Interacts (via the juxtamembrane region of the cytoplasmic C-terminal domain) with CHP1; the interaction occurs at the plasma membrane in a calcium-dependent manner. Interacts with CHP2; the interaction occurs in a calcium-dependent manner (By similarity).By similarity

Protein-protein interaction databases

BioGridi203321. 3 interactions.
IntActiQ61165. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ61165.
SMRiQ61165. Positions 159-184, 230-278, 342-369, 451-476, 507-549, 626-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni520 – 54324Interaction with CHP2By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
HOVERGENiHBG052615.
InParanoidiQ61165.
KOiK05742.
OMAiYDRVGIV.
OrthoDBiEOG7XWPN4.
TreeFamiTF317212.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR001970. Na/H_exchanger_1.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01085. NAHEXCHNGR1.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q61165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLRWSGVWG FHPPRIFPSL LVVVALVGLL PVLRSHGLQH SPTASTIRGS
60 70 80 90 100
EPPRERSIGD VTTAPSEPLH RPDDHNLTNL IIEHGGKPSR KAFPVLDIDY
110 120 130 140 150
PHVRTPFEIS LWILLACLMK IGFHVIPTIS SIVPESCLLI VVGLLVGGLI
160 170 180 190 200
KGVGETPPFL QSDVFFLFLL PPIILDAGYF LPLRQFTENL GTILIFAVVG
210 220 230 240 250
TLWNAFFLGG LLYAVCLVGG EQINNIGLLD TLLFGSIISA VDPVAVLAVF
260 270 280 290 300
EEIHINELLH ILVFGESLLN DAVTVVLYHL FEEFASYDSV GISDIFLGFL
310 320 330 340 350
SFFVVALGGV FVGVVYGVIA AFTSRFTSHI RVIEPLFVFL YSYMAYLSAE
360 370 380 390 400
LFHLSGIMAL IASGVVMRPY VEANISHKSH TTIKYFLKMW SSVSETLIFI
410 420 430 440 450
FLGVSTVAGS HQWNWTFVIS TLLFCLIARV LGVLVLTWFI NKFRIVKLTP
460 470 480 490 500
KDQFIIAYGG LRGAIAFSLG YLLDKKHFPM CDLFLTAIIT VIFFTVFVQG
510 520 530 540 550
MTIRPLVDLL AVKKKQETKR SINEEIHTQF LDHLLTGIED ICGHYGHHHW
560 570 580 590 600
KDKLNRFNKK YVKKCLIAGE RSKEPQLIAF YHKMEMKQAI ELVESGGMGK
610 620 630 640 650
IPSAVSTVSM QNIHPKAVTS DRILPALSKD KEEEIRKILR SNLQKTRQRL
660 670 680 690 700
RSYNRHTLVA DPYEEAWNQM LLRRQKARQL EQKITNYLTV PAHKLDSPTL
710 720 730 740 750
SRARIGSDPL AYEPKADLPV ITIDPASPQS PESVDLVNEE LKGKVLGLNR
760 770 780 790 800
GPRVTPEEEE EDEDGIIMIR SKEPSSPGTD DVFTPGSSDS PSSQRIQRCL
810 820
SDPGPHPEPG EGEPFIPKGQ
Length:820
Mass (Da):91,468
Last modified:November 1, 1997 - v1
Checksum:i0589C4D08DD348BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51112 mRNA. Translation: AAA92976.1.
CCDSiCCDS38903.1.
RefSeqiNP_058677.1. NM_016981.2.
UniGeneiMm.4312.

Genome annotation databases

EnsembliENSMUST00000030669; ENSMUSP00000030669; ENSMUSG00000028854.
GeneIDi20544.
KEGGimmu:20544.
UCSCiuc008vcs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51112 mRNA. Translation: AAA92976.1.
CCDSiCCDS38903.1.
RefSeqiNP_058677.1. NM_016981.2.
UniGeneiMm.4312.

3D structure databases

ProteinModelPortaliQ61165.
SMRiQ61165. Positions 159-184, 230-278, 342-369, 451-476, 507-549, 626-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203321. 3 interactions.
IntActiQ61165. 1 interaction.

PTM databases

PhosphoSiteiQ61165.

Proteomic databases

MaxQBiQ61165.
PaxDbiQ61165.
PRIDEiQ61165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030669; ENSMUSP00000030669; ENSMUSG00000028854.
GeneIDi20544.
KEGGimmu:20544.
UCSCiuc008vcs.1. mouse.

Organism-specific databases

CTDi6548.
MGIiMGI:102462. Slc9a1.

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
HOVERGENiHBG052615.
InParanoidiQ61165.
KOiK05742.
OMAiYDRVGIV.
OrthoDBiEOG7XWPN4.
TreeFamiTF317212.

Enzyme and pathway databases

ReactomeiREACT_324002. Sodium/Proton exchangers.
REACT_353590. Hyaluronan uptake and degradation.

Miscellaneous databases

NextBioi298831.
PROiQ61165.
SOURCEiSearch...

Gene expression databases

BgeeiQ61165.
ExpressionAtlasiQ61165. baseline and differential.
GenevestigatoriQ61165.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR001970. Na/H_exchanger_1.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01085. NAHEXCHNGR1.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of the mouse Na/H antiporter (NHE-1) and a potential splice variant."
    Dewey M.J., Ennis T.M., Bowman L.H.
    Mol. Biol. Rep. 28:111-117(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-609 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSL9A1_MOUSE
AccessioniPrimary (citable) accession number: Q61165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The region between transmembrane regions M4 and M5 and between M6 and M7 (also termed intracellular loops IL2 and IL4, respectively) seem to be localized at least in part in the membrane. The hydrophobic region H10 is proposed to be located within the membrane.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.