Sodium/hydrogen exchanger 1 - Mus musculus (Mouse)

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Q61165 (SL9A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sodium/hydrogen exchanger 1

Alternative name(s):
Na(+)/H(+) exchanger 1
Short name=NHE-1
Solute carrier family 9 member 1

Gene names

Name:	Slc9a1
Synonyms:	Nhe1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	820 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Oligomer. Interacts with calmodulin and TESC. Interacts (via the juxtamembrane region of the cytoplasmic C-terminus 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.
Subcellular location	Membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein. Note: Colocalizes with CHP1 and CHP2 at the reticulum endoplasmic and plasma membrane By similarity.
Post-translational modification	O-glycosylated By similarity. Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1 By similarity.
Sequence similarities	Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. [View classification]
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.

Ontologies

Keywords
Biological process	Antiport Ion transport Sodium transport Transport
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Calmodulin-binding Sodium
PTM	Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell differentiation Inferred from mutant phenotype PubMed 19011045. Source: MGI cell growth Inferred from electronic annotation. Source: Compara cellular response to acidity Inferred from sequence or structural similarity. Source: UniProtKB neuron death Inferred from electronic annotation. Source: Compara positive regulation of action potential Inferred from electronic annotation. Source: Compara positive regulation of cell growth Inferred from electronic annotation. Source: Compara positive regulation of intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara positive regulation of mitochondrial membrane permeability Inferred from electronic annotation. Source: Compara protein oligomerization Inferred from sequence or structural similarity. Source: UniProtKB regulation of intracellular pH Inferred from electronic annotation. Source: Compara regulation of pH Inferred from direct assay PubMed 10666043. Source: MGI regulation of sensory perception of pain Inferred from electronic annotation. Source: Compara regulation of the force of heart contraction Inferred from electronic annotation. Source: Compara response to acid Inferred from mutant phenotype PubMed 10673550. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara sodium ion export Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	basolateral plasma membrane Traceable author statement PubMed 10666043. Source: MGI endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	sodium:hydrogen antiporter activity Inferred from direct assay PubMed 10666043. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 820

820

Sodium/hydrogen exchanger 1

PRO_0000052348

Regions

Topological domain

1 – 12

Cytoplasmic Potential

Transmembrane

13 – 33

Helical; Name=M1; Potential

Topological domain

34 – 105

Extracellular Potential

Transmembrane

106 – 126

Helical; Name=M2; Potential

Topological domain

127 – 133

Cytoplasmic Potential

Transmembrane

134 – 153

Helical; Name=M3; Potential

Topological domain

154 – 158

Extracellular Potential

Transmembrane

159 – 178

Helical; Name=M4; Potential

Topological domain

179 – 195

Cytoplasmic Potential

Transmembrane

196 – 215

Helical; Name=M5; Potential

Topological domain

216 – 231

Extracellular Potential

Transmembrane

232 – 251

Helical; Name=M6; Potential

Topological domain

252 – 260

Cytoplasmic Potential

Transmembrane

261 – 280

Helical; Name=M7; Potential

Topological domain

281 – 298

Extracellular Potential

Transmembrane

299 – 319

Helical; Name=M8; Potential

Topological domain

320 – 342

Cytoplasmic Potential

Transmembrane

343 – 362

Helical; Name=M9; Potential

Topological domain

363 – 385

Extracellular Potential

Intramembrane

386 – 406

Name=H10; By similarity

Topological domain

407 – 414

Extracellular Potential

Transmembrane

415 – 434

Helical; Name=M10; Potential

Topological domain

435 – 452

Cytoplasmic Potential

Transmembrane

453 – 474

Helical; Name=M11; Potential

Topological domain

475 – 483

Extracellular Potential

Transmembrane

484 – 503

Helical; Name=M12; Potential

Topological domain

504 – 820

317

Cytoplasmic Potential

Region

520 – 543

Interaction with CHP2 By similarity

Sites

Site

165

Channel pore-lining By similarity

Amino acid modifications

Modified residue

603

Phosphoserine Ref.3

Modified residue

606

Phosphoserine Ref.3

Modified residue

609

Phosphoserine Ref.3

Modified residue

697

Phosphoserine Ref.5

Modified residue

701

Phosphoserine By similarity

Modified residue

707

Phosphoserine Ref.2 Ref.4

Modified residue

727

Phosphoserine By similarity

Modified residue

730

Phosphoserine By similarity

Modified residue

733

Phosphoserine By similarity

Modified residue

755

Phosphothreonine Ref.4

Modified residue

790

Phosphoserine By similarity

Glycosylation

374

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q61165 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 0589C4D08DD348BE
Show »

FASTA

820

91,468

        10         20         30         40         50         60 
MMLRWSGVWG FHPPRIFPSL LVVVALVGLL PVLRSHGLQH SPTASTIRGS EPPRERSIGD 

        70         80         90        100        110        120 
VTTAPSEPLH RPDDHNLTNL IIEHGGKPSR KAFPVLDIDY PHVRTPFEIS LWILLACLMK 

       130        140        150        160        170        180 
IGFHVIPTIS SIVPESCLLI VVGLLVGGLI KGVGETPPFL QSDVFFLFLL PPIILDAGYF 

       190        200        210        220        230        240 
LPLRQFTENL GTILIFAVVG TLWNAFFLGG LLYAVCLVGG EQINNIGLLD TLLFGSIISA 

       250        260        270        280        290        300 
VDPVAVLAVF EEIHINELLH ILVFGESLLN DAVTVVLYHL FEEFASYDSV GISDIFLGFL 

       310        320        330        340        350        360 
SFFVVALGGV FVGVVYGVIA AFTSRFTSHI RVIEPLFVFL YSYMAYLSAE LFHLSGIMAL 

       370        380        390        400        410        420 
IASGVVMRPY VEANISHKSH TTIKYFLKMW SSVSETLIFI FLGVSTVAGS HQWNWTFVIS 

       430        440        450        460        470        480 
TLLFCLIARV LGVLVLTWFI NKFRIVKLTP KDQFIIAYGG LRGAIAFSLG YLLDKKHFPM 

       490        500        510        520        530        540 
CDLFLTAIIT VIFFTVFVQG MTIRPLVDLL AVKKKQETKR SINEEIHTQF LDHLLTGIED 

       550        560        570        580        590        600 
ICGHYGHHHW KDKLNRFNKK YVKKCLIAGE RSKEPQLIAF YHKMEMKQAI ELVESGGMGK 

       610        620        630        640        650        660 
IPSAVSTVSM QNIHPKAVTS DRILPALSKD KEEEIRKILR SNLQKTRQRL RSYNRHTLVA 

       670        680        690        700        710        720 
DPYEEAWNQM LLRRQKARQL EQKITNYLTV PAHKLDSPTL SRARIGSDPL AYEPKADLPV 

       730        740        750        760        770        780 
ITIDPASPQS PESVDLVNEE LKGKVLGLNR GPRVTPEEEE EDEDGIIMIR SKEPSSPGTD 

       790        800        810        820 
DVFTPGSSDS PSSQRIQRCL SDPGPHPEPG EGEPFIPKGQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, MASS SPECTROMETRY. Tissue: Brain cortex.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-606 AND SER-609, MASS SPECTROMETRY. 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-707 AND THR-755, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51112 mRNA. Translation: AAA92976.1.
IPI	IPI00380785.
RefSeq	NP_058677.1. NM_016981.2.
UniGene	Mm.4312.
3D structure databases
ProteinModelPortal	Q61165.
SMR	Q61165. Positions 159-184, 342-369, 451-476, 507-549, 626-689.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61165. 1 interaction.
PTM databases
PhosphoSite	Q61165.
Proteomic databases
PaxDb	Q61165.
PRIDE	Q61165.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030669; ENSMUSP00000030669; ENSMUSG00000028854.
GeneID	20544.
KEGG	mmu:20544.
Organism-specific databases
CTD	6548.
MGI	MGI:102462. Slc9a1.
Phylogenomic databases
eggNOG	COG0025.
GeneTree	ENSGT00560000077158.
HOGENOM	HOG000247044.
HOVERGEN	HBG052615.
KO	K05742.
OMA	EFANYDR.
OrthoDB	EOG4FR0R9.
Gene expression databases
ArrayExpress	Q61165.
Bgee	Q61165.
Genevestigator	Q61165.
GermOnline	ENSMUSG00000028854. Mus musculus.
Family and domain databases
InterPro	IPR006153. Cation/H_exchanger. IPR018422. Cation/H_exchanger_CPA1. IPR001970. Na/H_exchanger_1. IPR004709. NaH_exchanger. [Graphical view]
PANTHER	PTHR10110. PTHR10110. 1 hit.
Pfam	PF00999. Na_H_Exchanger. 1 hit. [Graphical view]
PRINTS	PR01084. NAHEXCHNGR. PR01085. NAHEXCHNGR1.
TIGRFAMs	TIGR00840. b_cpa1. 1 hit.
ProtoNet	Search...
Other
NextBio	298831.
SOURCE	Search...

Entry information

Entry name

SL9A1_MOUSE

Accession

Primary (citable) accession number: Q61165

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents