UniProtKB - P26431 (SL9A1_RAT)
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Protein
Sodium/hydrogen exchanger 1
Gene
Slc9a1
Organism
Rattus norvegicus (Rat)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 165 | Channel pore-liningBy similarity | 1 |
GO - Molecular functioni
- calcium-dependent protein binding Source: UniProtKB
- calmodulin binding Source: UniProtKB-KW
- potassium:proton antiporter activity Source: GO_Central
- protein phosphatase 2B binding Source: RGD
- sodium:proton antiporter activity Source: UniProtKB
GO - Biological processi
- cardiac muscle cell contraction Source: RGD
- cardiac muscle cell differentiation Source: RGD
- cell differentiation Source: RGD
- cellular response to acidic pH Source: UniProtKB
- cellular response to antibiotic Source: RGD
- cellular response to cold Source: RGD
- cellular response to electrical stimulus Source: RGD
- cellular response to epinephrine stimulus Source: RGD
- cellular response to hypoxia Source: RGD
- cellular response to insulin stimulus Source: RGD
- cellular response to organic cyclic compound Source: RGD
- cellular sodium ion homeostasis Source: RGD
- hydrogen ion transmembrane transport Source: RGD
- negative regulation of apoptotic process Source: RGD
- neuron death Source: RGD
- positive regulation of action potential Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of calcineurin-NFAT signaling cascade Source: RGD
- positive regulation of calcium:sodium antiporter activity Source: RGD
- positive regulation of cardiac muscle hypertrophy Source: RGD
- positive regulation of cell growth Source: RGD
- positive regulation of intracellular signal transduction Source: RGD
- positive regulation of mitochondrial membrane permeability Source: RGD
- positive regulation of the force of heart contraction Source: RGD
- positive regulation of transcription by RNA polymerase II Source: RGD
- potassium ion transmembrane transport Source: GO_Central
- regulation of cardiac muscle contraction by calcium ion signaling Source: RGD
- regulation of intracellular pH Source: RGD
- regulation of pH Source: UniProtKB
- regulation of sensory perception of pain Source: RGD
- regulation of the force of heart contraction Source: RGD
- regulation of the force of heart contraction by cardiac conduction Source: RGD
- response to acidic pH Source: UniProtKB
- response to muscle stretch Source: RGD
- response to organic cyclic compound Source: RGD
- sodium ion export Source: UniProtKB
- sodium ion import across plasma membrane Source: RGD
- sodium ion transport Source: RGD
Keywordsi
Molecular function | Calmodulin-binding |
Biological process | Antiport, Ion transport, Sodium transport, Transport |
Ligand | Sodium |
Enzyme and pathway databases
Reactomei | R-RNO-2160916. Hyaluronan uptake and degradation. R-RNO-425986. Sodium/Proton exchangers. |
Protein family/group databases
TCDBi | 2.A.36.1.1. the monovalent cation:proton antiporter-1 (cpa1) family. |
Names & Taxonomyi
Protein namesi | Recommended name: Sodium/hydrogen exchanger 1Alternative name(s): Na(+)/H(+) exchanger 1 Short name: NHE-1 Solute carrier family 9 member 1 |
Gene namesi | Name:Slc9a1 Synonyms:Nhe1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3718. Slc9a1. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 12 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 13 – 33 | Helical; Name=M1Sequence analysisAdd BLAST | 21 | |
Topological domaini | 34 – 105 | ExtracellularSequence analysisAdd BLAST | 72 | |
Transmembranei | 106 – 131 | Helical; Name=M2Sequence analysisAdd BLAST | 26 | |
Topological domaini | 132 – 133 | CytoplasmicSequence analysis | 2 | |
Transmembranei | 134 – 153 | Helical; Name=M3Sequence analysisAdd BLAST | 20 | |
Topological domaini | 154 – 158 | ExtracellularSequence analysis | 5 | |
Transmembranei | 159 – 178 | Helical; Name=M4Sequence analysisAdd BLAST | 20 | |
Topological domaini | 179 – 195 | CytoplasmicSequence analysisAdd BLAST | 17 | |
Transmembranei | 196 – 215 | Helical; Name=M5Sequence analysisAdd BLAST | 20 | |
Topological domaini | 216 – 231 | ExtracellularSequence analysisAdd BLAST | 16 | |
Transmembranei | 232 – 251 | Helical; Name=M6Sequence analysisAdd BLAST | 20 | |
Topological domaini | 252 – 260 | CytoplasmicSequence analysis | 9 | |
Transmembranei | 261 – 280 | Helical; Name=M7Sequence analysisAdd BLAST | 20 | |
Topological domaini | 281 – 298 | ExtracellularSequence analysisAdd BLAST | 18 | |
Transmembranei | 299 – 319 | Helical; Name=M8Sequence analysisAdd BLAST | 21 | |
Topological domaini | 320 – 342 | CytoplasmicSequence analysisAdd BLAST | 23 | |
Transmembranei | 343 – 362 | Helical; Name=M9Sequence analysisAdd BLAST | 20 | |
Topological domaini | 363 – 385 | ExtracellularSequence analysisAdd BLAST | 23 | |
Intramembranei | 386 – 406 | Name=H10By similarityAdd BLAST | 21 | |
Topological domaini | 407 – 414 | ExtracellularSequence analysis | 8 | |
Transmembranei | 415 – 434 | Helical; Name=M10Sequence analysisAdd BLAST | 20 | |
Topological domaini | 435 – 452 | CytoplasmicSequence analysisAdd BLAST | 18 | |
Transmembranei | 453 – 474 | Helical; Name=M11Sequence analysisAdd BLAST | 22 | |
Topological domaini | 475 – 483 | ExtracellularSequence analysis | 9 | |
Transmembranei | 484 – 503 | Helical; Name=M12Sequence analysisAdd BLAST | 20 | |
Topological domaini | 504 – 820 | CytoplasmicSequence analysisAdd BLAST | 317 |
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 522 – 538 | INEEI…LLTGI → QNEEQHTQQLDHQQTGQ: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization. 1 PublicationAdd BLAST | 17 | |
Mutagenesisi | 530 – 535 | FLDHLL → AADHAA: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization. 1 Publication | 6 | |
Mutagenesisi | 530 – 535 | FLDHLL → QQDHQQ: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization. 1 Publication | 6 | |
Mutagenesisi | 530 – 535 | FLDHLL → RRDHRR: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization. 1 Publication | 6 |
Chemistry databases
ChEMBLi | CHEMBL2577. |
GuidetoPHARMACOLOGYi | 948. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052351 | 1 – 820 | Sodium/hydrogen exchanger 1Add BLAST | 820 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 374 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 603 | PhosphoserineCombined sources | 1 | |
Modified residuei | 606 | PhosphoserineBy similarity | 1 | |
Modified residuei | 607 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 609 | PhosphoserineCombined sources | 1 | |
Modified residuei | 697 | PhosphoserineCombined sources | 1 | |
Modified residuei | 701 | PhosphoserineCombined sources | 1 | |
Modified residuei | 707 | PhosphoserineCombined sources | 1 | |
Modified residuei | 727 | PhosphoserineCombined sources | 1 | |
Modified residuei | 730 | PhosphoserineCombined sources | 1 | |
Modified residuei | 733 | PhosphoserineCombined sources | 1 | |
Modified residuei | 755 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 790 | PhosphoserineCombined sources | 1 | |
Modified residuei | 801 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
N-glycosylated and O-glycosylated in the N-terminal region.2 Publications
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1.1 Publication
Keywords - PTMi
Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P26431. |
PRIDEi | P26431. |
PTM databases
iPTMneti | P26431. |
PhosphoSitePlusi | P26431. |
Expressioni
Tissue specificityi
Not tissue specific.
Gene expression databases
Bgeei | ENSRNOG00000007982. |
Genevisiblei | P26431. RN. |
Interactioni
Subunit structurei
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). Oligomer. Interacts with CHP1, CHP2 and TESC.By similarity2 Publications
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
Chp2 | Q810D1 | 2 | EBI-77471,EBI-6146708 |
GO - Molecular functioni
- calcium-dependent protein binding Source: UniProtKB
- calmodulin binding Source: UniProtKB-KW
- protein phosphatase 2B binding Source: RGD
Protein-protein interaction databases
BioGridi | 246906. 1 interactor. |
IntActi | P26431. 3 interactors. |
STRINGi | 10116.ENSRNOP00000011049. |
Chemistry databases
BindingDBi | P26431. |
Structurei
3D structure databases
ProteinModelPortali | P26431. |
SMRi | P26431. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 520 – 543 | Interaction with CHP2By similarityAdd BLAST | 24 |
Sequence similaritiesi
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. [View classification]Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1966. Eukaryota. COG0025. LUCA. |
GeneTreei | ENSGT00760000119074. |
HOGENOMi | HOG000247044. |
HOVERGENi | HBG052615. |
InParanoidi | P26431. |
KOi | K05742. |
OMAi | YDRVGIV. |
OrthoDBi | EOG091G02Q0. |
PhylomeDBi | P26431. |
TreeFami | TF317212. |
Family and domain databases
InterProi | View protein in InterPro IPR006153. Cation/H_exchanger. IPR018422. Cation/H_exchanger_CPA1. IPR001970. Na/H_exchanger_1. IPR004709. NaH_exchanger. IPR032103. NHE_CaM-bd. |
PANTHERi | PTHR10110. PTHR10110. 1 hit. PTHR10110:SF59. PTHR10110:SF59. 1 hit. |
Pfami | View protein in Pfam PF00999. Na_H_Exchanger. 1 hit. PF16644. NEXCaM_BD. 1 hit. |
PRINTSi | PR01084. NAHEXCHNGR. PR01085. NAHEXCHNGR1. |
TIGRFAMsi | TIGR00840. b_cpa1. 1 hit. |
i Sequence
Sequence statusi: Complete.
P26431-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MMLRWSGIWG LYPPRIFPSL LVVVALVGLL PVLRSHGLQL NPTASTIRGS
60 70 80 90 100
EPPRERSIGD VTTAPSEPLH HPDDRNLTNL YIEHGAKPVR KAFPVLDIDY
110 120 130 140 150
LHVRTPFEIS 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 FEEFASYEYV GISDIFLGFL
310 320 330 340 350
SFFVVSLGGV 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 QNIHPKSAAS ERILPALSKD KEEEIRKILR SNLQKTRQRL
660 670 680 690 700
RSYNRHTLVA DPYEEAWNQM LLRRQKARQL EQKITNYLTV PAHKLDSPTM
710 720 730 740 750
SRARIGSDPL AYEPKADLPV ITIDPASPQS PESVDLVNEE LKGKVLGLKR
760 770 780 790 800
GPRTTPEEEE EDEDGVIMIR SKEPSSPGTD DVFTPGPSDS PGSQRIQRCL
810 820
SDPGPHPEPG EGEPFIPKGQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M85299 mRNA. Translation: AAA98479.1. |
PIRi | A40204. |
RefSeqi | NP_036784.1. NM_012652.1. |
UniGenei | Rn.5025. |
Genome annotation databases
Ensembli | ENSRNOT00000011049; ENSRNOP00000011049; ENSRNOG00000007982. |
GeneIDi | 24782. |
KEGGi | rno:24782. |
UCSCi | RGD:3718. rat. |
Similar proteinsi
Entry informationi
Entry namei | SL9A1_RAT | |
Accessioni | P26431Primary (citable) accession number: P26431 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
Last sequence update: | October 1, 1996 | |
Last modified: | March 28, 2018 | |
This is version 157 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata 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
Although PubMed:18321853 show that TESC-binding results in the maturation and accumulation of SLC9A1 at the cell surface, previous studies with human SLC9A1 report that TESC-binding results in a decrease in activity.Curated
Although PubMed:18321853 show that they CHP1 and TESC bind at the same C-terminal site, previous studies with human SLC9A1 report that they bind to different sites.Curated