Slc9a1
entrez
24782
canonical
uniprot
P26431
canonical
ensembl
ENSRNOG00000007982
resolver
ensembl
ENSRNOG00055024603
resolver
ensembl
ENSRNOG00060029701
resolver
ensembl
ENSRNOG00065028991
resolver
ensp
ENSRNOP00000011049
resolver
ensp
ENSRNOP00055034569
resolver
ensp
ENSRNOP00060042898
resolver
ensp
ENSRNOP00065041160
resolver
enst
ENSRNOT00000011049
resolver
enst
ENSRNOT00055042337
resolver
enst
ENSRNOT00060051581
resolver
enst
ENSRNOT00065050094
resolver
genesymbol
Slc9a1
resolver
genesymbol_syn
Nhe1
resolver
uniprot_entry
SL9A1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Activated at acidic pHs. Inhibited by cariporide and eniporide (By similarity). Inhibited by amiloride and 5-amino-substituted derivatives. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) bind and activates SLC9A1 transporter activity (Probable). {ECO:0000250|UniProtKB:P19634, ECO:0000305|PubMed:10893269}.
uniprot
proteins
amino_acid_sequence
MMLRWSGIWGLYPPRIFPSLLVVVALVGLLPVLRSHGLQLNPTASTIRGSEPPRERSIGDVTTAPSEPLHHPDDRNLTNLYIEHGAKPVRKAFPVLDIDYLHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLLYAVCLVGGEQINNIGLLDTLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFASYEYVGISDIFLGFLSFFVVSLGGVFVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHQWNWTFVISTLLFCLIARVLGVLVLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKSAASERILPALSKDKEEEIRKILRSNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKITNYLTVPAHKLDSPTMSRARIGSDPLAYEPKADLPVITIDPASPQSPESVDLVNEELKGKVLGLKRGPRTTPEEEEEDEDGVIMIRSKEPSSPGTDDVFTPGPSDSPGSQRIQRCLSDPGPHPEPGEGEPFIPKGQ
uniprot
proteins
function
FUNCTION: Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in exchange for external protons driven by the inward sodium ion chemical gradient, protecting cells from acidification that occurs from metabolism (Probable) (PubMed:10893269, PubMed:11163215). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (PubMed:6334130). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival (PubMed:34774621). In addition, can transport lithium Li(+) and also functions as a Na(+)/Li(+) antiporter. SLC9A1 also functions in membrane anchoring and organization of scaffolding complexes that coordinate signaling inputs (By similarity). {ECO:0000250|UniProtKB:P19634, ECO:0000269|PubMed:10893269, ECO:0000269|PubMed:11163215, ECO:0000269|PubMed:34774621, ECO:0000269|PubMed:6334130, ECO:0000305|PubMed:6334130}.
uniprot
proteins
mass_dalton
91647
uniprot
proteins
mutagenesis
MUTAGEN 266; /note="E->I: Abolishes sodium:proton antiporter activity."; /evidence="ECO:0000269|PubMed:11163215"; MUTAGEN 522..538; /note="INEEIHTQFLDHLLTGI->QNEEQHTQQLDHQQTGQ: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization."; /evidence="ECO:0000269|PubMed:21543739"; MUTAGEN 530..535; /note="FLDHLL->AADHAA: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization."; /evidence="ECO:0000269|PubMed:18321853"; MUTAGEN 530..535; /note="FLDHLL->QQDHQQ: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization."; /evidence="ECO:0000269|PubMed:18321853"; MUTAGEN 530..535; /note="FLDHLL->RRDHRR: Abolishes interaction with TESC and markedly reduces transporter activity. Does not alter its cell membrane localization."; /evidence="ECO:0000269|PubMed:18321853
uniprot
proteins
post_translational_modification
PTM: N-glycosylated and O-glycosylated in the N-terminal region. {ECO:0000269|PubMed:21543739, ECO:0000269|PubMed:9688597}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1. {ECO:0000269|PubMed:21543739}.; PTM: Palmitoylated; may play a major role in SLC9A1 regulation. {ECO:0000269|PubMed:34774621}.; PTM: Phosphorylation at Thr-784 increases SLC9A1 activity; specifically dephosphorylated by PPP3CA. Specifically dephosphorylated at Thr-784 by PPP3CA that negatively regulates SLC9A1 activity. Phosphorylation at Ser-652 by AKT1 reduces SLC9A1 binding to CALM1. {ECO:0000250|UniProtKB:P19634}.
uniprot
proteins
protein_family
Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family
uniprot
proteins
pubmed
10893269
uniprot
proteins
pubmed
11163215
uniprot
proteins
pubmed
12576672
uniprot
proteins
pubmed
1577762
uniprot
proteins
pubmed
18321853
uniprot
proteins
pubmed
21543739
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
34774621
uniprot
proteins
pubmed
6334130
uniprot
proteins
pubmed
9688597
uniprot
proteins
sequence_length
820
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21543739}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19634}. Basolateral cell membrane {ECO:0000250|UniProtKB:P48762}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19634}. Note=Localized basolaterally in every epithelial cell, except in the choroid plexus where SLC9A1 is expressed luminally. {ECO:0000250|UniProtKB:P19634}.
uniprot
proteins
transmembrane_region
TRANSMEM 103..125; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 135..152; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 163..180; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 191..219; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 227..253; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 257..287; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 292..326; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 333..345; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 355..375; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 378..408; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 415..442; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 449..473; /note="Helical; Name=12"; /evidence="ECO:0000250|UniProtKB:P19634"; TRANSMEM 480..509; /note="Helical; Name=13"; /evidence="ECO:0000250|UniProtKB:P19634
uniprot
proteins