Slc9a1
entrez
20544
canonical
uniprot
Q61165
canonical
ensembl
ENSMUSG00000028854
resolver
ensp
ENSMUSP00000030669
resolver
enst
ENSMUST00000030669
resolver
genesymbol
Slc9a1
resolver
genesymbol_syn
Nhe1
resolver
uniprot
Q3UDC9
resolver
uniprot_entry
Q3UDC9_MOUSE
resolver
uniprot_entry
SL9A1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Activated at acidic pHs. Inhibited by cariporide and eniporide. Inhibited by amiloride and 5-amino-substituted derivatives. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) bind and differentially regulate SLC9A1 activity. {ECO:0000250|UniProtKB:P19634}.
uniprot
proteins
amino_acid_sequence
MMLRWSGVWGFHPPRIFPSLLVVVALVGLLPVLRSHGLQHSPTASTIRGSEPPRERSIGDVTTAPSEPLHRPDDHNLTNLIIEHGGKPSRKAFPVLDIDYPHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLLYAVCLVGGEQINNIGLLDTLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFASYDSVGISDIFLGFLSFFVVALGGVFVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHQWNWTFVISTLLFCLIARVLGVLVLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKAVTSDRILPALSKDKEEEIRKILRSNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKITNYLTVPAHKLDSPTLSRARIGSDPLAYEPKADLPVITIDPASPQSPESVDLVNEELKGKVLGLNRGPRVTPEEEEEDEDGIIMIRSKEPSSPGTDDVFTPGSSDSPSSQRIQRCLSDPGPHPEPGEGEPFIPKGQ
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Slc9a1 is the cause of slow-wave epilepsy (swe) phenotype (PubMed:9335342). Mutant mice display slow-wave epilepsy, with a neurological syndrome including ataxia and a unique epilepsy phenotype consisting of 3/sec absence and tonic-clonic seizures. Mutants show selective neuronal death in the cerebellum and brainstem. Mice display also several other significant abnormalities in growth and development, and less than half of the mutant homozygous animals survived to weaning. Most died by 35-40 days (PubMed:9335342). {ECO:0000269|PubMed:9335342}.
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 (By similarity). Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key role in maintening intracellular pH neutral and cell volume, and thus is important for cell growth, proliferation, migration and survival. 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:0000250|UniProtKB:P26431}.
uniprot
proteins
mass_dalton
91468
uniprot
proteins
post_translational_modification
PTM: O-glycosylated. {ECO:0000250|UniProtKB:P19634}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1. {ECO:0000250|UniProtKB:P26431}.; PTM: Palmitoylated; may play a major role in SLC9A1 regulation. {ECO:0000250|UniProtKB:P26431}.; PTM: Phosphorylation at Thr-784 increases SLC9A1 activity. 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
10199808
uniprot
proteins
pubmed
11931388
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19369449
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9335342
uniprot
proteins
sequence_length
820
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19634}; 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:0000269|PubMed:19369449}.
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