SLC26A5
entrez
375611
canonical
uniprot
P58743
canonical
ensembl
ENSG00000170615
resolver
ensp
ENSP00000304783
resolver
ensp
ENSP00000342396
resolver
ensp
ENSP00000349210
resolver
ensp
ENSP00000377336
resolver
ensp
ENSP00000389733
resolver
genesymbol
SLC26A5
resolver
genesymbol_syn
PRES
resolver
hgnc
HGNC:9359
resolver
uniprot
Q496J2
resolver
uniprot
Q7Z7F3
resolver
uniprot
Q86UF8
resolver
uniprot
Q86UF9
resolver
uniprot
Q86UG0
resolver
uniprot_entry
S26A5_HUMAN
resolver
uniprot_sec
Q496J2
resolver
uniprot_sec
Q7Z7F3
resolver
uniprot_sec
Q86UF8
resolver
uniprot_sec
Q86UF9
resolver
uniprot_sec
Q86UG0
resolver
amino_acid_sequence
MDHAEENEILAATQRYYVERPIFSHPVLQERLHTKDKVPDSIADKLKQAFTCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPIFGLYSSFYPVIMYCFLGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLKESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGLCNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVDGEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALAEQEASAPPSQEDLEPNATPATPEA
uniprot
proteins
disease_involvement
DISEASE: Deafness, autosomal recessive, 61 (DFNB61) [MIM:613865]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. {ECO:0000269|PubMed:12719379}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ (By similarity). Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane (By similarity). The nature of the voltage sensor is not completely clear, and two models compete. In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (PubMed:34390643). However, the effective voltage sensor may be the result of a hybrid voltage sensor, assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion) (By similarity). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization (PubMed:34390643). The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (PubMed:34390643). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state (PubMed:34390643). In addition, can act as a weak Cl(-)/HCO3(-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). Moreover, supports a role in cardiac mechanical amplification serving as an elastic element to enhance the actomyosin- based sarcomere contraction system (By similarity). {ECO:0000250|UniProtKB:D7PC76, ECO:0000250|UniProtKB:Q99NH7, ECO:0000250|UniProtKB:Q9EPH0, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643}.
uniprot
proteins
mass_dalton
81264
uniprot
proteins
mutagenesis
MUTAGEN 101; /note="F->Y: Decreases salicylate inhibition."; /evidence="ECO:0000269|PubMed:34390643
uniprot
proteins
protein_family
SLC26A/SulP transporter (TC 2.A.53) family
uniprot
proteins
pubmed
12719379
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
34390643
uniprot
proteins
pubmed
39482536
uniprot
proteins
sequence_length
744
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000305|PubMed:34390643}; Multi-pass membrane protein {ECO:0000269|PubMed:34390643}. Note=Localized at the lateral cell membrane of outer hair cells (By similarity). Alters profoundly the shape of its surrounding lipid bilayer (PubMed:34390643). {ECO:0000250, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643}.
uniprot
proteins
transmembrane_region
TRANSMEM 76..105; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 109..126; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 138..151; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 169..196; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 207..230; /note="Helical; Name=5a"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 259..282; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 292..307; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 333..367; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 371..388; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 397..406; /note="Helical; Name=10"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 411..432; /note="Helical; Name=11"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 437..464; /note="Helical; Name=12"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 466..481; /note="Helical; Name=13"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3"; TRANSMEM 484..504; /note="Helical; Name=14"; /evidence="ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
uniprot
proteins