Slc26a5
entrez
80979
canonical
uniprot
Q99NH7
canonical
ensembl
ENSMUSG00000029015
resolver
ensp
ENSMUSP00000030878
resolver
ensp
ENSMUSP00000110830
resolver
enst
ENSMUST00000030878
resolver
enst
ENSMUST00000115176
resolver
genesymbol
Slc26a5
resolver
genesymbol_syn
Pres
resolver
uniprot
F7BK71
resolver
uniprot
Q32MT6
resolver
uniprot
Q32MT7
resolver
uniprot
Q80ZB1
resolver
uniprot_entry
F7BK71_MOUSE
resolver
uniprot_entry
Q32MT6_MOUSE
resolver
uniprot_entry
Q32MT7_MOUSE
resolver
uniprot_entry
S26A5_MOUSE
resolver
uniprot_sec
Q80ZB1
resolver
amino_acid_sequence
MDHAEENEIPAETQRYYVERPIFSHPVLQERLHVKDKVTESIGDKLKQAFTCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLHESYSVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGICNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYKVLGQLPDTDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSSALKRKTGVNPALIMGARRKAMRKYAKEVGNANVANATVVKVDAEVDGENATKPEEEDDEVKFPPIVIKTTFPEELQRFLPQGENVHTVILDFTQVNFVDSVGVKTLAGIVKEYGDVGIYVYLAGCSPQVVNDLTRNNFFENPALKELLFHSIHDAVLGSQVREAMAEQEATASLPQEDMEPNATPTTPEA
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 (PubMed:12239568). 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 (PubMed:12239568). The nature of the voltage sensor is not completely clear, and two models compete (By similarity). 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) (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (PubMed:33951436). {ECO:0000250|UniProtKB:D7PC76, ECO:0000250|UniProtKB:P58743, ECO:0000250|UniProtKB:Q9EPH0, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:12239568, ECO:0000269|PubMed:33951436}.
uniprot
proteins
mass_dalton
81337
uniprot
proteins
protein_family
SLC26A/SulP transporter (TC 2.A.53) family
uniprot
proteins
pubmed
12239568
uniprot
proteins
pubmed
12584604
uniprot
proteins
pubmed
12782792
uniprot
proteins
pubmed
14553901
uniprot
proteins
pubmed
33951436
uniprot
proteins
sequence_length
744
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000269|PubMed:12584604, ECO:0000269|PubMed:14553901}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P58743}. Note=Localized at the outer hair cells (OHC) lateral plasma membrane (PubMed:12584604, PubMed:14553901). Alters profoundly the shape of its surrounding lipid bilayer (By similarity). {ECO:0000250|UniProtKB:P58743, ECO:0000269|PubMed:12584604, ECO:0000269|PubMed:14553901}.
uniprot
proteins
transmembrane_region
TRANSMEM 76..105; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 109..126; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 138..151; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 169..196; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 207..230; /note="Helical; Name=5a"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 259..282; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 292..307; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 333..367; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 371..388; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 397..406; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 411..432; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 437..464; /note="Helical; Name=12"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 466..481; /note="Helical; Name=13"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 484..504; /note="Helical; Name=14"; /evidence="ECO:0000250|UniProtKB:P58743
uniprot
proteins