Slc26a5
entrez
83819
canonical
uniprot
Q9EPH0
canonical
ensembl
ENSRNOG00000011616
resolver
ensembl
ENSRNOG00055021385
resolver
ensembl
ENSRNOG00060027095
resolver
ensembl
ENSRNOG00065017809
resolver
ensp
ENSRNOP00000015733
resolver
ensp
ENSRNOP00055029727
resolver
ensp
ENSRNOP00060039299
resolver
ensp
ENSRNOP00065023681
resolver
enst
ENSRNOT00000015733
resolver
enst
ENSRNOT00055036588
resolver
enst
ENSRNOT00060047228
resolver
enst
ENSRNOT00065029826
resolver
genesymbol
Slc26a5
resolver
genesymbol_syn
Pres
resolver
uniprot
Q9ERC6
resolver
uniprot_entry
S26A5_RAT
resolver
uniprot_sec
Q9ERC6
resolver
activity_regulation
ACTIVITY REGULATION: Salicylate, an inhibitor of outer hair cell motility, acts as a competitive antagonist at the prestin anion-binding site. {ECO:0000269|PubMed:11423665}.
uniprot
proteins
amino_acid_sequence
MDHAEENEIPAETQKYLVERPIFSHPVLQERLHVKDKVTDSIGDKLKQAFTCTPKKVRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLHESYSVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGICNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYTVLGQLPDTDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSSALKRKTGVNPAIIMGARRKAMRKYAKEVGNANIANATVVKVDAEVDGENATKPEEEDDEVKFPPIVIKTTFPEELQRFLPQGENIHTVILDFTQVNFMDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTSNRFFENPALKELLFHSIHDAVLGSQVREAMAEQETTVLPPQEDMEPNATPTTPEA
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:11125015, PubMed:11274441). 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:11125015, PubMed:11274441). 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 (PubMed:11423665). 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 (PubMed:24710176). 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) (PubMed:22063625, PubMed:22890707), while firstly found as being unable to mediate electrogenic anion transport (PubMed:17442754, PubMed:22063625, PubMed:22890707). 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:P58743, ECO:0000250|UniProtKB:Q99NH7, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11274441, ECO:0000269|PubMed:11423665, ECO:0000269|PubMed:17442754, ECO:0000269|PubMed:22063625, ECO:0000269|PubMed:22890707, ECO:0000269|PubMed:24710176}.
uniprot
proteins
mass_dalton
81279
uniprot
proteins
mutagenesis
MUTAGEN 104; /note="L->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 149; /note="V->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 154; /note="D->N: Shifts the voltage-sensitivity to more negative values."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 155; /note="D->N: Shifts the voltage-sensitivity to more negative values."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 169; /note="E->Q: No effect."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 177; /note="K->Q: No effect."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 197; /note="R->Q: Shifts the voltage-sensitivity to more negative values."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 202; /note="A->C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 233; /note="K->Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 235; /note="K->Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 236; /note="R->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 236; /note="R->Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 276; /note="K->C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 277; /note="E->Q: Shifts the voltage-sensitivity to slightly more positive values."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 281; /note="R->Q: No effect; when associated with Q-283 and Q-285."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 283; /note="K->Q: No effect; when associated with Q-218 and Q-285."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 285; /note="K->Q: No effect; when associated with Q-281 and Q-283."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 331; /note="P->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 332; /note="D->Q: No effect."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 342; /note="D->Q: Shifts the voltage-sensitivity to more positive values."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 359; /note="K->C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 389; /note="Q->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 398; /note="S->C: Does not affect anion-dependent electromotility-related charge movement. Strongly attenuates inhibition by oxalate of electromotility-related charge movement. Is sensible to intracellular thiol-reactive reagents. Is completely insensitive to both reagents applied to the extracellular face of the membrane. Strongly affects the interaction with oxalate."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 399; /note="R->C: Largely abolishes anion-dependent electromotility-related charge movement."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 399; /note="R->E: Fully abolishes anion-dependent electromotility-related charge movement."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 399; /note="R->K: Does not affect anion-dependent electromotility-related charge movement."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 399; /note="R->Q: Fully abolishes anion-dependent electromotility-related charge movement."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 399; /note="R->S: Does not affect anion-dependent electromotility-related charge movement. Abrogates salicylate inhibition of electromotility-related charge movement."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 408; /note="G->C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 409; /note="K->Q: No effect."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 431; /note="L->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 465; /note="S->C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 485; /note="D->C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents."; /evidence="ECO:0000269|PubMed:24710176"; MUTAGEN 557; /note="K->Q: No effect; when associated with Q-558 and Q-559."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 558; /note="R->Q: No effect; when associated with Q-557 and Q-559."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 559; /note="K->Q: No effect; when associated with Q-557 and Q-558."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 571; /note="R->Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 572; /note="R->Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577."; /evidence="ECO:0000269|PubMed:11423665"; MUTAGEN 577; /note="K->Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572."; /evidence="ECO:0000269|PubMed:11423665
uniprot
proteins
protein_family
SLC26A/SulP transporter (TC 2.A.53) family
uniprot
proteins
pubmed
11125015
uniprot
proteins
pubmed
11274441
uniprot
proteins
pubmed
11423665
uniprot
proteins
pubmed
11867734
uniprot
proteins
pubmed
12782792
uniprot
proteins
pubmed
17442754
uniprot
proteins
pubmed
20471983
uniprot
proteins
pubmed
22063625
uniprot
proteins
pubmed
22890707
uniprot
proteins
pubmed
24710176
uniprot
proteins
pubmed
26635354
uniprot
proteins
pubmed
33667636
uniprot
proteins
sequence_length
744
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11867734, ECO:0000305|PubMed:11274441}; Multi-pass membrane protein {ECO:0000269|PubMed:24710176}. Note=Lateral membrane of outer hair cells (PubMed:11125015, PubMed:11867734). Alters profoundly the shape of its surrounding lipid bilayer (By similarity). {ECO:0000250|UniProtKB:P58743, ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11867734}.
uniprot
proteins
transmembrane_region
TRANSMEM 76..104; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 109..126; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 138..149; /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..276; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 292..307; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P58743"; TRANSMEM 333..359; /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..431; /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 485..504; /note="Helical; Name=14"; /evidence="ECO:0000250|UniProtKB:P58743
uniprot
proteins