true2002-03-272024-03-27171S26A5_MOUSEExpression of prestin, a membrane motor protein, in the mammalian auditory and vestibular periphery.Dougherty G.W.Kachar B.doi:10.1016/s0378-5955(03)00192-82003Hear. Res.18427-40NUCLEOTIDE SEQUENCE [MRNA]SUBCELLULAR LOCATIONTISSUE SPECIFICITYC57BL/6JOrgan of CortiGenomic characterization and expression of mouse prestin, the motor protein of outer hair cells.Zheng J.Long K.B.Matsuda K.Madison L.D.Ryan A.Dallos P.D.doi:10.1007/s00335-002-2227-y2003Mamm. Genome1487-96NUCLEOTIDE SEQUENCE [MRNA]SUBCELLULAR LOCATIONTISSUE SPECIFICITYCBA/CaJMural R.J.Adams M.D.Myers E.W.Smith H.O.Venter J.C.2005-07EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.Liberman M.C.Gao J.He D.Z.Wu X.Jia S.Zuo J.doi:10.1038/nature010592002Nature419300-304FUNCTIONDISRUPTION PHENOTYPEExpression of prestin-homologous solute carrier (SLC26) in auditory organs of nonmammalian vertebrates and insects.Weber T.Gopfert M.C.Winter H.Zimmermann U.Kohler H.Meier A.Hendrich O.Rohbock K.Robert D.Knipper M.doi:10.1073/pnas.13305571002003Proc. Natl. Acad. Sci. U.S.A.1007690-7695TISSUE SPECIFICITYPrestin amplifies cardiac motor functions.Zhang X.D.Thai P.N.Ren L.Perez Flores M.C.Ledford H.A.Park S.Lee J.H.Sihn C.R.Chang C.W.Chen W.C.Timofeyev V.Zuo J.Chan J.W.Yamoah E.N.Chiamvimonvat N.doi:10.1016/j.celrep.2021.1090972021Cell Rep.35109097FUNCTIONTISSUE SPECIFICITYProtein Spotlight; Pump up the volume - Issue 22 of May 2002the sulfate permease (sulp) family2 sites, No reported glycans2 sites162 antibodies from 26 providersmouseSlc26a5Eukaryota3 hits in 76 CRISPR screensProteinExpressed in animal zygote and 12 other cell types or tissuesbaseline and differentialSTAS_anti-anti-sigma_factorsSTAS_SulP_like_sulfate_transporterSTAS domainS04_transporter_CSSLC26A/SulP_domSLC26A/SulP_famSTAS_domSTAS_dom_sfsulPPRESTINSULFATE TRANSPORTERSTASSulfate_transpSpoIIaa-likeSLC26ASTASMMPrestinSolute carrier family 26 member 5Slc26a5PresVoltage-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).Homodimer (By similarity). Interacts (via STAS domain) with CALM; this interaction is calcium-dependent and the STAS domain interacts with only one lobe of CALM which is an elongated conformation (By similarity).Localized at the outer hair cells (OHC) lateral plasma membrane (PubMed:14553901, PubMed:12584604). Alters profoundly the shape of its surrounding lipid bilayer (By similarity).Expressed in the outer hair cells (OHC) of the organ of Corti of the inner ear (PubMed:14553901, PubMed:12584604, PubMed:12782792). Also weak expression in brain and testis (PubMed:12584604). Very weakly expressed in heart, spleen, muscle and lactating mammary glands (PubMed:12584604). Expressed in cardiac myocytes (at protein level), both in the surface sarcolemma and along the t-tubule (PubMed:33951436). Weakly expressed in skeletal muscle cells (at protein level) (PubMed:33951436).The STAS domain mediates dimerization, with both STAS domains latched onto each other in a domain-swapped manner. The N-terminus domain is involved in dimerization such that each N-terminus domain embraces both STAS domains (By similarity). The STAS domain harbors a unique anion-binding site important for the fine regulation of the high-frequency electromotile properties (By similarity). The transmembrane domain consists of 14 transmembrane segments organized in a 7(+)7 inverted repeat architecture that can be divided into two main helix bundles, the ''core'' domain and the ''gate'' domain (By similarity). The transmembrane regions are domain-swapped with the STAS domain containing N- and C-terminal cytoplasmic domains (By similarity). The STAS domain mediates CALM binding CALM (By similarity).Homozygous knockout mice lacking Slc26a5 have no obvious developmental or behavioral abnormalities, except that, at one month, mice show small size difference compared to wild-type (PubMed:12239568). Mice show loss of electromotility, shortened outer hair cells (OHCs), and a reduction of hearing sensitivity of 40-60 dB (PubMed:12239568).Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.Prestin813371744Cytoplasmic75Helical; Name=176105Extracellular106108Helical; Name=2109126Cytoplasmic127137Helical; Name=3138151Extracellular152168Helical; Name=4169196Cytoplasmic197206Helical; Name=5a207230Extracellular231241Helical; Name=5b242253Extracellular254258Helical; Name=6259282Cytoplasmic283291Helical; Name=7292307Extracellular308332Helical; Name=8333367Cytoplasmic368370Helical; Name=9371388Extracellular389396Helical; Name=10397406Cytoplasmic407410Helical; Name=11411432Extracellular433436Helical; Name=12437464Cytoplasmic465Helical; Name=13466481Extracellular482483Helical; Name=14484504Cytoplasmic505STAS525713Extended region for STAS domain718Disordered720Involved in motor function158Polar residues729398Controls the electromotile activityContributes to anion binding399N-linked (GlcNAc...) asparagine163N-linked (GlcNAc...) asparagine166P469antagonist2011-07-2738133766546d6b9f94ddaeaaa3269cbfd29056MDHAEENEIPAETQRYYVERPIFSHPVLQERLHVKDKVTESIGDKLKQAFTCTPKKIRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLHESYSVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGICNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYKVLGQLPDTDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSSALKRKTGVNPALIMGARRKAMRKYAKEVGNANVANATVVKVDAEVDGENATKPEEEDDEVKFPPIVIKTTFPEELQRFLPQGENVHTVILDFTQVNFVDSVGVKTLAGIVKEYGDVGIYVYLAGCSPQVVNDLTRNNFFENPALKELLFHSIHDAVLGSQVREAMAEQEATASLPQEDMEPNATPTTPEAtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue