ID S26A5_HUMAN Reviewed; 744 AA. AC P58743; Q496J2; Q7Z7F3; Q86UF8; Q86UF9; Q86UG0; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=Prestin {ECO:0000303|PubMed:12719379}; DE AltName: Full=Solute carrier family 26 member 5; GN Name=SLC26A5 {ECO:0000312|HGNC:HGNC:9359}; Synonyms=PRES; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND INVOLVEMENT IN RP DFNB61. RC TISSUE=Organ of Corti; RX PubMed=12719379; DOI=10.1093/hmg/ddg127; RA Liu X.Z., Ouyang X.M., Xia X.J., Zheng J., Pandya A., Li F., Du L.L., RA Welch K.O., Petit C., Smith R.J.H., Webb B.T., Yan D., Arnos K.S., RA Corey D., Dallos P., Nance W.E., Chen Z.-Y.; RT "Prestin, a cochlear motor protein, is defective in non-syndromic hearing RT loss."; RL Hum. Mol. Genet. 12:1155-1162(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RA Mount D.B.; RT "Sequence of an alternatively spliced isoform of prestin (SLC26A5e)."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] {ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) IN COMPLEX WITH RP CHOLESTEROL; CHLORIDE ION AND SALICYLATE, SUBUNIT, MUTAGENESIS OF PHE-101, RP DOMAIN, TOPOLOGY, AND SUBCELLULAR LOCATION. RX PubMed=34390643; DOI=10.1016/j.cell.2021.07.034; RA Ge J., Elferich J., Dehghani-Ghahnaviyeh S., Zhao Z., Meadows M., RA von Gersdorff H., Tajkhorshid E., Gouaux E.; RT "Molecular mechanism of prestin electromotive signal amplification."; RL Cell 184:4669-4679.e13(2021). CC -!- FUNCTION: Voltage-sensitive motor protein that drives outer hair cell CC (OHC) electromotility (eM) and participates in sound amplification in CC the hearing organ (By similarity). Converts changes in the CC transmembrane electric potential into mechanical displacements CC resulting in the coupling of its expansion to movement of a charged CC voltage sensor across the lipid membrane (By similarity). The nature of CC the voltage sensor is not completely clear, and two models compete. In CC the first model, acts as an incomplete transporter where intracellular CC chloride anion acts as extrinsic voltage sensor that drives CC conformational change in the protein which is sufficient to produce a CC length change in the plane of the membrane and hence in the length of CC the OHC (By similarity). The second model in which multiple charged CC amino acid residues are distributed at the intracellular and CC extracellular membrane interfaces that form an intrinsic voltage CC sensor, whose movement produces the non-linear capacitance (NLC) CC (PubMed:34390643). However, the effective voltage sensor may be the CC result of a hybrid voltage sensor, assembled from intrinsic charge CC (charged residues) and extrinsic charge (bound anion) (By similarity). CC Notably, binding of anions to the anion-binding pocket partially CC neutralizes the intrinsic positive charge rather than to form an CC electrically negative sensor, therefore remaining charge may serve as CC voltage sensor that, after depolarization, moves from down (expanded CC state) to up (contracted) conformation, which is accompanied by an CC eccentric contraction of the intermembrane cross-sectional area of the CC protein as well as a major increase in the hydrophobic thickness of the CC protein having as consequences the plasma membrane thickening and the CC cell contraction after membrane depolarization (PubMed:34390643). The CC anion-binding pocket transits from the inward-open (Down) state, where CC it is exposed toward the intracellular solvent in the absence of anion, CC to the occluded (Up) state upon anion binding (PubMed:34390643). CC Salicylate competes for the anion-binding site and inhibits the CC voltage-sensor movement, and therefore inhibits the charge transfer and CC electromotility by displacing Cl(-) from the anion-binding site and by CC preventing the structural transitions to the contracted state CC (PubMed:34390643). In addition, can act as a weak Cl(-)/HCO3(-) CC antiporter across the cell membrane and so regulate the intracellular CC pH of the outer hair cells (OHCs), while firstly found as being unable CC to mediate electrogenic anion transport (By similarity). Moreover, CC supports a role in cardiac mechanical amplification serving as an CC elastic element to enhance the actomyosin- based sarcomere contraction CC system (By similarity). {ECO:0000250|UniProtKB:D7PC76, CC ECO:0000250|UniProtKB:Q99NH7, ECO:0000250|UniProtKB:Q9EPH0, CC ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 CC hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9EPH0}; CC -!- SUBUNIT: Homodimer (PubMed:34390643). Interacts (via STAS domain) with CC CALM; this interaction is calcium-dependent and the STAS domain CC interacts with only one lobe of CALM which is an elongated conformation CC (By similarity). {ECO:0000250|UniProtKB:A0FKN5, CC ECO:0000250|UniProtKB:Q9EPH0, ECO:0000269|PubMed:34390643}. CC -!- INTERACTION: CC P58743-6; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-18029942, EBI-988826; CC -!- SUBCELLULAR LOCATION: Lateral cell membrane CC {ECO:0000305|PubMed:34390643}; Multi-pass membrane protein CC {ECO:0000269|PubMed:34390643}. Note=Localized at the lateral cell CC membrane of outer hair cells (By similarity). Alters profoundly the CC shape of its surrounding lipid bilayer (PubMed:34390643). {ECO:0000250, CC ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:34390643}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=SLC26A5a; CC IsoId=P58743-1; Sequence=Displayed; CC Name=2; Synonyms=SLC26A5b; CC IsoId=P58743-2; Sequence=VSP_010194, VSP_010195; CC Name=3; Synonyms=SLC26A5c; CC IsoId=P58743-3; Sequence=VSP_010192, VSP_010193; CC Name=4; Synonyms=SLC26A5d; CC IsoId=P58743-4; Sequence=VSP_010190, VSP_010191; CC Name=5; CC IsoId=P58743-5; Sequence=VSP_043153; CC Name=6; CC IsoId=P58743-6; Sequence=VSP_043153, VSP_047640; CC -!- DOMAIN: The STAS domain mediates dimerization, with both STAS domains CC latched onto each other in a domain-swapped manner (PubMed:34390643). CC The N-terminus domain is involved in dimerization such that each N- CC terminus domain embraces both STAS domains (PubMed:34390643). The STAS CC domain harbors a unique anion-binding site important for the fine CC regulation of the high-frequency electromotile properties (By CC similarity). The transmembrane domain consists of 14 transmembrane CC segments organized in a 7(+)7 inverted repeat architecture that can be CC divided into two main helix bundles, the ''core'' domain and the CC ''gate'' domain (PubMed:34390643). The transmembrane regions are CC domain-swapped with the STAS domain containing N- and C-terminal CC cytoplasmic domains (By similarity). The STAS domain mediates CALM CC binding CALM (By similarity). {ECO:0000250|UniProtKB:D7PC76, CC ECO:0000250|UniProtKB:Q9EPH0, ECO:0000269|PubMed:34390643}. CC -!- DISEASE: Deafness, autosomal recessive, 61 (DFNB61) [MIM:613865]: A CC form of non-syndromic sensorineural hearing loss. Sensorineural CC deafness results from damage to the neural receptors of the inner ear, CC the nerve pathways to the brain, or the area of the brain that receives CC sound information. {ECO:0000269|PubMed:12719379}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Pump up the volume - Issue CC 22 of May 2002; CC URL="https://web.expasy.org/spotlight/back_issues/022"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF523354; AAP31417.1; -; mRNA. DR EMBL; AY256823; AAP31532.1; -; mRNA. DR EMBL; AY256824; AAP31533.1; -; mRNA. DR EMBL; AY256825; AAP31534.1; -; mRNA. DR EMBL; AY289134; AAP43686.1; -; mRNA. DR EMBL; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093701; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC100833; AAI00834.1; -; mRNA. DR CCDS; CCDS43629.1; -. [P58743-3] DR CCDS; CCDS43630.1; -. [P58743-2] DR CCDS; CCDS55150.1; -. [P58743-5] DR CCDS; CCDS5732.1; -. [P58743-4] DR CCDS; CCDS5733.1; -. [P58743-1] DR RefSeq; NP_001161434.1; NM_001167962.1. [P58743-5] DR RefSeq; NP_001308716.1; NM_001321787.1. DR RefSeq; NP_945350.1; NM_198999.2. [P58743-1] DR RefSeq; NP_996766.1; NM_206883.2. [P58743-2] DR RefSeq; NP_996767.1; NM_206884.2. [P58743-3] DR RefSeq; NP_996768.1; NM_206885.2. [P58743-4] DR RefSeq; XP_011514472.1; XM_011516170.2. [P58743-1] DR PDB; 7LGU; EM; 2.30 A; A/B=1-744. DR PDB; 7LGW; EM; 2.70 A; A/B=1-744. DR PDB; 7LH2; EM; 3.43 A; A/B=1-744. DR PDB; 7LH3; EM; 4.30 A; A/B=1-744. DR PDBsum; 7LGU; -. DR PDBsum; 7LGW; -. DR PDBsum; 7LH2; -. DR PDBsum; 7LH3; -. DR AlphaFoldDB; P58743; -. DR EMDB; EMD-23329; -. DR EMDB; EMD-23331; -. DR EMDB; EMD-23334; -. DR EMDB; EMD-23335; -. DR SMR; P58743; -. DR BioGRID; 131988; 1. DR IntAct; P58743; 1. DR STRING; 9606.ENSP00000304783; -. DR TCDB; 2.A.53.2.19; the sulfate permease (sulp) family. DR GlyCosmos; P58743; 2 sites, No reported glycans. DR GlyGen; P58743; 2 sites. DR iPTMnet; P58743; -. DR PhosphoSitePlus; P58743; -. DR BioMuta; SLC26A5; -. DR DMDM; 20139418; -. DR jPOST; P58743; -. DR MassIVE; P58743; -. DR PaxDb; 9606-ENSP00000304783; -. DR PeptideAtlas; P58743; -. DR Antibodypedia; 31198; 162 antibodies from 26 providers. DR DNASU; 375611; -. DR Ensembl; ENST00000306312.8; ENSP00000304783.3; ENSG00000170615.16. [P58743-1] DR Ensembl; ENST00000339444.10; ENSP00000342396.6; ENSG00000170615.16. [P58743-2] DR Ensembl; ENST00000356767.8; ENSP00000349210.4; ENSG00000170615.16. [P58743-4] DR Ensembl; ENST00000393723.2; ENSP00000377324.1; ENSG00000170615.16. [P58743-6] DR Ensembl; ENST00000393730.5; ENSP00000377331.1; ENSG00000170615.16. [P58743-5] DR Ensembl; ENST00000393735.6; ENSP00000377336.2; ENSG00000170615.16. [P58743-3] DR Ensembl; ENST00000432958.6; ENSP00000389733.2; ENSG00000170615.16. [P58743-5] DR GeneID; 375611; -. DR KEGG; hsa:375611; -. DR MANE-Select; ENST00000306312.8; ENSP00000304783.3; NM_198999.3; NP_945350.1. DR UCSC; uc003vbt.3; human. [P58743-1] DR AGR; HGNC:9359; -. DR CTD; 375611; -. DR DisGeNET; 375611; -. DR GeneCards; SLC26A5; -. DR HGNC; HGNC:9359; SLC26A5. DR HPA; ENSG00000170615; Not detected. DR MalaCards; SLC26A5; -. DR MIM; 604943; gene. DR MIM; 613865; phenotype. DR neXtProt; NX_P58743; -. DR OpenTargets; ENSG00000170615; -. DR Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB. DR PharmGKB; PA33731; -. DR VEuPathDB; HostDB:ENSG00000170615; -. DR eggNOG; KOG0236; Eukaryota. DR GeneTree; ENSGT01070000253775; -. DR HOGENOM; CLU_003182_9_4_1; -. DR InParanoid; P58743; -. DR OMA; WNENQDL; -. DR OrthoDB; 1067648at2759; -. DR PhylomeDB; P58743; -. DR TreeFam; TF313784; -. DR PathwayCommons; P58743; -. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; P58743; -. DR BioGRID-ORCS; 375611; 10 hits in 1151 CRISPR screens. DR ChiTaRS; SLC26A5; human. DR GeneWiki; Prestin; -. DR GenomeRNAi; 375611; -. DR Pharos; P58743; Tbio. DR PRO; PR:P58743; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P58743; Protein. DR Bgee; ENSG00000170615; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 59 other cell types or tissues. DR ExpressionAtlas; P58743; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB. DR GO; GO:0120249; C:lateral wall of outer hair cell; IEA:Ensembl. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; ISS:UniProtKB. DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl. DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB. DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB. DR GO; GO:0090102; P:cochlea development; IEA:Ensembl. DR GO; GO:0015755; P:fructose transmembrane transport; IEA:Ensembl. DR GO; GO:0034766; P:negative regulation of monoatomic ion transmembrane transport; IEA:Ensembl. DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl. DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl. DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl. DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl. DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl. DR GO; GO:0009751; P:response to salicylic acid; IEA:Ensembl. DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1. DR Gene3D; 3.30.750.24; STAS domain; 1. DR InterPro; IPR018045; S04_transporter_CS. DR InterPro; IPR011547; SLC26A/SulP_dom. DR InterPro; IPR001902; SLC26A/SulP_fam. DR InterPro; IPR002645; STAS_dom. DR InterPro; IPR036513; STAS_dom_sf. DR NCBIfam; TIGR00815; sulP; 1. DR PANTHER; PTHR11814:SF32; PRESTIN; 1. DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1. DR Pfam; PF01740; STAS; 1. DR Pfam; PF00916; Sulfate_transp; 1. DR SUPFAM; SSF52091; SpoIIaa-like; 1. DR PROSITE; PS01130; SLC26A; 1. DR PROSITE; PS50801; STAS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell shape; Deafness; KW Glycoprotein; Hearing; Membrane; Motor protein; Non-syndromic deafness; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..744 FT /note="Prestin" FT /id="PRO_0000080167" FT TOPO_DOM 1..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 76..105 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 106..108 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 109..126 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 127..137 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 138..151 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 152..168 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 169..196 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 197..206 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 207..230 FT /note="Helical; Name=5a" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 231..241 FT /note="Extracellular" FT /evidence="ECO:0000305" FT INTRAMEM 242..253 FT /note="Helical; Name=5b" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 254..258 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 259..282 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 283..291 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 292..307 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 308..332 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 333..367 FT /note="Helical; Name=8" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 368..370 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 371..388 FT /note="Helical; Name=9" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 389..396 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 397..406 FT /note="Helical; Name=10" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 407..410 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 411..432 FT /note="Helical; Name=11" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 433..436 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 437..464 FT /note="Helical; Name=12" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 465 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 466..481 FT /note="Helical; Name=13" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 482..483 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 484..504 FT /note="Helical; Name=14" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, FT ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3" FT TOPO_DOM 505..744 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 525..713 FT /note="STAS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198" FT REGION 505..718 FT /note="Extended region for STAS domain" FT /evidence="ECO:0000250|UniProtKB:Q9EPH0" FT REGION 718..744 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 158..168 FT /note="Involved in motor function" FT /evidence="ECO:0000250|UniProtKB:Q9JKQ2" FT BINDING 398 FT /ligand="salicylate" FT /ligand_id="ChEBI:CHEBI:30762" FT /ligand_note="antagonist" FT /evidence="ECO:0000269|PubMed:34390643, FT ECO:0007744|PDB:7LH2" FT SITE 398 FT /note="Controls the electromotile activity" FT /evidence="ECO:0000250|UniProtKB:A0FKN5, FT ECO:0000250|UniProtKB:Q9EPH0" FT SITE 399 FT /note="Contributes to anion binding" FT /evidence="ECO:0000250|UniProtKB:Q9EPH0" FT CARBOHYD 163 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 325..335 FT /note="LLPPANPDTSL -> FHTEMTRRWRP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010190" FT VAR_SEQ 336..744 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010191" FT VAR_SEQ 438..469 FT /note="Missing (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_043153" FT VAR_SEQ 506..516 FT /note="PSYKVLGKLPE -> FHTEMTRRWRP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010192" FT VAR_SEQ 517..744 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010193" FT VAR_SEQ 595 FT /note="A -> ATQ (in isoform 6)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_047640" FT VAR_SEQ 682..685 FT /note="QVVN -> FIQR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010194" FT VAR_SEQ 686..744 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12719379" FT /id="VSP_010195" FT MUTAGEN 101 FT /note="F->Y: Decreases salicylate inhibition." FT /evidence="ECO:0000269|PubMed:34390643" FT STRAND 15..21 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 25..30 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 42..48 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 54..64 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:7LGU" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 76..104 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 109..115 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 118..126 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 138..151 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 169..195 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 207..224 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 226..230 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 242..252 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 259..281 FT /evidence="ECO:0007829|PDB:7LGU" FT TURN 282..285 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 292..307 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 336..365 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 371..387 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 397..405 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 412..426 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 437..447 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 449..453 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 454..456 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 457..464 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 466..481 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 486..504 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 508..513 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:7LGU" FT TURN 523..525 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 535..542 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 564..578 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 627..630 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 641..645 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 654..669 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 673..678 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 681..689 FT /evidence="ECO:0007829|PDB:7LGU" FT TURN 690..693 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 696..701 FT /evidence="ECO:0007829|PDB:7LGU" FT STRAND 702..705 FT /evidence="ECO:0007829|PDB:7LGU" FT HELIX 706..724 FT /evidence="ECO:0007829|PDB:7LGU" SQ SEQUENCE 744 AA; 81264 MW; 9E64BE6DB2DC065E CRC64; MDHAEENEIL AATQRYYVER PIFSHPVLQE RLHTKDKVPD SIADKLKQAF TCTPKKIRNI IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPI FGLYSSFYPV IMYCFLGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG TGISAGFNLK ESYNVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT LANKHGYQVD GNQELIALGL CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGKLPETDVY IDIDAYEEVK EIPGIKIFQI NAPIYYANSD LYSNALKRKT GVNPAVIMGA RRKAMRKYAK EVGNANMANA TVVKADAEVD GEDATKPEEE DGEVKYPPIV IKSTFPEEMQ RFMPPGDNVH TVILDFTQVN FIDSVGVKTL AGIVKEYGDV GIYVYLAGCS AQVVNDLTRN RFFENPALWE LLFHSIHDAV LGSQLREALA EQEASAPPSQ EDLEPNATPA TPEA //