ID S26A5_RAT Reviewed; 744 AA.
AC Q9EPH0; Q9ERC6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=Prestin {ECO:0000303|PubMed:11274441};
DE AltName: Full=Solute carrier family 26 member 5;
GN Name=Slc26a5 {ECO:0000312|RGD:69334}; Synonyms=Pres;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Cochlea;
RX PubMed=11274441; DOI=10.1073/pnas.071613498;
RA Ludwig J., Oliver D., Frank G., Kloecker N., Gummer A.W., Fakler B.;
RT "Reciprocal electromechanical properties of rat prestin: the motor molecule
RT from rat outer hair cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4178-4183(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 249-668.
RC STRAIN=Sprague-Dawley;
RA Beisel K.W., Nelson N.C., Beisel C.L., Delimont D.C., He D.Z.Z.,
RA Fritzsch B.;
RT "Dynamic developmental expression of cochlear hair cell genes: prestin and
RT otoferlin.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY THYROID HORMONE.
RC STRAIN=Sprague-Dawley;
RX PubMed=11867734; DOI=10.1073/pnas.052609899;
RA Weber T., Zimmermann U., Winter H., Mack A., Koepschall I., Rohbock K.,
RA Zenner H.P., Knipper M.;
RT "Thyroid hormone is a critical determinant for the regulation of the
RT cochlear motor protein prestin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2901-2906(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11125015; DOI=10.1523/jneurosci.20-24-j0002.2000;
RA Belyantseva I.A., Adler H.J., Curi R., Frolenkov G.I., Kachar B.;
RT "Expression and localization of prestin and the sugar transporter GLUT-5
RT during development of electromotility in cochlear outer hair cells.";
RL J. Neurosci. 20:RC116-RC116(2000).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-154; ASP-155; GLU-169; LYS-177; ARG-197;
RP LYS-233; LYS-235; ARG-236; GLU-277; ARG-281; LYS-283; LYS-285; ASP-332;
RP ASP-342; LYS-409; LYS-557; ARG-558; LYS-559; ARG-571; ARG-572 AND LYS-577.
RX PubMed=11423665; DOI=10.1126/science.1060939;
RA Oliver D., He D.Z.Z., Kloecker N., Ludwig J., Schulte U., Waldegger S.,
RA Ruppersberg J.P., Dallos P., Fakler B.;
RT "Intracellular anions as the voltage sensor of prestin, the outer hair cell
RT motor protein.";
RL Science 292:2340-2343(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12782792; DOI=10.1073/pnas.1330557100;
RA Weber T., Gopfert M.C., Winter H., Zimmermann U., Kohler H., Meier A.,
RA Hendrich O., Rohbock K., Robert D., Knipper M.;
RT "Expression of prestin-homologous solute carrier (SLC26) in auditory organs
RT of nonmammalian vertebrates and insects.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7690-7695(2003).
RN [7]
RP FUNCTION.
RX PubMed=17442754; DOI=10.1073/pnas.0608583104;
RA Schaechinger T.J., Oliver D.;
RT "Nonmammalian orthologs of prestin (SLC26A5) are electrogenic
RT divalent/chloride anion exchangers.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7693-7698(2007).
RN [8]
RP FUNCTION.
RX PubMed=22063625; DOI=10.1113/jphysiol.2011.209577;
RA Schaenzler M., Fahlke C.;
RT "Anion transport by the cochlear motor protein prestin.";
RL J. Physiol. (Lond.) 590:259-272(2012).
RN [9]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=22890707; DOI=10.1113/jphysiol.2012.241448;
RA Mistrik P., Daudet N., Morandell K., Ashmore J.F.;
RT "Mammalian prestin is a weak Cl-/HCO(3)- electrogenic antiporter.";
RL J. Physiol. (Lond.) 590:5597-5610(2012).
RN [10]
RP FUNCTION, MUTAGENESIS OF LEU-104; VAL-149; ALA-202; ARG-236; LYS-276;
RP PRO-331; LYS-359; GLN-389; SER-398; ARG-399; GLY-408; LEU-431; SER-465 AND
RP ASP-485, SITE, AND TOPOLOGY.
RX PubMed=24710176; DOI=10.1038/ncomms4622;
RA Gorbunov D., Sturlese M., Nies F., Kluge M., Bellanda M., Battistutta R.,
RA Oliver D.;
RT "Molecular architecture and the structural basis for anion interaction in
RT prestin and SLC26 transporters.";
RL Nat. Commun. 5:3622-3622(2014).
RN [11]
RP INTERACTION WITH CALM, AND DOMAIN.
RX PubMed=33667636; DOI=10.1016/j.jsb.2021.107714;
RA Costanzi E., Coletti A., Zambelli B., Macchiarulo A., Bellanda M.,
RA Battistutta R.;
RT "Calmodulin binds to the STAS domain of SLC26A5 prestin with a calcium-
RT dependent, one-lobe, binding mode.";
RL J. Struct. Biol. 213:107714-107714(2021).
RN [12] {ECO:0007744|PDB:3LLO}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 505-563 AND 637-718, AND REGION.
RX PubMed=20471983; DOI=10.1016/j.jmb.2010.05.013;
RA Pasqualetto E., Aiello R., Gesiot L., Bonetto G., Bellanda M.,
RA Battistutta R.;
RT "Structure of the cytosolic portion of the motor protein prestin and
RT functional role of the STAS domain in SLC26/SulP anion transporters.";
RL J. Mol. Biol. 400:448-462(2010).
RN [13] {ECO:0007744|PDB:5EUS, ECO:0007744|PDB:5EUU, ECO:0007744|PDB:5EUW, ECO:0007744|PDB:5EUX, ECO:0007744|PDB:5EUZ}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 505-563 AND 637-718 IN COMPLEX
RP WITH CHLORIDE ION; BROMIDE ION; IODIDE ION; NITRATE ION AND THIOCYANATE
RP ION, AND DOMAIN.
RX PubMed=26635354; DOI=10.1042/bj20151089;
RA Lolli G., Pasqualetto E., Costanzi E., Bonetto G., Battistutta R.;
RT "The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding
RT site.";
RL Biochem. J. 473:365-370(2016).
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 (PubMed:11125015, PubMed:11274441). Converts changes
CC in the 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 (PubMed:11125015,
CC PubMed:11274441). The nature of the voltage sensor is not completely
CC clear, and two models compete. In the first model, acts as an
CC incomplete transporter where intracellular chloride anion acts as
CC extrinsic voltage sensor that drives conformational change in the
CC protein which is sufficient to produce a length change in the plane of
CC the membrane and hence in the length of the OHC (PubMed:11423665). The
CC second model in which multiple charged amino acid residues are
CC distributed at the intracellular and extracellular membrane interfaces
CC that form an intrinsic voltage sensor, whose movement produces the non-
CC linear capacitance (NLC) (By similarity). However, the effective
CC voltage sensor may be the result of a hybrid voltage sensor assembled
CC from intrinsic charge (charged residues) and extrinsic charge (bound
CC anion) (By similarity). Notably, binding of anions to the anion-binding
CC pocket partially neutralizes the intrinsic positive charge rather than
CC to form an electrically negative sensor, therefore remaining charge may
CC serve as voltage sensor that, after depolarization, moves from down
CC (expanded state) to up (contracted) conformation, which is accompanied
CC by an eccentric contraction of the intermembrane cross-sectional area
CC of the protein as well as a major increase in the hydrophobic thickness
CC of the protein having as consequences the plasma membrane thickening
CC and the cell contraction after membrane depolarization (By similarity).
CC The anion-binding pocket transits from the inward-open (Down) state,
CC where it is exposed toward the intracellular solvent in the absence of
CC anion, to the occluded (Up) state upon anion binding (PubMed:24710176).
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 (By
CC similarity). In addition, can act as a weak Cl(-)/HCO3(-) antiporter
CC across the cell membrane and so regulate the intracellular pH of the
CC outer hair cells (OHCs) (PubMed:22063625, PubMed:22890707), while
CC firstly found as being unable to mediate electrogenic anion transport
CC (PubMed:17442754) (PubMed:22890707, PubMed:17442754, PubMed:22063625).
CC Moreover, supports a role in cardiac mechanical amplification serving
CC as an elastic element to enhance the actomyosin- based sarcomere
CC contraction system (By similarity). {ECO:0000250|UniProtKB:D7PC76,
CC ECO:0000250|UniProtKB:P58743, ECO:0000250|UniProtKB:Q99NH7,
CC ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:11125015,
CC ECO:0000269|PubMed:11274441, ECO:0000269|PubMed:11423665,
CC ECO:0000269|PubMed:17442754, ECO:0000269|PubMed:22063625,
CC ECO:0000269|PubMed:22890707, ECO:0000269|PubMed:24710176}.
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:0000269|PubMed:22890707};
CC -!- ACTIVITY REGULATION: Salicylate, an inhibitor of outer hair cell
CC motility, acts as a competitive antagonist at the prestin anion-binding
CC site. {ECO:0000269|PubMed:11423665}.
CC -!- SUBUNIT: Homodimer (By similarity). 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 (PubMed:33667636). {ECO:0000250|UniProtKB:P58743,
CC ECO:0000269|PubMed:33667636}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000269|PubMed:11125015, ECO:0000269|PubMed:11867734,
CC ECO:0000305|PubMed:11274441}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24710176}. Note=Lateral membrane of outer hair
CC cells (PubMed:11125015, PubMed:11867734). Alters profoundly the shape
CC of its surrounding lipid bilayer (By similarity).
CC {ECO:0000250|UniProtKB:P58743, ECO:0000269|PubMed:11125015,
CC ECO:0000269|PubMed:11867734}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in outer hair cells of
CC cochleae (PubMed:11125015, PubMed:12782792) (at protein level)
CC (PubMed:11867734). Not detected in other cells of the organ of Corti
CC (PubMed:11125015). {ECO:0000269|PubMed:11125015,
CC ECO:0000269|PubMed:11867734, ECO:0000269|PubMed:12782792}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the outer hair cells in the cochlea
CC from day 7 onwards, including at day 12, at the onset of hearing in
CC rats (at protein level) (PubMed:11867734). Low levels are present in
CC newborn rats and up to day 6. Subsequently, levels increase strongly.
CC Adult levels are detected starting from day 9 in the basal turn of the
CC cochlea, from day 10-11 in the middle turn, and from day 12 in the
CC apical turn. {ECO:0000269|PubMed:11867734}.
CC -!- INDUCTION: Up-regulated in cochlea by thyroid hormone T3, perhaps
CC acting via thyroid hormone receptor (at protein level).
CC {ECO:0000269|PubMed:11867734}.
CC -!- DOMAIN: The STAS domain mediates dimerization, with both STAS domains
CC latched onto each other in a domain-swapped manner (By similarity). The
CC N-terminus domain is involved in dimerization such that each N-terminus
CC domain embraces both STAS domains (By similarity). The STAS domain
CC harbors a unique anion-binding site important for the fine regulation
CC of the high-frequency electromotile properties (PubMed:26635354). The
CC transmembrane domain consists of 14 transmembrane segments organized a
CC 7(+)7 inverted repeat architecture that can be divided into two main
CC helix bundles, the ''core'' domain and the ''gate'' domain
CC (PubMed:24710176). The transmembrane regions are domain-swapped with
CC the STAS domain containing N- and C-terminal cytoplasmic domains (By
CC similarity). The STAS domain mediates CALM binding CALM
CC (PubMed:33667636). {ECO:0000250|UniProtKB:D7PC76,
CC ECO:0000250|UniProtKB:P58743, ECO:0000250|UniProtKB:Q9JKQ2,
CC ECO:0000269|PubMed:24710176, ECO:0000269|PubMed:26635354,
CC ECO:0000269|PubMed:33667636}.
CC -!- MISCELLANEOUS: The anion-binding site that controls electromotility and
CC associated charge movement in mammalian corresponds to the central
CC binding site of the anion translocation pathway in non-mammalian.
CC {ECO:0000269|PubMed:24710176}.
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";
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DR EMBL; AJ303372; CAC21555.1; -; mRNA.
DR EMBL; AF315652; AAG30297.1; -; mRNA.
DR EMBL; AJ428404; CAD21439.1; -; Genomic_DNA.
DR RefSeq; NP_110467.1; NM_030840.1.
DR RefSeq; XP_017448406.1; XM_017592917.1.
DR PDB; 3LLO; X-ray; 1.57 A; A=505-563, A=637-718.
DR PDB; 5EUS; X-ray; 1.83 A; A=505-563, A=637-718.
DR PDB; 5EUU; X-ray; 1.87 A; A=505-563, A=637-718.
DR PDB; 5EUW; X-ray; 1.81 A; A=505-563, A=637-718.
DR PDB; 5EUX; X-ray; 2.04 A; A=505-563, A=637-718.
DR PDB; 5EUZ; X-ray; 2.40 A; A=505-563, A=637-718.
DR PDBsum; 3LLO; -.
DR PDBsum; 5EUS; -.
DR PDBsum; 5EUU; -.
DR PDBsum; 5EUW; -.
DR PDBsum; 5EUX; -.
DR PDBsum; 5EUZ; -.
DR AlphaFoldDB; Q9EPH0; -.
DR SMR; Q9EPH0; -.
DR STRING; 10116.ENSRNOP00000015733; -.
DR GlyCosmos; Q9EPH0; 2 sites, No reported glycans.
DR GlyGen; Q9EPH0; 2 sites.
DR iPTMnet; Q9EPH0; -.
DR PhosphoSitePlus; Q9EPH0; -.
DR PaxDb; 10116-ENSRNOP00000015733; -.
DR Ensembl; ENSRNOT00000015733.3; ENSRNOP00000015733.2; ENSRNOG00000011616.5.
DR Ensembl; ENSRNOT00055036588; ENSRNOP00055029727; ENSRNOG00055021385.
DR Ensembl; ENSRNOT00060047228; ENSRNOP00060039299; ENSRNOG00060027095.
DR Ensembl; ENSRNOT00065029826; ENSRNOP00065023681; ENSRNOG00065017809.
DR GeneID; 83819; -.
DR KEGG; rno:83819; -.
DR AGR; RGD:69334; -.
DR CTD; 375611; -.
DR RGD; 69334; Slc26a5.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01070000253775; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q9EPH0; -.
DR OMA; ICWGLVD; -.
DR OrthoDB; 1067648at2759; -.
DR PhylomeDB; Q9EPH0; -.
DR TreeFam; TF313784; -.
DR EvolutionaryTrace; Q9EPH0; -.
DR PRO; PR:Q9EPH0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011616; Expressed in testis.
DR Genevisible; Q9EPH0; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0120249; C:lateral wall of outer hair cell; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:RGD.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:RGD.
DR GO; GO:0098656; P:monoatomic anion transmembrane transport; IDA:RGD.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IDA:RGD.
DR GO; GO:0034766; P:negative regulation of monoatomic ion transmembrane transport; IDA:RGD.
DR GO; GO:0019532; P:oxalate transport; IDA:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:RGD.
DR GO; GO:0045793; P:positive regulation of cell size; IDA:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0035864; P:response to potassium ion; IEP:RGD.
DR GO; GO:0009751; P:response to salicylic acid; IEP:RGD.
DR GO; GO:1902074; P:response to salt; IEP:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR CDD; cd07043; STAS_anti-anti-sigma_factors; 1.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR DisProt; DP01937; -.
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; Cell membrane; Cell shape; Glycoprotein; Hearing; Membrane;
KW Motor protein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Prestin"
FT /id="PRO_0000080170"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 76..104
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 105..108
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 109..126
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 127..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 138..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 150..168
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 169..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 197..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 207..230
FT /note="Helical; Name=5a"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 231..241
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT INTRAMEM 242..253
FT /note="Helical; Name=5b"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 254..258
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 259..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 277..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 292..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 308..332
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 333..359
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 360..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 371..388
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 389..396
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 397..406
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 407..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 411..431
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 432..436
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 437..464
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 466..481
FT /note="Helical; Name=13"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 482..484
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24710176"
FT TRANSMEM 485..504
FT /note="Helical; Name=14"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT TOPO_DOM 505..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24710176"
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:0000269|PubMed:20471983,
FT ECO:0007744|PDB:3LLO"
FT REGION 720..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 COMPBIAS 729..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000250|UniProtKB:P58743"
FT SITE 398
FT /note="Controls the electromotile activity"
FT /evidence="ECO:0000269|PubMed:24710176"
FT SITE 399
FT /note="Contributes to anion binding"
FT /evidence="ECO:0000269|PubMed:24710176"
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 MUTAGEN 104
FT /note="L->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 149
FT /note="V->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 154
FT /note="D->N: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 155
FT /note="D->N: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 169
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 177
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 197
FT /note="R->Q: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 202
FT /note="A->C: Is only accessible to the intracellular side
FT application of thiol-reactive reagents. Is not affected by
FT thiol-reactive reagents extracellular side application."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 233
FT /note="K->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-235 and Q-236."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 235
FT /note="K->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-233 and Q-236."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 236
FT /note="R->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 236
FT /note="R->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-233 and Q-235."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 276
FT /note="K->C: Is only accessible to the intracellular side
FT application of thiol-reactive reagents. Is not affected by
FT thiol-reactive reagents extracellular side application."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 277
FT /note="E->Q: Shifts the voltage-sensitivity to slightly
FT more positive values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 281
FT /note="R->Q: No effect; when associated with Q-283 and Q-
FT 285."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 283
FT /note="K->Q: No effect; when associated with Q-218 and Q-
FT 285."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 285
FT /note="K->Q: No effect; when associated with Q-281 and Q-
FT 283."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 331
FT /note="P->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 332
FT /note="D->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 342
FT /note="D->Q: Shifts the voltage-sensitivity to more
FT positive values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 359
FT /note="K->C: Is only accessible to the intracellular side
FT application of thiol-reactive reagents. Is not affected by
FT thiol-reactive reagents extracellular side application."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 389
FT /note="Q->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 398
FT /note="S->C: Does not affect anion-dependent
FT electromotility-related charge movement. Strongly
FT attenuates inhibition by oxalate of electromotility-related
FT charge movement. Is sensible to intracellular thiol-
FT reactive reagents. Is completely insensitive to both
FT reagents applied to the extracellular face of the membrane.
FT Strongly affects the interaction with oxalate."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 399
FT /note="R->C: Largely abolishes anion-dependent
FT electromotility-related charge movement."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 399
FT /note="R->E: Fully abolishes anion-dependent
FT electromotility-related charge movement."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 399
FT /note="R->K: Does not affect anion-dependent
FT electromotility-related charge movement."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 399
FT /note="R->Q: Fully abolishes anion-dependent
FT electromotility-related charge movement."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 399
FT /note="R->S: Does not affect anion-dependent
FT electromotility-related charge movement. Abrogates
FT salicylate inhibition of electromotility-related charge
FT movement."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 408
FT /note="G->C: Is only accessible to the intracellular side
FT application of thiol-reactive reagents. Is not affected by
FT thiol-reactive reagents extracellular side application."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 409
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 431
FT /note="L->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 465
FT /note="S->C: Is only accessible to the intracellular side
FT application of thiol-reactive reagents. Is not affected by
FT thiol-reactive reagents extracellular side application."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 485
FT /note="D->C: Is accessible from the extracellular side
FT after extracellular application of thiol-reactive
FT reagents."
FT /evidence="ECO:0000269|PubMed:24710176"
FT MUTAGEN 557
FT /note="K->Q: No effect; when associated with Q-558 and Q-
FT 559."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 558
FT /note="R->Q: No effect; when associated with Q-557 and Q-
FT 559."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 559
FT /note="K->Q: No effect; when associated with Q-557 and Q-
FT 558."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 571
FT /note="R->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-572 and Q-
FT 577."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 572
FT /note="R->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-571 and Q-
FT 577."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 577
FT /note="K->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-571 and Q-
FT 572."
FT /evidence="ECO:0000269|PubMed:11423665"
FT CONFLICT 251
FT /note="L -> V (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="I -> M (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="R -> S (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="D -> G (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 662..663
FT /note="GI -> VM (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 654..668
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 690..693
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 696..701
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 706..712
FT /evidence="ECO:0007829|PDB:3LLO"
SQ SEQUENCE 744 AA; 81279 MW; E49E842CF7A3CD58 CRC64;
MDHAEENEIP AETQKYLVER PIFSHPVLQE RLHVKDKVTD SIGDKLKQAF TCTPKKVRNI
IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV
IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM
SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM
ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL
FLGLDYGLIT AVIIALLTVI YRTQSPSYTV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI
NAPIYYANSD LYSSALKRKT GVNPAIIMGA RRKAMRKYAK EVGNANIANA TVVKVDAEVD
GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENIH TVILDFTQVN FMDSVGVKTL
AGIVKEYGDV GIYVYLAGCS AQVVNDLTSN RFFENPALKE LLFHSIHDAV LGSQVREAMA
EQETTVLPPQ EDMEPNATPT TPEA
//