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Database: UniProt
Entry: S26A5_RAT
LinkDB: S26A5_RAT
Original site: S26A5_RAT 
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
//
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