ID F6V6F2_ORNAN Unreviewed; 745 AA.
AC F6V6F2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Prestin {ECO:0000256|ARBA:ARBA00040148, ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Solute carrier family 26 member 5 {ECO:0000256|ARBA:ARBA00042390, ECO:0000256|RuleBase:RU362052};
GN Name=SLC26A5 {ECO:0000313|Ensembl:ENSOANP00000023682.2};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000023682.2, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000023682.2}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000023682.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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. Converts changes in the transmembrane electric
CC potential into mechanical displacements resulting in the coupling of
CC its expansion to movement of a charged voltage sensor across the lipid
CC membrane. The nature of the voltage sensor is not completely clear, and
CC two models compete. In the first model, acts as an incomplete
CC transporter where intracellular chloride anion acts as extrinsic
CC voltage sensor that drives conformational change in the protein which
CC is sufficient to produce a length change in the plane of the membrane
CC and hence in the length of the OHC. The second model in which multiple
CC charged 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 However, the effective voltage sensor may be the result of a hybrid
CC voltage sensor, assembled from intrinsic charge (charged residues) and
CC extrinsic charge (bound anion). Notably, binding of anions to the
CC anion-binding pocket partially neutralizes the intrinsic positive
CC charge rather than to form an electrically negative sensor, therefore
CC remaining charge may serve as voltage sensor that, after
CC depolarization, moves from down (expanded state) to up (contracted)
CC conformation, which is accompanied by an eccentric contraction of the
CC intermembrane cross-sectional area of the protein as well as a major
CC increase in the hydrophobic thickness of the protein having as
CC consequences the plasma membrane thickening and the cell contraction
CC after membrane depolarization. The anion-binding pocket transits from
CC the inward-open (Down) state, where it is exposed toward the
CC intracellular solvent in the absence of anion, to the occluded (Up)
CC state upon anion binding. Salicylate competes for the anion-binding
CC site and inhibits the voltage-sensor movement, and therefore inhibits
CC the charge transfer and electromotility by displacing Cl(-) from the
CC anion-binding site and by preventing the structural transitions to the
CC contracted state. 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. Moreover, supports a role in
CC cardiac mechanical amplification serving as an elastic element to
CC enhance the actomyosin- based sarcomere contraction system.
CC {ECO:0000256|RuleBase:RU362052}.
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:0000256|ARBA:ARBA00036219};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|RuleBase:RU362052}.
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DR AlphaFoldDB; F6V6F2; -.
DR STRING; 9258.ENSOANP00000023682; -.
DR Ensembl; ENSOANT00000023686.2; ENSOANP00000023682.2; ENSOANG00000015044.3.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01070000253775; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; F6V6F2; -.
DR OMA; ICWGLVD; -.
DR OrthoDB; 1067648at2759; -.
DR TreeFam; TF313784; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000015044; Expressed in ovary and 1 other cell type or tissue.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
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:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|RuleBase:RU362052};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hearing {ECO:0000256|ARBA:ARBA00022740, ECO:0000256|RuleBase:RU362052};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Motor protein {ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 99..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 173..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 256..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 337..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 438..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 475..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 524..717
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 596..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 81638 MW; 8DE8695DCC409DEC CRC64;
MDHGPEHEVL AATQRYCVER PIFSHQVLHG RLHKKEKVSE PIGDKIKQAL SCTPKKVKHI
IYRFLPICKW LPAYKPREYI VGDIVSGIST GVLQLPQGIA YALLAAVPPI FGLYSSFYPV
IMYTVFGTSR HISIGPFAVI SLMIGGVAVR LVPDDMFAGG MNSTNSTEER DHLRVKVAMS
VTLLSGIIQF FLGVLRFGFV AIYLTEPLVR GFTTAAAVHV FTSQLKYLLG VKTKRHSGPL
SVVYSTVAVV TNIKKLNIAS LVVGVLCFGI LLGGKEFNER FKKKLPAPIP LEFFAVVIGT
GVSAGLDLKE SYKLDVVGSL PLGLGTPAVP DASLFHLVYV DAIAIAIVGF SVTISMAKIF
AIKHGYQVDG NQELIALGIC NFFGSLFQTF SISCAISRSL VQEGTGGKTQ LAGCLASLMI
LLVILAAGFL FESLPQAVLA AIVIVNLKGM MMQFTDLPHF WRTSKIELTI WLTTFVSSLF
LGLDYGLITA VIIALMTVIY RTQSPRYRVL GQIPNTDVYC DVDAYEEVRE HPGIKIFQIN
APIYYANSDL YNNALRRKTG VNAAVIMAAR RKILKKHARE MKRTNKPKST VVKVVHDSEG
GGEGGAKQEI QNDEQSGKGP AEPIVQNTFP EELERFMPPG ANVHTIILDF TQVNFIDSVG
VKTLKGIIKE YGDVGIYVYV AGCSEQVVED LTRNKFFEKP SMKEMLFHSI YDAVLGCKVR
EALAQQAALA PPPQETTDQL DSPEP
//