ID G3VPM6_SARHA Unreviewed; 747 AA.
AC G3VPM6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:ENSSHAP00000005131.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000005131.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000005131.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000005131.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3VPM6; -.
DR STRING; 9305.ENSSHAP00000005131; -.
DR Ensembl; ENSSHAT00000005182.2; ENSSHAP00000005131.1; ENSSHAG00000004489.2.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01070000253775; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; G3VPM6; -.
DR OMA; WNENQDL; -.
DR TreeFam; TF313784; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
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: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:UP000007648};
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..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 213..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 251..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 339..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 376..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 440..457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 477..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 526..719
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 581..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 81648 MW; 0F48E664B0B15971 CRC64;
MDHTQENEIL IATQTYCVER PIYSYPALHG KLHKKDKVSD PIGDKIKRAL SCTPKKIRNI
IYMFLPICKW LPAYKPREYV FGDFVSGIST GVLHLPQGLA FAMLAAVPPV FGLYSSFYPV
ILYCFFGTSR HVSIGPFAVI SLMIGGVAVR LVPDDMYVGG GGANSTNSTE ERDAMRVKVA
MSVTLLSGII QFCLGVLRFG FVAIYLTEPL VRGFTTAAAV HVFTSMLKYL FGVKTKRHSG
PFSVVYSTLA VIANVKKLNI CSLVVGLMCF ALLLGGKEFN ERFKNKLPAP IPLEIVAVII
GTGISAGFNL EESYKVDVVG SLPLGLLAPA TPDSSLFHLV YVDAIAIAIV GFSVTISMAK
IFAVKHGYQV DGNQELIALG ICNTIGSLFQ TFSISCSLSR SLVQESTGGN TQLAGCLASL
LILLVILAIG FLFESLPQAV LSAIVIVNLK GMFMQFSDLP FFWRTSKIEL TIWLTTFVSS
LFLGLDYGLI TAVIIALMTV IYRTQSPTYT VLGQLPNTDV YIDIDAYEEV KEHPGIKIFQ
INAPIYYANS DLYSNALSRK TGVNPALIMA ARRKVLKKHA KELGTKGKPQ SSVVKVDEDA
ETGGEEDAKQ EEQIEENAKP VTIDSLVQKT FPPELERFLP PGPNVHTMIL DFSQVNFIDS
VGVKTVAGIL KEYGDVGIYV YLAACSVQVV NDLTRNRFFE NPCVKELLFH SIHDAVLGAK
VREALAQQEA LAEPPEEDSE PIIDPET
//
