ID B5TGH8_9CHIR Unreviewed; 741 AA.
AC B5TGH8;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
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|EMBL:ACI02079.1};
OS Rhinolophus luctus (Woolly horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=337453 {ECO:0000313|EMBL:ACI02079.1};
RN [1] {ECO:0000313|EMBL:ACI02079.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18776049; DOI=10.1073/pnas.0802097105;
RA Li G., Wang J., Rossiter S.J., Jones G., Cotton J.A., Zhang S.;
RT "The hearing gene Prestin reunites echolocating bats.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13959-13964(2008).
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 EMBL; EU914933; ACI02079.1; -; mRNA.
DR AlphaFoldDB; B5TGH8; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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 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..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 178..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 260..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 438..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 469..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 525..713
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 741 AA; 80920 MW; E558F8165F4F9B1D CRC64;
MDHAEETELL AAAERYYVER PIFSHLVLQE RLHKKDKISD SIGDKLKQAF TCTPKKIRNI
IYMFLPITKW LPAYNFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV
IMYCFFGTSR HVSIGPFAVI SLMIGGVAVR LVPDDIAVPG GVNATNGTEF RDALRVKVAM
SVTLLAGIIQ FCLGICRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
TGISAGFGLH ESYNVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
LANKHGYQVD GNQELIALGL CNSTGSLFQT FAISCSLSRS LVQEGTGGKT QLAGCLASLM
ILMVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWKTSKIELT IWLSTFVSSL
FLGLDYGLIT AVIIALMTVI YRTQSPTYTV LGQLPDTDVY IDIDAYEEVK EISGIKIFQI
NAPIYYANSD LYSSALKRKT GVNPAFILGA RRKAMKKYAK EGGNINIANA TDVKADAEVD
AEDGTKPEEE GDEVKYPPVV IKSTFPEELQ RFMPPLQNIH TVILDFTQVN FIDSVGVKTL
QGIVKEYGDV GIYVYLAGCS AQVISDLTQN RFFENPALLD LLFHSIHDAV LGSLVREALE
EKEVAATMPQ EDSEPNATPD V
//
