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Entry: F1SB52_PIG
LinkDB: F1SB52_PIG
Original site: F1SB52_PIG 
ID   F1SB52_PIG              Unreviewed;       740 AA.
AC   F1SB52;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   24-JAN-2024, entry version 82.
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:ENSSSCP00000016355.3,
GN   ECO:0000313|VGNC:VGNC:93030};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016355.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016355.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016355.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000016355.3}
RP   IDENTIFICATION.
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; F1SB52; -.
DR   PaxDb; 9823-ENSSSCP00000016355; -.
DR   Ensembl; ENSSSCT00000016803.4; ENSSSCP00000016355.3; ENSSSCG00000015425.4.
DR   VGNC; VGNC:93030; SLC26A5.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01070000253775; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   OMA; ICWGLVD; -.
DR   TreeFam; TF313784; -.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Bgee; ENSSSCG00000015425; Expressed in oocyte and 8 other cell types or tissues.
DR   ExpressionAtlas; F1SB52; baseline.
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   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:UP000008227};
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        184..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        212..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        256..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        334..354
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        475..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          524..712
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          716..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  81005 MW;  BD8327F491B8D8A8 CRC64;
     MDHAEENELL AATQRYYVER PIFSHPVLQE RLHKKDKISD SIGDKLKQAF TCTPKKIRNI
     IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV
     IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM
     SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
     FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
     TGISAGFNLK SYNVDVVGTL PLGLLPPANP DTSLFHLVYV DAIAIAIVGF SVTISMAKTL
     ANKHGYQVDG NQELIALGLC NSIGSLFQTF SISCSLSRSL VQEGTGGKTQ LAGCLASLMI
     LLVILATGFL FESLPQAVLS AIVIVNLKGM FMQFSDLPFF WRTSKIELTI WLTTFVSSLF
     LGLDYGLITA VIIALLTVIY RTQSPSYKVL GQLPETDVYI DIDAYEEVKE IPGIKIFQIN
     APIYYANSDL YSNALKRKTG VNPALIMGAR RKAMKKYAKE MGNANMANAA VVKVDAEVDG
     EDGTKPEEGE DEIKYPPIVI KSKFPEELQR FMPPGDNIHT IILDFTQVNF IDSVGVKTLA
     VMVKEYGDVG IYVYLAGCSA QVVDDLTRNR FFENPALREL LFHSIHDAVL GSQVREAMAE
     RDASAPPLQE DSEPNATPEA
//
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