GenomeNet

Database: UniProt
Entry: G1PCI8_MYOLU
LinkDB: G1PCI8_MYOLU
Original site: G1PCI8_MYOLU 
ID   G1PCI8_MYOLU            Unreviewed;       745 AA.
AC   G1PCI8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-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:ENSMLUP00000008129.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000008129.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000008129.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000008129.2}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAPE02058007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02058008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PCI8; -.
DR   STRING; 59463.ENSMLUP00000008129; -.
DR   Ensembl; ENSMLUT00000008921.2; ENSMLUP00000008129.2; ENSMLUG00000008900.2.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01070000253775; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   InParanoid; G1PCI8; -.
DR   OMA; ICWGLVD; -.
DR   TreeFam; TF313784; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0016328; C:lateral plasma membrane; 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: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:UP000001074};
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        335..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        378..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        414..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        442..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        479..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          528..716
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          723..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   745 AA;  81194 MW;  BC4E96272C72A89B CRC64;
     MDHAEETELL AAAQKYYVDR PIFSHLALQE ILHTKDKIPD SIGDKLKQAF TCTPKKIRNI
     IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV
     IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM
     SVTLLAGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
     FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
     TGISAGFSLH ESYNVDVVGS LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
     LGNKHGYQVD GNQMEKELIA LGLCNSIGSL FQTFAISCSL SRSLVQEGTG GKTQLAGCLA
     SLMILMVILA TGFLFESLPQ AVLSAIVIVN LKGMFMQFSD LPFFWRTSKI ELTIWLTTFV
     SSLFLGLDYG LITAVIIALM TVIYRTQSPS YKVLGQLPDT DVYIDIDAYE EVKEIPGIKI
     FQINAPIYYA NSDLYSSALK RKTGVNPALI MGARRKAMKK YAKEVGNANL ANATMIKADG
     EVDGEDATKT EEEDDEIKFP PVVIKTTIPE ELQRFMPPGD NVHTVILDFT QVNFIDSVGV
     KTLSGIVKEY GDVGIYVYLA GCSAQVVNDL TSNFFFENPA LKELLFHSIH DAVLGSQLRE
     ALAEQEALTP PPQEDAEPNA TQAEA
//
DBGET integrated database retrieval system