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Database: UniProt
Entry: A0A384BP48_URSMA
LinkDB: A0A384BP48_URSMA
Original site: A0A384BP48_URSMA 
ID   A0A384BP48_URSMA        Unreviewed;       744 AA.
AC   A0A384BP48;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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:ENSUMAP00000018808,
GN   ECO:0000313|RefSeq:XP_040500280.1};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_040500280.1};
RN   [1] {ECO:0000313|Ensembl:ENSUMAP00000018808}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_040500280.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_040500280.1};
RG   RefSeq;
RL   Submitted (SEP-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   RefSeq; XP_008684368.1; XM_008686146.1.
DR   RefSeq; XP_040500280.1; XM_040644346.1.
DR   Ensembl; ENSUMAT00000022240.1; ENSUMAP00000018808.1; ENSUMAG00000013785.1.
DR   OMA; ICWGLVD; -.
DR   OrthoDB; 1067648at2759; -.
DR   Proteomes; UP000261680; Unplaced.
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:UP000261680};
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..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        411..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        439..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        476..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          525..713
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          718..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  81146 MW;  AF035391232DE4BE CRC64;
     MDHAEENEIL AASQRYYVER PIFSHPVLQE RLHKKDKISD SIGDKLKQAF TCTPKKIRNI
     IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV
     IMYCFLGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM
     SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
     FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
     TGISAGFNLK ESYDMDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
     LANKHGYQVD GNQELIALGL CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM
     ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL
     FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI
     NAPIYYANSD LYSSALKRKT GVNPAVIMGA RRKAMKKYAK EVGNANVANA NVVKVDAEVD
     GEDATKPEEE DDEVKYPPIV IKSTLPEELQ RFMPPGDNVH TIILDFTQVN FIDSVGVKTL
     AGIVKEYGDV GIYVYLAGCS AQVVNDLTQN RFFENPALKE LLFHSIHDAV LGSRLREALA
     EQEASAPAPQ EDSEPNATPA TPEA
//
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