S26A5_MERUN
ID S26A5_MERUN Reviewed; 744 AA.
AC Q9JKQ2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Prestin;
DE AltName: Full=Solute carrier family 26 member 5;
GN Name=SLC26A5; Synonyms=PRES;
OS Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Organ of Corti;
RX PubMed=10821263; DOI=10.1038/35012009;
RA Zheng J., Shen W., He D.Z.Z., Long K.B., Madison L.D., Dallos P.;
RT "Prestin is the motor protein of cochlear outer hair cells.";
RL Nature 405:149-155(2000).
RN [2]
RP TOPOLOGY.
RX PubMed=11435925; DOI=10.1097/00001756-200107030-00032;
RA Zheng J., Long K.B., Shen W., Madison L.D., Dallos P.;
RT "Prestin topology: localization of protein epitopes in relation to the
RT plasma membrane.";
RL NeuroReport 12:1929-1935(2001).
CC -!- FUNCTION: Motor protein that converts auditory stimuli to length
CC changes in outer hair cells and mediates sound amplification in the
CC mammalian hearing organ. Prestin is a bidirectional voltage-to-force
CC converter, it can operate at microsecond rates. It uses cytoplasmic
CC anions as extrinsic voltage sensors, probably chloride and bicarbonate.
CC After binding to a site with millimolar affinity, these anions are
CC translocated across the membrane in response to changes in the
CC transmembrane voltage. They move towards the extracellular surface
CC following hyperpolarization, and towards the cytoplasmic side in
CC response to depolarization. As a consequence, this translocation
CC triggers conformational changes in the protein that ultimately alter
CC its surface area in the plane of the plasma membrane. The area
CC decreases when the anion is near the cytoplasmic face of the membrane
CC (short state), and increases when the ion has crossed the membrane to
CC the outer surface (long state). So, it acts as an incomplete
CC transporter. It swings anions across the membrane, but does not allow
CC these anions to dissociate and escape to the extracellular space.
CC Salicylate, an inhibitor of outer hair cell motility, acts as
CC competitive antagonist at the prestin anion-binding site (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Note=Basolateral wall of outer hair cells.
CC -!- TISSUE SPECIFICITY: Highly expressed in mature outer hair cells, but
CC not in inner hair cells or other cells of the basilar membrane and the
CC organ of Corti.
CC -!- DEVELOPMENTAL STAGE: Detected in the organ of Corti as early as 6 days
CC after birth; levels increase up to day 20, concomitant with the
CC development of high sensitivity hearing.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Pump up the volume - Issue
CC 22 of May 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/022";
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DR EMBL; AF230376; AAF71715.1; -; mRNA.
DR PDB; 7SUN; EM; 3.60 A; A/B=1-744.
DR PDBsum; 7SUN; -.
DR AlphaFoldDB; Q9JKQ2; -.
DR SMR; Q9JKQ2; -.
DR PRIDE; Q9JKQ2; -.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR030282; Prestin.
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 PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF32; PTHR11814:SF32; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell shape; Glycoprotein; Hearing; Membrane;
KW Motor protein; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Prestin"
FT /id="PRO_0000080168"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 525..713
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 717..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 744 AA; 81419 MW; 1CDF66589DAACBBC CRC64;
MDHAEENEIP VATQKYHVER PIFSHPVLQE RLHVKDKVSE 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
TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM
ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL
FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI
NAPIYYANSD LYSNALKRKT GVNPALIMGA RRKAMRKYAK EVGNANIANA AVVKVDGEVD
GENATKPEEE DDEVKYPPIV IKTTFPEELQ RFMPQTENVH TIILDFTQVN FIDSVGVKTL
AVMVKEYGDV GIYVYLAGCS PQVVNDLTRN RFFENPALKE LLFHSIHDAV LGSHVREAMA
EQEASAPPPQ DDMEPNATPT TPEA
