S26A5_MOUSE
ID S26A5_MOUSE Reviewed; 744 AA.
AC Q99NH7; Q80ZB1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Prestin;
DE AltName: Full=Solute carrier family 26 member 5;
GN Name=Slc26a5; Synonyms=Pres;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Organ of Corti;
RX PubMed=14553901; DOI=10.1016/s0378-5955(03)00192-8;
RA Dougherty G.W., Kachar B.;
RT "Expression of prestin, a membrane motor protein, in the mammalian auditory
RT and vestibular periphery.";
RL Hear. Res. 184:27-40(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CBA/CaJ;
RX PubMed=12584604; DOI=10.1007/s00335-002-2227-y;
RA Zheng J., Long K.B., Matsuda K., Madison L.D., Ryan A., Dallos P.D.;
RT "Genomic characterization and expression of mouse prestin, the motor
RT protein of outer hair cells.";
RL Mamm. Genome 14:87-96(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Lateral wall of outer hair cells.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the outer hair cells (OHC) of the
CC organ of Corti of the inner ear. Also weak expression in brain and
CC testis. Very weakly expressed in heart, spleen, muscle and lactating
CC mammary glands. {ECO:0000269|PubMed:12584604}.
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; AY024359; AAG59999.2; -; mRNA.
DR EMBL; AF529192; AAO59381.1; -; mRNA.
DR EMBL; CH466586; EDL03187.1; -; Genomic_DNA.
DR CCDS; CCDS19109.1; -.
DR RefSeq; NP_001276716.1; NM_001289787.1.
DR RefSeq; NP_001276717.1; NM_001289788.1.
DR RefSeq; NP_109652.3; NM_030727.5.
DR AlphaFoldDB; Q99NH7; -.
DR SMR; Q99NH7; -.
DR STRING; 10090.ENSMUSP00000030878; -.
DR TCDB; 2.A.53.2.5; the sulfate permease (sulp) family.
DR GlyGen; Q99NH7; 2 sites.
DR iPTMnet; Q99NH7; -.
DR PhosphoSitePlus; Q99NH7; -.
DR PaxDb; Q99NH7; -.
DR PRIDE; Q99NH7; -.
DR Antibodypedia; 31198; 138 antibodies from 26 providers.
DR DNASU; 80979; -.
DR Ensembl; ENSMUST00000030878; ENSMUSP00000030878; ENSMUSG00000029015.
DR GeneID; 80979; -.
DR KEGG; mmu:80979; -.
DR UCSC; uc008wpe.2; mouse.
DR CTD; 375611; -.
DR MGI; MGI:1933154; Slc26a5.
DR VEuPathDB; HostDB:ENSMUSG00000029015; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q99NH7; -.
DR OMA; EAPHDIK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q99NH7; -.
DR TreeFam; TF313784; -.
DR BioGRID-ORCS; 80979; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q99NH7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99NH7; protein.
DR Bgee; ENSMUSG00000029015; Expressed in animal zygote and 10 other tissues.
DR ExpressionAtlas; Q99NH7; baseline and differential.
DR Genevisible; Q99NH7; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0120249; C:lateral wall of outer hair cell; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098656; P:anion transmembrane transport; ISO:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0015755; P:fructose transmembrane transport; ISO:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; ISO:MGI.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:MGI.
DR GO; GO:0045793; P:positive regulation of cell size; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR GO; GO:0009751; P:response to salicylic acid; IEA:Ensembl.
DR GO; GO:1902074; P:response to salt; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
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 2: Evidence at transcript level;
KW Cell membrane; Cell shape; Glycoprotein; Hearing; Membrane; Motor protein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Prestin"
FT /id="PRO_0000080169"
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..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..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 720..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Polar residues"
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"
FT CONFLICT 469
FT /note="L -> P (in Ref. 1; AAG59999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 81337 MW; 37A2524F5E75E31B CRC64;
MDHAEENEIP AETQRYYVER PIFSHPVLQE RLHVKDKVTE 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 LYSSALKRKT GVNPALIMGA RRKAMRKYAK EVGNANVANA TVVKVDAEVD
GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENVH TVILDFTQVN FVDSVGVKTL
AGIVKEYGDV GIYVYLAGCS PQVVNDLTRN NFFENPALKE LLFHSIHDAV LGSQVREAMA
EQEATASLPQ EDMEPNATPT TPEA
