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Q9EPH0 (S26A5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prestin
Alternative name(s):
Solute carrier family 26 member 5
Gene names
Name:Slc26a5
Synonyms:Pres
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length744 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Lateral wall of outer hair cells.

Tissue specificity

Specifically expressed in outer hair cells. Not detected in other cells of the organ of Corti. Ref.4

Developmental stage

Low levels are present in newborn rats and up to day 6. Subsequently, levels increase strongly. Adult levels are detected starting from day 9 in the basal turn of the cochlea, from day 10-11 in the middle turn, and from day 12 in the apical turn.

Sequence similarities

Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. [View classification]

Contains 1 STAS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 744744Prestin
PRO_0000080170

Regions

Topological domain1 – 7979Cytoplasmic Potential
Transmembrane80 – 10021Helical; Name=1; Potential
Topological domain101 – 1022Extracellular Potential
Transmembrane103 – 12321Helical; Name=2; Potential
Topological domain124 – 1318Cytoplasmic Potential
Transmembrane132 – 15221Helical; Name=3; Potential
Topological domain153 – 18331Extracellular Potential
Transmembrane184 – 20421Helical; Name=4; Potential
Topological domain205 – 2117Cytoplasmic Potential
Transmembrane212 – 23221Helical; Name=5; Potential
Topological domain233 – 25321Extracellular Potential
Transmembrane254 – 27421Helical; Name=6; Potential
Topological domain275 – 28612Cytoplasmic Potential
Transmembrane287 – 30721Helical; Name=7; Potential
Topological domain308 – 33427Extracellular Potential
Transmembrane335 – 35521Helical; Name=8; Potential
Topological domain356 – 37419Cytoplasmic Potential
Transmembrane375 – 39521Helical; Name=9; Potential
Topological domain396 – 41116Extracellular Potential
Transmembrane412 – 43221Helical; Name=10; Potential
Topological domain433 – 4419Cytoplasmic Potential
Transmembrane442 – 46221Helical; Name=11; Potential
Topological domain463 – 47917Extracellular Potential
Transmembrane480 – 50021Helical; Name=12; Potential
Topological domain501 – 744244Cytoplasmic Potential
Domain525 – 713189STAS

Amino acid modifications

Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1541D → N: Shifts the voltage-sensitivity to more negative values. Ref.5
Mutagenesis1551D → N: Shifts the voltage-sensitivity to more negative values. Ref.5
Mutagenesis1691E → Q: No effect. Ref.5
Mutagenesis1771K → Q: No effect. Ref.5
Mutagenesis1971R → Q: Shifts the voltage-sensitivity to more negative values. Ref.5
Mutagenesis2331K → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236. Ref.5
Mutagenesis2351K → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236. Ref.5
Mutagenesis2361R → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235. Ref.5
Mutagenesis2771E → Q: Shifts the voltage-sensitivity to slightly more positive values. Ref.5
Mutagenesis2811R → Q: No effect; when associated with Q-283 and Q-285. Ref.5
Mutagenesis2831K → Q: No effect; when associated with Q-218 and Q-285. Ref.5
Mutagenesis2851K → Q: No effect; when associated with Q-281 and Q-283. Ref.5
Mutagenesis3321D → Q: No effect. Ref.5
Mutagenesis3421D → Q: Shifts the voltage-sensitivity to more positive values. Ref.5
Mutagenesis4091K → Q: No effect. Ref.5
Mutagenesis5571K → Q: No effect; when associated with Q-558 and Q-559. Ref.5
Mutagenesis5581R → Q: No effect; when associated with Q-557 and Q-559. Ref.5
Mutagenesis5591K → Q: No effect; when associated with Q-557 and Q-558. Ref.5
Mutagenesis5711R → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577. Ref.5
Mutagenesis5721R → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577. Ref.5
Mutagenesis5771K → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572. Ref.5
Sequence conflict2511L → V in AAG30297. Ref.2
Sequence conflict5671I → M in AAG30297. Ref.2
Sequence conflict5721R → S in AAG30297. Ref.2
Sequence conflict6121D → G in AAG30297. Ref.2
Sequence conflict662 – 6632GI → VM in AAG30297. Ref.2

Secondary structure

........................ 744
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9EPH0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E49E842CF7A3CD58

FASTA74481,279
        10         20         30         40         50         60 
MDHAEENEIP AETQKYLVER PIFSHPVLQE RLHVKDKVTD SIGDKLKQAF TCTPKKVRNI 

        70         80         90        100        110        120 
IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV 

       130        140        150        160        170        180 
IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM 

       190        200        210        220        230        240 
SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI 

       250        260        270        280        290        300 
FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG 

       310        320        330        340        350        360 
TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT 

       370        380        390        400        410        420 
LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM 

       430        440        450        460        470        480 
ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL 

       490        500        510        520        530        540 
FLGLDYGLIT AVIIALLTVI YRTQSPSYTV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI 

       550        560        570        580        590        600 
NAPIYYANSD LYSSALKRKT GVNPAIIMGA RRKAMRKYAK EVGNANIANA TVVKVDAEVD 

       610        620        630        640        650        660 
GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENIH TVILDFTQVN FMDSVGVKTL 

       670        680        690        700        710        720 
AGIVKEYGDV GIYVYLAGCS AQVVNDLTSN RFFENPALKE LLFHSIHDAV LGSQVREAMA 

       730        740 
EQETTVLPPQ EDMEPNATPT TPEA 

« Hide

References

[1]"Reciprocal electromechanical properties of rat prestin: the motor molecule from rat outer hair cells."
Ludwig J., Oliver D., Frank G., Kloecker N., Gummer A.W., Fakler B.
Proc. Natl. Acad. Sci. U.S.A. 98:4178-4183(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TOPOLOGY.
Tissue: Cochlea.
[2]"Dynamic developmental expression of cochlear hair cell genes: prestin and otoferlin."
Beisel K.W., Nelson N.C., Beisel C.L., Delimont D.C., He D.Z.Z., Fritzsch B.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 249-668.
Strain: Sprague-Dawley.
[3]"Thyroid horomone is a critical determinant for the regulation of the cochlear motor protein prestin."
Weber T., Zimmermann U., Winter H., Mack A., Koepschall I., Rohbock K., Zenner H.P., Knipper M.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
Strain: Sprague-Dawley.
[4]"Expression and localization of prestin and the sugar transporter GLUT-5 during development of electromotility in cochlear outer hair cells."
Belyantseva I.A., Adler H.J., Curi R., Frolenkov G.I., Kachar B.
J. Neurosci. 20:RC116-RC116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein."
Oliver D., He D.Z.Z., Kloecker N., Ludwig J., Schulte U., Waldegger S., Ruppersberg J.P., Dallos P., Fakler B.
Science 292:2340-2343(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MODE OF ACTION, MUTAGENESIS OF ASP-154; ASP-155; GLU-169; LYS-177; ARG-197; LYS-233; LYS-235; ARG-236; GLU-277; ARG-281; LYS-283; LYS-285; ASP-332; ASP-342; LYS-409; LYS-557; ARG-558; LYS-559; ARG-571; ARG-572 AND LYS-577.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Pump up the volume - Issue 22 of May 2002

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ303372 mRNA. Translation: CAC21555.1.
AF315652 mRNA. Translation: AAG30297.1.
AJ428404 Genomic DNA. Translation: CAD21439.1.
RefSeqNP_110467.1. NM_030840.1.
UniGeneRn.64631.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLOX-ray1.57A505-718[»]
ProteinModelPortalQ9EPH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015733.

Proteomic databases

PaxDbQ9EPH0.
PRIDEQ9EPH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015733; ENSRNOP00000015733; ENSRNOG00000011616.
GeneID83819.
KEGGrno:83819.

Organism-specific databases

CTD375611.
RGD69334. Slc26a5.

Phylogenomic databases

eggNOGCOG0659.
GeneTreeENSGT00750000117367.
HOGENOMHOG000006546.
HOVERGENHBG000639.
InParanoidQ9EPH0.
KOK14703.
OMAEVGNANM.
OrthoDBEOG76T9QT.
PhylomeDBQ9EPH0.
TreeFamTF313784.

Gene expression databases

GenevestigatorQ9EPH0.

Family and domain databases

Gene3D3.30.750.24. 2 hits.
InterProIPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view]
PfamPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMSSF52091. SSF52091. 2 hits.
TIGRFAMsTIGR00815. sulP. 1 hit.
PROSITEPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9EPH0.
NextBio616430.
PROQ9EPH0.

Entry information

Entry nameS26A5_RAT
AccessionPrimary (citable) accession number: Q9EPH0
Secondary accession number(s): Q9ERC6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references