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Q9EPH0

- S26A5_RAT

UniProt

Q9EPH0 - S26A5_RAT

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Protein

Prestin

Gene
Slc26a5, Pres
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. motor activity Source: RGD
  2. secondary active sulfate transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. metabolic process Source: GOC
  2. regulation of cell shape Source: UniProtKB-KW
  3. regulation of membrane potential Source: Ensembl
  4. sensory perception of sound Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell shape, Hearing

Names & Taxonomyi

Protein namesi
Recommended name:
Prestin
Alternative name(s):
Solute carrier family 26 member 5
Gene namesi
Name:Slc26a5
Synonyms:Pres
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi69334. Slc26a5.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7979Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei80 – 10021Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini101 – 1022Extracellular Reviewed prediction
Transmembranei103 – 12321Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini124 – 1318Cytoplasmic Reviewed prediction
Transmembranei132 – 15221Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini153 – 18331Extracellular Reviewed predictionAdd
BLAST
Transmembranei184 – 20421Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini205 – 2117Cytoplasmic Reviewed prediction
Transmembranei212 – 23221Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini233 – 25321Extracellular Reviewed predictionAdd
BLAST
Transmembranei254 – 27421Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini275 – 28612Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei287 – 30721Helical; Name=7; Reviewed predictionAdd
BLAST
Topological domaini308 – 33427Extracellular Reviewed predictionAdd
BLAST
Transmembranei335 – 35521Helical; Name=8; Reviewed predictionAdd
BLAST
Topological domaini356 – 37419Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei375 – 39521Helical; Name=9; Reviewed predictionAdd
BLAST
Topological domaini396 – 41116Extracellular Reviewed predictionAdd
BLAST
Transmembranei412 – 43221Helical; Name=10; Reviewed predictionAdd
BLAST
Topological domaini433 – 4419Cytoplasmic Reviewed prediction
Transmembranei442 – 46221Helical; Name=11; Reviewed predictionAdd
BLAST
Topological domaini463 – 47917Extracellular Reviewed predictionAdd
BLAST
Transmembranei480 – 50021Helical; Name=12; Reviewed predictionAdd
BLAST
Topological domaini501 – 744244Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. lateral plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541D → N: Shifts the voltage-sensitivity to more negative values. 1 Publication
Mutagenesisi155 – 1551D → N: Shifts the voltage-sensitivity to more negative values. 1 Publication
Mutagenesisi169 – 1691E → Q: No effect. 1 Publication
Mutagenesisi177 – 1771K → Q: No effect. 1 Publication
Mutagenesisi197 – 1971R → Q: Shifts the voltage-sensitivity to more negative values. 1 Publication
Mutagenesisi233 – 2331K → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236. 1 Publication
Mutagenesisi235 – 2351K → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236. 1 Publication
Mutagenesisi236 – 2361R → Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235. 1 Publication
Mutagenesisi277 – 2771E → Q: Shifts the voltage-sensitivity to slightly more positive values. 1 Publication
Mutagenesisi281 – 2811R → Q: No effect; when associated with Q-283 and Q-285. 1 Publication
Mutagenesisi283 – 2831K → Q: No effect; when associated with Q-218 and Q-285. 1 Publication
Mutagenesisi285 – 2851K → Q: No effect; when associated with Q-281 and Q-283. 1 Publication
Mutagenesisi332 – 3321D → Q: No effect. 1 Publication
Mutagenesisi342 – 3421D → Q: Shifts the voltage-sensitivity to more positive values. 1 Publication
Mutagenesisi409 – 4091K → Q: No effect. 1 Publication
Mutagenesisi557 – 5571K → Q: No effect; when associated with Q-558 and Q-559. 1 Publication
Mutagenesisi558 – 5581R → Q: No effect; when associated with Q-557 and Q-559. 1 Publication
Mutagenesisi559 – 5591K → Q: No effect; when associated with Q-557 and Q-558. 1 Publication
Mutagenesisi571 – 5711R → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577. 1 Publication
Mutagenesisi572 – 5721R → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577. 1 Publication
Mutagenesisi577 – 5771K → Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744PrestinPRO_0000080170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi163 – 1631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi166 – 1661N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9EPH0.
PRIDEiQ9EPH0.

Expressioni

Tissue specificityi

Specifically expressed in outer hair cells. Not detected in other cells of the organ of Corti.1 Publication

Developmental stagei

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.

Gene expression databases

GenevestigatoriQ9EPH0.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015733.

Structurei

Secondary structure

1
744
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi507 – 5137
Beta strandi520 – 5223
Turni523 – 5253
Beta strandi535 – 5406
Helixi544 – 55411
Beta strandi640 – 6456
Helixi654 – 66815
Turni669 – 6713
Beta strandi673 – 6786
Helixi681 – 6899
Turni690 – 6934
Helixi696 – 7016
Beta strandi702 – 7054
Helixi706 – 7127

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLOX-ray1.57A505-563[»]
A637-718[»]
ProteinModelPortaliQ9EPH0.

Miscellaneous databases

EvolutionaryTraceiQ9EPH0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini525 – 713189STASAdd
BLAST

Sequence similaritiesi

Contains 1 STAS domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0659.
GeneTreeiENSGT00750000117367.
HOGENOMiHOG000006546.
HOVERGENiHBG000639.
InParanoidiQ9EPH0.
KOiK14703.
OMAiQRFMPPG.
OrthoDBiEOG76T9QT.
PhylomeDBiQ9EPH0.
TreeFamiTF313784.

Family and domain databases

Gene3Di3.30.750.24. 2 hits.
InterProiIPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view]
PfamiPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 2 hits.
TIGRFAMsiTIGR00815. sulP. 1 hit.
PROSITEiPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPH0-1 [UniParc]FASTAAdd to Basket

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MDHAEENEIP AETQKYLVER PIFSHPVLQE RLHVKDKVTD SIGDKLKQAF    50
TCTPKKVRNI IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA 100
FAMLAAVPPV FGLYSSFYPV IMYCFFGTSR HISIGPFAVI SLMIGGVAVR 150
LVPDDIVIPG GVNATNGTEA RDALRVKVAM SVTLLSGIIQ FCLGVCRFGF 200
VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI FSVVYSTVAV 250
LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG 300
TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG 350
FSVTISMAKT LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS 400
LVQEGTGGKT QLAGCLASLM ILLVILATGF LFESLPQAVL SAIVIVNLKG 450
MFMQFSDLPF FWRTSKIELT IWLTTFVSSL FLGLDYGLIT AVIIALLTVI 500
YRTQSPSYTV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI NAPIYYANSD 550
LYSSALKRKT GVNPAIIMGA RRKAMRKYAK EVGNANIANA TVVKVDAEVD 600
GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENIH TVILDFTQVN 650
FMDSVGVKTL AGIVKEYGDV GIYVYLAGCS AQVVNDLTSN RFFENPALKE 700
LLFHSIHDAV LGSQVREAMA EQETTVLPPQ EDMEPNATPT TPEA 744
Length:744
Mass (Da):81,279
Last modified:March 1, 2001 - v1
Checksum:iE49E842CF7A3CD58
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511L → V in AAG30297. 1 Publication
Sequence conflicti567 – 5671I → M in AAG30297. 1 Publication
Sequence conflicti572 – 5721R → S in AAG30297. 1 Publication
Sequence conflicti612 – 6121D → G in AAG30297. 1 Publication
Sequence conflicti662 – 6632GI → VM in AAG30297. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ303372 mRNA. Translation: CAC21555.1.
AF315652 mRNA. Translation: AAG30297.1.
AJ428404 Genomic DNA. Translation: CAD21439.1.
RefSeqiNP_110467.1. NM_030840.1.
UniGeneiRn.64631.

Genome annotation databases

EnsembliENSRNOT00000015733; ENSRNOP00000015733; ENSRNOG00000011616.
GeneIDi83819.
KEGGirno:83819.

Cross-referencesi

Web resourcesi

Protein Spotlight

Pump up the volume - Issue 22 of May 2002

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ303372 mRNA. Translation: CAC21555.1 .
AF315652 mRNA. Translation: AAG30297.1 .
AJ428404 Genomic DNA. Translation: CAD21439.1 .
RefSeqi NP_110467.1. NM_030840.1.
UniGenei Rn.64631.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LLO X-ray 1.57 A 505-563 [» ]
A 637-718 [» ]
ProteinModelPortali Q9EPH0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000015733.

Proteomic databases

PaxDbi Q9EPH0.
PRIDEi Q9EPH0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015733 ; ENSRNOP00000015733 ; ENSRNOG00000011616 .
GeneIDi 83819.
KEGGi rno:83819.

Organism-specific databases

CTDi 375611.
RGDi 69334. Slc26a5.

Phylogenomic databases

eggNOGi COG0659.
GeneTreei ENSGT00750000117367.
HOGENOMi HOG000006546.
HOVERGENi HBG000639.
InParanoidi Q9EPH0.
KOi K14703.
OMAi QRFMPPG.
OrthoDBi EOG76T9QT.
PhylomeDBi Q9EPH0.
TreeFami TF313784.

Miscellaneous databases

EvolutionaryTracei Q9EPH0.
NextBioi 616430.
PROi Q9EPH0.

Gene expression databases

Genevestigatori Q9EPH0.

Family and domain databases

Gene3Di 3.30.750.24. 2 hits.
InterProi IPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view ]
Pfami PF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view ]
SUPFAMi SSF52091. SSF52091. 2 hits.
TIGRFAMsi TIGR00815. sulP. 1 hit.
PROSITEi PS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiS26A5_RAT
AccessioniPrimary (citable) accession number: Q9EPH0
Secondary accession number(s): Q9ERC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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