Q9JKQ2 (S26A5_MERUN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Prestin Alternative name(s): Solute carrier family 26 member 5 | ||||
| Gene names |
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| Organism | Meriones unguiculatus (Mongolian jird) (Mongolian gerbil) | ||||
| Taxonomic identifier | 10047 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Gerbillinae › Meriones![]() |
Protein attributes
| Sequence length | 744 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | Basolateral cell membrane; Multi-pass membrane protein. Note: Basolateral wall of outer hair cells. |
| Tissue specificity | Highly expressed in mature outer hair cells, but not in inner hair cells or other cells of the basilar membrane and the organ of Corti. |
| Developmental stage | Detected in the organ of Corti as early as 6 days after birth; levels increase up to day 20, concomitant with the development of high sensitivity hearing. |
| Sequence similarities | Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. [View classification] Contains 1 STAS domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Hearing |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Motor protein |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological_process | regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW sensory perception of soundInferred from electronic annotation. Source: UniProtKB-KW sulfate transportInferred from electronic annotation. Source: InterPro |
| Cellular_component | basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | secondary active sulfate transmembrane transporter activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 744 | 744 | Prestin | PRO_0000080168 | |||||
Regions | |||||||||
| Topological domain | 1 – 79 | 79 | Cytoplasmic Potential | ||||||
| Transmembrane | 80 – 100 | 21 | Helical; Name=1; Potential | ||||||
| Topological domain | 101 – 102 | 2 | Extracellular Potential | ||||||
| Transmembrane | 103 – 123 | 21 | Helical; Name=2; Potential | ||||||
| Topological domain | 124 – 131 | 8 | Cytoplasmic Potential | ||||||
| Transmembrane | 132 – 152 | 21 | Helical; Name=3; Potential | ||||||
| Topological domain | 153 – 183 | 31 | Extracellular Potential | ||||||
| Transmembrane | 184 – 204 | 21 | Helical; Name=4; Potential | ||||||
| Topological domain | 205 – 211 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 212 – 232 | 21 | Helical; Name=5; Potential | ||||||
| Topological domain | 233 – 253 | 21 | Extracellular Potential | ||||||
| Transmembrane | 254 – 274 | 21 | Helical; Name=6; Potential | ||||||
| Topological domain | 275 – 286 | 12 | Cytoplasmic Potential | ||||||
| Transmembrane | 287 – 307 | 21 | Helical; Name=7; Potential | ||||||
| Topological domain | 308 – 334 | 27 | Extracellular Potential | ||||||
| Transmembrane | 335 – 355 | 21 | Helical; Name=8; Potential | ||||||
| Topological domain | 356 – 374 | 19 | Cytoplasmic Potential | ||||||
| Transmembrane | 375 – 395 | 21 | Helical; Name=9; Potential | ||||||
| Topological domain | 396 – 411 | 16 | Extracellular Potential | ||||||
| Transmembrane | 412 – 432 | 21 | Helical; Name=10; Potential | ||||||
| Topological domain | 433 – 441 | 9 | Cytoplasmic Potential | ||||||
| Transmembrane | 442 – 462 | 21 | Helical; Name=11; Potential | ||||||
| Topological domain | 463 – 479 | 17 | Extracellular Potential | ||||||
| Transmembrane | 480 – 500 | 21 | Helical; Name=12; Potential | ||||||
| Topological domain | 501 – 744 | 244 | Cytoplasmic Potential | ||||||
| Domain | 525 – 713 | 189 | STAS | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 163 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 166 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Prestin is the motor protein of cochlear outer hair cells." Zheng J., Shen W., He D.Z.Z., Long K.B., Madison L.D., Dallos P. Nature 405:149-155(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Organ of Corti. |
| [2] | "Prestin topology: localization of protein epitopes in relation to the plasma membrane." Zheng J., Long K.B., Shen W., Madison L.D., Dallos P. NeuroReport 12:1929-1935(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY. |
Web resources
| Protein Spotlight Pump up the volume - Issue 22 of May 2002 |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF230376 mRNA. Translation: AAF71715.1. |
3D structure databases | |
| ProteinModelPortal | Q9JKQ2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG000639. |
Family and domain databases | |
| Gene3D | 3.30.750.24. 2 hits. |
| InterPro | IPR018045. S04_transporter_CS. IPR002645. STAS_dom. IPR001902. SulP_transpt. IPR011547. Sulph_transpt. [Graphical view] |
| Pfam | PF01740. STAS. 1 hit. PF00916. Sulfate_transp. 1 hit. [Graphical view] |
| SUPFAM | SSF52091. STAS. 1 hit. |
| TIGRFAMs | TIGR00815. sulP. 1 hit. |
| PROSITE | PS01130. SLC26A. 1 hit. PS50801. STAS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | S26A5_MERUN | ||||||||
| Accession | Primary (citable) accession number: Q9JKQ2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |

Clusters with
