S26A5_RAT
ID S26A5_RAT Reviewed; 744 AA.
AC Q9EPH0; Q9ERC6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Prestin;
DE AltName: Full=Solute carrier family 26 member 5;
GN Name=Slc26a5; Synonyms=Pres;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TOPOLOGY.
RC TISSUE=Cochlea;
RX PubMed=11274441; DOI=10.1073/pnas.071613498;
RA Ludwig J., Oliver D., Frank G., Kloecker N., Gummer A.W., Fakler B.;
RT "Reciprocal electromechanical properties of rat prestin: the motor molecule
RT from rat outer hair cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4178-4183(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 249-668.
RC STRAIN=Sprague-Dawley;
RA Beisel K.W., Nelson N.C., Beisel C.L., Delimont D.C., He D.Z.Z.,
RA Fritzsch B.;
RT "Dynamic developmental expression of cochlear hair cell genes: prestin and
RT otoferlin.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-20.
RC STRAIN=Sprague-Dawley;
RA Weber T., Zimmermann U., Winter H., Mack A., Koepschall I., Rohbock K.,
RA Zenner H.P., Knipper M.;
RT "Thyroid horomone is a critical determinant for the regulation of the
RT cochlear motor protein prestin.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11125015; DOI=10.1523/jneurosci.20-24-j0002.2000;
RA Belyantseva I.A., Adler H.J., Curi R., Frolenkov G.I., Kachar B.;
RT "Expression and localization of prestin and the sugar transporter GLUT-5
RT during development of electromotility in cochlear outer hair cells.";
RL J. Neurosci. 20:RC116-RC116(2000).
RN [5]
RP MODE OF ACTION, AND MUTAGENESIS OF ASP-154; ASP-155; GLU-169; LYS-177;
RP ARG-197; LYS-233; LYS-235; ARG-236; GLU-277; ARG-281; LYS-283; LYS-285;
RP ASP-332; ASP-342; LYS-409; LYS-557; ARG-558; LYS-559; ARG-571; ARG-572 AND
RP LYS-577.
RX PubMed=11423665; DOI=10.1126/science.1060939;
RA Oliver D., He D.Z.Z., Kloecker N., Ludwig J., Schulte U., Waldegger S.,
RA Ruppersberg J.P., Dallos P., Fakler B.;
RT "Intracellular anions as the voltage sensor of prestin, the outer hair cell
RT motor protein.";
RL Science 292:2340-2343(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: Cell membrane; Multi-pass membrane protein.
CC Note=Lateral wall of outer hair cells.
CC -!- TISSUE SPECIFICITY: Specifically expressed in outer hair cells. Not
CC detected in other cells of the organ of Corti.
CC {ECO:0000269|PubMed:11125015}.
CC -!- DEVELOPMENTAL STAGE: Low levels are present in newborn rats and up to
CC day 6. Subsequently, levels increase strongly. Adult levels are
CC detected starting from day 9 in the basal turn of the cochlea, from day
CC 10-11 in the middle turn, and from day 12 in the apical turn.
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; AJ303372; CAC21555.1; -; mRNA.
DR EMBL; AF315652; AAG30297.1; -; mRNA.
DR EMBL; AJ428404; CAD21439.1; -; Genomic_DNA.
DR RefSeq; NP_110467.1; NM_030840.1.
DR RefSeq; XP_017448406.1; XM_017592917.1.
DR PDB; 3LLO; X-ray; 1.57 A; A=505-563, A=637-718.
DR PDB; 5EUS; X-ray; 1.83 A; A=505-563, A=637-718.
DR PDB; 5EUU; X-ray; 1.87 A; A=505-563, A=637-718.
DR PDB; 5EUW; X-ray; 1.81 A; A=505-563, A=637-718.
DR PDB; 5EUX; X-ray; 2.04 A; A=505-563, A=637-718.
DR PDB; 5EUZ; X-ray; 2.40 A; A=505-563, A=637-718.
DR PDBsum; 3LLO; -.
DR PDBsum; 5EUS; -.
DR PDBsum; 5EUU; -.
DR PDBsum; 5EUW; -.
DR PDBsum; 5EUX; -.
DR PDBsum; 5EUZ; -.
DR AlphaFoldDB; Q9EPH0; -.
DR SMR; Q9EPH0; -.
DR STRING; 10116.ENSRNOP00000015733; -.
DR GlyGen; Q9EPH0; 2 sites.
DR iPTMnet; Q9EPH0; -.
DR PhosphoSitePlus; Q9EPH0; -.
DR PaxDb; Q9EPH0; -.
DR Ensembl; ENSRNOT00000015733; ENSRNOP00000015733; ENSRNOG00000011616.
DR GeneID; 83819; -.
DR KEGG; rno:83819; -.
DR CTD; 375611; -.
DR RGD; 69334; Slc26a5.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q9EPH0; -.
DR OMA; EAPHDIK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9EPH0; -.
DR TreeFam; TF313784; -.
DR EvolutionaryTrace; Q9EPH0; -.
DR PRO; PR:Q9EPH0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011616; Expressed in testis.
DR Genevisible; Q9EPH0; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0120249; C:lateral wall of outer hair cell; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:0003774; F:cytoskeletal motor activity; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
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; ISO:RGD.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0098656; P:anion transmembrane transport; IDA:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; IDA:RGD.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:RGD.
DR GO; GO:0045793; P:positive regulation of cell size; IDA:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0035864; P:response to potassium ion; IEP:RGD.
DR GO; GO:0009751; P:response to salicylic acid; IEP:RGD.
DR GO; GO:1902074; P:response to salt; IEP:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR DisProt; DP01937; -.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Prestin"
FT /id="PRO_0000080170"
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 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 MUTAGEN 154
FT /note="D->N: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 155
FT /note="D->N: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 169
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 177
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 197
FT /note="R->Q: Shifts the voltage-sensitivity to more
FT negative values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 233
FT /note="K->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-235 and Q-236."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 235
FT /note="K->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-233 and Q-236."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 236
FT /note="R->Q: Shifts the voltage-sensitivity to more
FT negative values; when associated with Q-233 and Q-235."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 277
FT /note="E->Q: Shifts the voltage-sensitivity to slightly
FT more positive values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 281
FT /note="R->Q: No effect; when associated with Q-283 and Q-
FT 285."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 283
FT /note="K->Q: No effect; when associated with Q-218 and Q-
FT 285."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 285
FT /note="K->Q: No effect; when associated with Q-281 and Q-
FT 283."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 332
FT /note="D->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 342
FT /note="D->Q: Shifts the voltage-sensitivity to more
FT positive values."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 409
FT /note="K->Q: No effect."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 557
FT /note="K->Q: No effect; when associated with Q-558 and Q-
FT 559."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 558
FT /note="R->Q: No effect; when associated with Q-557 and Q-
FT 559."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 559
FT /note="K->Q: No effect; when associated with Q-557 and Q-
FT 558."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 571
FT /note="R->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-572 and Q-
FT 577."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 572
FT /note="R->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-571 and Q-
FT 577."
FT /evidence="ECO:0000269|PubMed:11423665"
FT MUTAGEN 577
FT /note="K->Q: Shifts the voltage-sensitivity to slightly
FT more positive values; when associated with Q-571 and Q-
FT 572."
FT /evidence="ECO:0000269|PubMed:11423665"
FT CONFLICT 251
FT /note="L -> V (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="I -> M (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="R -> S (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="D -> G (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT CONFLICT 662..663
FT /note="GI -> VM (in Ref. 2; AAG30297)"
FT /evidence="ECO:0000305"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 654..668
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:3LLO"
FT TURN 690..693
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 696..701
FT /evidence="ECO:0007829|PDB:3LLO"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:3LLO"
FT HELIX 706..712
FT /evidence="ECO:0007829|PDB:3LLO"
SQ SEQUENCE 744 AA; 81279 MW; E49E842CF7A3CD58 CRC64;
MDHAEENEIP AETQKYLVER PIFSHPVLQE RLHVKDKVTD SIGDKLKQAF TCTPKKVRNI
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 YRTQSPSYTV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI
NAPIYYANSD LYSSALKRKT GVNPAIIMGA RRKAMRKYAK EVGNANIANA TVVKVDAEVD
GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENIH TVILDFTQVN FMDSVGVKTL
AGIVKEYGDV GIYVYLAGCS AQVVNDLTSN RFFENPALKE LLFHSIHDAV LGSQVREAMA
EQETTVLPPQ EDMEPNATPT TPEA
