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Proton-gated ion channel (GLIC) (Ligand-gated ion channel) (LGIC)

 GLIC_GLOVI              Reviewed;         359 AA.
Q7NDN8;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
25-APR-2018, entry version 97.
RecName: Full=Proton-gated ion channel;
AltName: Full=GLIC;
AltName: Full=Ligand-gated ion channel;
Short=LGIC;
Flags: Precursor;
Name=glvI; OrderedLocusNames=glr4197;
Gloeobacter violaceus (strain PCC 7421).
Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales;
Gloeobacteraceae; Gloeobacter.
NCBI_TaxID=251221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 7421;
PubMed=14621292; DOI=10.1093/dnares/10.4.137;
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C.,
Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S.,
Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of Gloeobacter violaceus PCC 7421, a
cyanobacterium that lacks thylakoids.";
DNA Res. 10:137-145(2003).
[2]
FUNCTION AS A PROTON-GATED ION CHANNEL, ION SELECTIVITY, ENZYME
REGULATION, AND SUBUNIT.
STRAIN=PCC 7421;
PubMed=17167423; DOI=10.1038/nature05371;
Bocquet N., Prado de Carvalho L., Cartaud J., Neyton J., Le Poupon C.,
Taly A., Grutter T., Changeux J.P., Corringer P.J.;
"A prokaryotic proton-gated ion channel from the nicotinic
acetylcholine receptor family.";
Nature 445:116-119(2007).
[3]
MODULATION BY ANESTHETICS, AND ENZYME REGULATION.
STRAIN=PCC 7421;
PubMed=19933531; DOI=10.1213/ANE.0b013e3181c4bc69;
Weng Y., Yang L., Corringer P.J., Sonner J.M.;
"Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion
channel.";
Anesth. Analg. 110:59-63(2010).
[4]
ANESTHETIC-BINDING, MUTAGENESIS STUDIES, AND FLUORESCENCE QUENCHING
EXPERIMENTS.
STRAIN=PCC 7421;
PubMed=20858424; DOI=10.1016/j.bpj.2010.07.023;
Chen Q., Cheng M.H., Xu Y., Tang P.;
"Anesthetic binding in a pentameric ligand-gated ion channel: GLIC.";
Biophys. J. 99:1801-1809(2010).
[5]
REVIEW.
PubMed=19995852; DOI=10.1113/jphysiol.2009.183160;
Corringer P.J., Baaden M., Bocquet N., Delarue M., Dufresne V.,
Nury H., Prevost M., Van Renterghem C.;
"Atomic structure and dynamics of pentameric ligand-gated ion
channels: new insight from bacterial homologues.";
J. Physiol. (Lond.) 588:565-572(2010).
[6]
GATING MECHANISM.
PubMed=21041674; DOI=10.1073/pnas.1009313107;
Zhu F., Hummer G.;
"Pore opening and closing of a pentameric ligand-gated ion channel.";
Proc. Natl. Acad. Sci. U.S.A. 107:19814-19819(2010).
[7]
ION SELECTIVITY MECHANISM.
PubMed=21244835; DOI=10.1016/j.bpj.2010.11.077;
Fritsch S., Ivanov I., Wang H., Cheng X.;
"Ion selectivity mechanism in a bacterial pentameric ligand-gated ion
channel.";
Biophys. J. 100:390-398(2011).
[8]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 44-359, AND SUBUNIT.
STRAIN=PCC 7421;
PubMed=18987633; DOI=10.1038/nature07462;
Bocquet N., Nury H., Baaden M., Le Poupon C., Changeux J.P.,
Delarue M., Corringer P.J.;
"X-ray structure of a pentameric ligand-gated ion channel in an
apparently open conformation.";
Nature 457:111-114(2009).
[9]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 43-359 OF WILD-TYPE AND
MUTANT ALA-264, SUBUNIT, AND MUTAGENESIS OF GLU-264.
STRAIN=PCC 7421;
PubMed=18987630; DOI=10.1038/nature07461;
Hilf R.J., Dutzler R.;
"Structure of a potentially open state of a proton-activated
pentameric ligand-gated ion channel.";
Nature 457:115-118(2009).
[10]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 44-235, AND GATING
MECHANISM.
STRAIN=PCC 7421;
PubMed=19917292; DOI=10.1016/j.jmb.2009.11.024;
Nury H., Bocquet N., Le Poupon C., Raynal B., Haouz A.,
Corringer P.J., Delarue M.;
"Crystal structure of the extracellular domain of a bacterial ligand-
gated ion channel.";
J. Mol. Biol. 395:1114-1127(2010).
[11]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 43-359 OF WILD-TYPE AND
MUTANT ASP-264 IN COMPLEXES WITH POSITIVELY CHARGED INHIBITORS, ENZYME
REGULATION, MUTAGENESIS OF GLU-264; THR-268 AND SER-272, AND
MECHANISMS OF OPEN CHANNEL BLOCK.
STRAIN=PCC 7421;
PubMed=21037567; DOI=10.1038/nsmb.1933;
Hilf R.J., Bertozzi C., Zimmermann I., Reiter A., Trauner D.,
Dutzler R.;
"Structural basis of open channel block in a prokaryotic pentameric
ligand-gated ion channel.";
Nat. Struct. Mol. Biol. 17:1330-1336(2010).
[12]
X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 44-359 OF MUTANT PHE-279.
STRAIN=PCC 7421;
PubMed=20308576; DOI=10.1073/pnas.1001832107;
Nury H., Poitevin F., Van Renterghem C., Changeux J.P.,
Corringer P.J., Delarue M., Baaden M.;
"One-microsecond molecular dynamics simulation of channel gating in a
nicotinic receptor homologue.";
Proc. Natl. Acad. Sci. U.S.A. 107:6275-6280(2010).
[13]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 44-359 IN COMPLEXES WITH
PROPOFOL AND DESFLURANE ANESTHETICS, AND MUTAGENESIS OF ILE-244;
VAL-284 AND THR-297.
STRAIN=PCC 7421;
PubMed=21248852; DOI=10.1038/nature09647;
Nury H., Van Renterghem C., Weng Y., Tran A., Baaden M., Dusfresne V.,
Changeux J.P., Sonner J.M., Delarue M., Corringer P.J.;
"X-ray structures of general anaesthetics bound to a pentameric
ligand-gated ion channel.";
Nature 469:428-431(2011).
-!- FUNCTION: Cationic channel with similar permeabilities for Na(+)
and K(+), that is activated by an increase of the proton
concentration on the extracellular side. Displays no permeability
for chloride ions. Shows slow kinetics of activation, no
desensitization and a single channel conductance of 8 pS. Might
contribute to adaptation to external pH change.
{ECO:0000269|PubMed:17167423}.
-!- ENZYME REGULATION: Tetraethylammonium (TEA) and tetrabutylammonium
(TBA) inhibit the proton-activated currents in a dose- and
voltage-dependent manner in vitro, whereas the blocker of acid
sensing ion channels, amiloride, has no effect. Channel current of
GLIC can be inhibited by inhaled and intravenous general
anesthetics at and below concentrations used clinically. Ion
conduction is also inhibited by lidocaine and by divalent
transition metal ions such as cadmium ions.
{ECO:0000269|PubMed:17167423, ECO:0000269|PubMed:19933531,
ECO:0000269|PubMed:21037567}.
-!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:17167423,
ECO:0000269|PubMed:18987630, ECO:0000269|PubMed:18987633}.
-!- INTERACTION:
Self; NbExp=26; IntAct=EBI-8423601, EBI-8423601;
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000305}.
-!- DOMAIN: Consists of an N-terminal ligand-binding domain that
encloses a wide aqueous vestibule and a transmembrane domain that
forms a narrow channel.
-!- MISCELLANEOUS: The homologous nature of GLIC to eukaryotic
nicotinic acetylcholine receptors and other eukaryotic pentameric
ligand-gated ion channels, and its sensitivity to general
anesthetics, define GLIC as a structural and functional model of
signal transduction in the nervous system, also relevant for
exploring the molecular basis of anesthetic action.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. {ECO:0000305}.
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EMBL; BA000045; BAC92138.1; -; Genomic_DNA.
RefSeq; NP_927143.1; NC_005125.1.
RefSeq; WP_011144181.1; NC_005125.1.
PDB; 2XQ3; X-ray; 3.50 A; A/B/C/D/E=43-359.
PDB; 2XQ4; X-ray; 3.60 A; A/B/C/D/E=43-359.
PDB; 2XQ5; X-ray; 3.50 A; A/B/C/D/E=43-359.
PDB; 2XQ6; X-ray; 3.70 A; A/B/C/D/E=43-359.
PDB; 2XQ7; X-ray; 3.40 A; A/B/C/D/E=43-359.
PDB; 2XQ8; X-ray; 3.60 A; A/B/C/D/E=43-359.
PDB; 2XQ9; X-ray; 3.20 A; A/B/C/D/E=43-359.
PDB; 2XQA; X-ray; 3.70 A; A/B/C/D/E=43-359.
PDB; 3EAM; X-ray; 2.90 A; A/B/C/D/E=44-359.
PDB; 3EHZ; X-ray; 3.10 A; A/B/C/D/E=50-359.
PDB; 3EI0; X-ray; 3.50 A; A/B/C/D/E=50-359.
PDB; 3IGQ; X-ray; 2.30 A; A/B/C/D/E/F=44-235.
PDB; 3LSV; X-ray; 3.15 A; A/B/C/D/E=44-359.
PDB; 3P4W; X-ray; 3.20 A; A/B/C/D/E=44-359.
PDB; 3P50; X-ray; 3.30 A; A/B/C/D/E=44-359.
PDB; 3TLS; X-ray; 3.20 A; A/B/C/D/E=44-359.
PDB; 3TLT; X-ray; 3.30 A; A/B/C/D/E=44-359.
PDB; 3TLU; X-ray; 2.85 A; A/B/C/D/E=44-359.
PDB; 3TLV; X-ray; 2.90 A; A/B/C/D/E=44-359.
PDB; 3TLW; X-ray; 2.60 A; A/B/C/D/E=44-359.
PDB; 3UU3; X-ray; 3.15 A; A/B/C/D/E=44-359.
PDB; 3UU4; X-ray; 3.05 A; A/B/C/D/E=44-359.
PDB; 3UU5; X-ray; 2.90 A; A/B/C/D/E=44-359.
PDB; 3UU6; X-ray; 2.98 A; A/B/C/D/E=44-359.
PDB; 3UU8; X-ray; 3.25 A; A/B/C/D/E=44-359.
PDB; 3UUB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=44-359.
PDB; 4F8H; X-ray; 2.99 A; A/B/C/D/E=43-359.
PDB; 4HFB; X-ray; 2.75 A; A/B/C/D/E=44-359.
PDB; 4HFC; X-ray; 3.05 A; A/B/C/D/E=44-359.
PDB; 4HFD; X-ray; 3.10 A; A/B/C/D/E=44-359.
PDB; 4HFE; X-ray; 2.80 A; A/B/C/D/E=44-359.
PDB; 4HFH; X-ray; 2.65 A; A/B/C/D/E=44-359.
PDB; 4HFI; X-ray; 2.40 A; A/B/C/D/E=44-359.
PDB; 4IL4; X-ray; 3.30 A; A/B/C/D/E=44-359.
PDB; 4IL9; X-ray; 2.83 A; A/B/C/D/E=44-358.
PDB; 4ILA; X-ray; 3.50 A; A/B/C/D/E=44-358.
PDB; 4ILB; X-ray; 3.15 A; A/B/C/D/E=44-358.
PDB; 4ILC; X-ray; 2.99 A; A/B/C/D/E=44-358.
PDB; 4IRE; X-ray; 3.19 A; A/B/C/D/E=43-359.
PDB; 4LMJ; X-ray; 3.44 A; A/B/C/D/E=44-359.
PDB; 4LMK; X-ray; 3.22 A; A/B/C/D/E=44-359.
PDB; 4LML; X-ray; 3.80 A; A/B/C/D/E=44-359.
PDB; 4NPP; X-ray; 3.35 A; A/B/C/D/E=44-359.
PDB; 4NPQ; X-ray; 4.35 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=44-359.
PDB; 4QH1; X-ray; 3.40 A; A/B/C/D/E=44-359.
PDB; 4QH4; X-ray; 3.20 A; A/B/C/D/E=44-359.
PDB; 4QH5; X-ray; 3.00 A; A/B/C/D/E=44-359.
PDB; 4X5T; X-ray; 3.50 A; A/B/C/D/E=44-235.
PDB; 4YEU; X-ray; 4.60 A; A/B/C/D/E=236-357.
PDB; 4ZZB; X-ray; 3.40 A; A/B/C/D/E=44-359.
PDB; 4ZZC; X-ray; 3.10 A; A/B/C/D/E=43-359.
PDB; 5HCJ; X-ray; 2.95 A; A/B/C/D/E=44-359.
PDB; 5HCM; X-ray; 3.15 A; A/B/C/D/E=44-359.
PDB; 5HEG; X-ray; 3.21 A; A/B/C/D/E=44-359.
PDB; 5HEH; X-ray; 3.30 A; A/B/C/D/E=44-359.
PDB; 5IUX; X-ray; 2.60 A; A/B/C/D/E=43-359.
PDB; 5J0Z; X-ray; 3.25 A; A/B/C/D/E=47-357.
PDB; 5L47; X-ray; 3.30 A; A/B/C/D/E=43-359.
PDB; 5L4E; X-ray; 3.50 A; A/B/C/D/E=43-359.
PDB; 5L4H; X-ray; 3.30 A; A/B/C/D/E=43-359.
PDB; 5MUO; X-ray; 3.19 A; A/B/C/D/E=44-359.
PDB; 5MUR; X-ray; 3.10 A; A/B/C/D/E=43-359.
PDB; 5MVM; X-ray; 3.10 A; A/B/C/D/E=43-359.
PDB; 5MVN; X-ray; 3.49 A; A/B/C/D/E=43-359.
PDB; 5MZQ; X-ray; 2.80 A; A/B/C/D/E=43-359.
PDB; 5MZR; X-ray; 2.65 A; A/B/C/D/E=43-359.
PDB; 5MZT; X-ray; 2.65 A; A/B/C/D/E=43-359.
PDB; 5OSA; X-ray; 2.75 A; A/B/C/D/E=44-236.
PDB; 5OSB; X-ray; 3.80 A; A/B/C/D/E=44-236.
PDB; 5OSC; X-ray; 3.10 A; A/B/C/D/E=44-236.
PDB; 5V6N; X-ray; 3.35 A; A/B/C/D/E=50-359.
PDB; 5V6O; X-ray; 3.12 A; A/B/C/D/E=50-359.
PDB; 6F0I; X-ray; 3.00 A; A/B/C/D/E=43-359.
PDB; 6F0J; X-ray; 3.15 A; A/B/C/D/E=43-359.
PDB; 6F0M; X-ray; 2.65 A; A/B/C/D/E=43-359.
PDB; 6F0N; X-ray; 3.20 A; A/B/C/D/E=43-359.
PDB; 6F0R; X-ray; 2.50 A; A/B/C/D/E=43-359.
PDB; 6F0U; X-ray; 2.35 A; A/B/C/D/E=43-359.
PDB; 6F0V; X-ray; 2.85 A; A/B/C/D/E=43-359.
PDB; 6F0Z; X-ray; 2.50 A; A/B/C/D/E=43-359.
PDB; 6F10; X-ray; 2.85 A; A/B/C/D/E=43-359.
PDB; 6F11; X-ray; 2.95 A; A/B/C/D/E=43-359.
PDB; 6F12; X-ray; 3.20 A; A/B/C/D/E=43-359.
PDB; 6F13; X-ray; 2.70 A; A/B/C/D/E=43-359.
PDB; 6F15; X-ray; 2.85 A; A/B/C/D/E=43-359.
PDB; 6F16; X-ray; 2.60 A; A/B/C/D/E=43-359.
PDB; 6F7A; X-ray; 6.00 A; A/B/C/D/E=47-357.
PDBsum; 2XQ3; -.
PDBsum; 2XQ4; -.
PDBsum; 2XQ5; -.
PDBsum; 2XQ6; -.
PDBsum; 2XQ7; -.
PDBsum; 2XQ8; -.
PDBsum; 2XQ9; -.
PDBsum; 2XQA; -.
PDBsum; 3EAM; -.
PDBsum; 3EHZ; -.
PDBsum; 3EI0; -.
PDBsum; 3IGQ; -.
PDBsum; 3LSV; -.
PDBsum; 3P4W; -.
PDBsum; 3P50; -.
PDBsum; 3TLS; -.
PDBsum; 3TLT; -.
PDBsum; 3TLU; -.
PDBsum; 3TLV; -.
PDBsum; 3TLW; -.
PDBsum; 3UU3; -.
PDBsum; 3UU4; -.
PDBsum; 3UU5; -.
PDBsum; 3UU6; -.
PDBsum; 3UU8; -.
PDBsum; 3UUB; -.
PDBsum; 4F8H; -.
PDBsum; 4HFB; -.
PDBsum; 4HFC; -.
PDBsum; 4HFD; -.
PDBsum; 4HFE; -.
PDBsum; 4HFH; -.
PDBsum; 4HFI; -.
PDBsum; 4IL4; -.
PDBsum; 4IL9; -.
PDBsum; 4ILA; -.
PDBsum; 4ILB; -.
PDBsum; 4ILC; -.
PDBsum; 4IRE; -.
PDBsum; 4LMJ; -.
PDBsum; 4LMK; -.
PDBsum; 4LML; -.
PDBsum; 4NPP; -.
PDBsum; 4NPQ; -.
PDBsum; 4QH1; -.
PDBsum; 4QH4; -.
PDBsum; 4QH5; -.
PDBsum; 4X5T; -.
PDBsum; 4YEU; -.
PDBsum; 4ZZB; -.
PDBsum; 4ZZC; -.
PDBsum; 5HCJ; -.
PDBsum; 5HCM; -.
PDBsum; 5HEG; -.
PDBsum; 5HEH; -.
PDBsum; 5IUX; -.
PDBsum; 5J0Z; -.
PDBsum; 5L47; -.
PDBsum; 5L4E; -.
PDBsum; 5L4H; -.
PDBsum; 5MUO; -.
PDBsum; 5MUR; -.
PDBsum; 5MVM; -.
PDBsum; 5MVN; -.
PDBsum; 5MZQ; -.
PDBsum; 5MZR; -.
PDBsum; 5MZT; -.
PDBsum; 5OSA; -.
PDBsum; 5OSB; -.
PDBsum; 5OSC; -.
PDBsum; 5V6N; -.
PDBsum; 5V6O; -.
PDBsum; 6F0I; -.
PDBsum; 6F0J; -.
PDBsum; 6F0M; -.
PDBsum; 6F0N; -.
PDBsum; 6F0R; -.
PDBsum; 6F0U; -.
PDBsum; 6F0V; -.
PDBsum; 6F0Z; -.
PDBsum; 6F10; -.
PDBsum; 6F11; -.
PDBsum; 6F12; -.
PDBsum; 6F13; -.
PDBsum; 6F15; -.
PDBsum; 6F16; -.
PDBsum; 6F7A; -.
ProteinModelPortal; Q7NDN8; -.
SMR; Q7NDN8; -.
DIP; DIP-59040N; -.
MINT; Q7NDN8; -.
STRING; 251221.glr4197; -.
TCDB; 1.A.9.8.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
EnsemblBacteria; BAC92138; BAC92138; BAC92138.
GeneID; 2602600; -.
KEGG; gvi:glr4197; -.
eggNOG; ENOG4105TA1; Bacteria.
eggNOG; ENOG4111U8M; LUCA.
InParanoid; Q7NDN8; -.
OMA; FRTTFCK; -.
OrthoDB; POG091H13WE; -.
PhylomeDB; Q7NDN8; -.
BioCyc; GVIO251221:G1G3K-4249-MONOMER; -.
EvolutionaryTrace; Q7NDN8; -.
Proteomes; UP000000557; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006028; GABAA/Glycine_rcpt.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
PANTHER; PTHR18945; PTHR18945; 2.
Pfam; PF02931; Neur_chan_LBD; 1.
PRINTS; PR00253; GABAARECEPTR.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
Potassium; Potassium channel; Potassium transport; Receptor;
Reference proteome; Signal; Sodium; Sodium channel; Sodium transport;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 43 {ECO:0000255}.
CHAIN 44 359 Proton-gated ion channel.
/FTId=PRO_0000412722.
TOPO_DOM 44 235 Periplasmic. {ECO:0000255}.
TRANSMEM 236 258 Helical.
TOPO_DOM 259 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 286 Helical.
TOPO_DOM 287 294 Periplasmic. {ECO:0000255}.
TRANSMEM 295 323 Helical.
TOPO_DOM 324 326 Cytoplasmic. {ECO:0000255}.
TRANSMEM 327 359 Helical.
MUTAGEN 244 244 I->Y: Marked gain of function, with a
ten-fold shift of the proton dose-
response curve towards lower
concentrations.
{ECO:0000269|PubMed:21248852}.
MUTAGEN 264 264 E->A: Decreases cation selectivity.
Decreases the binding affinity of TEA and
TBA. Nearly abolishes block by Cd(2+).
{ECO:0000269|PubMed:18987630,
ECO:0000269|PubMed:21037567}.
MUTAGEN 264 264 E->Q,D: Decreases binding affinity of
TBA. {ECO:0000269|PubMed:18987630,
ECO:0000269|PubMed:21037567}.
MUTAGEN 268 268 T->A: Increases the binding affinity of
TBA. Weakens block by Cd(2+).
{ECO:0000269|PubMed:21037567}.
MUTAGEN 272 272 S->A: Increases the binding affinity of
TBA. {ECO:0000269|PubMed:21037567}.
MUTAGEN 284 284 V->M: Displays an increased sensitivity
to propofol but not to desflurane.
{ECO:0000269|PubMed:21248852}.
MUTAGEN 297 297 T->A: Marked gain of function, with a
ten-fold shift of the proton dose-
response curve towards lower
concentrations. Shows also slower
apparent rate constants for activation
and deactivation. Displays an increased
sensitivity to propofol but a decreased
sensitivity to desflurane.
{ECO:0000269|PubMed:21248852}.
STRAND 53 55 {ECO:0000244|PDB:6F0U}.
STRAND 58 70 {ECO:0000244|PDB:3IGQ}.
STRAND 76 90 {ECO:0000244|PDB:3IGQ}.
HELIX 92 94 {ECO:0000244|PDB:3IGQ}.
HELIX 98 101 {ECO:0000244|PDB:3IGQ}.
STRAND 104 107 {ECO:0000244|PDB:6F0U}.
HELIX 110 112 {ECO:0000244|PDB:3IGQ}.
STRAND 118 126 {ECO:0000244|PDB:3IGQ}.
STRAND 128 136 {ECO:0000244|PDB:3IGQ}.
TURN 138 140 {ECO:0000244|PDB:4F8H}.
STRAND 141 153 {ECO:0000244|PDB:3IGQ}.
TURN 159 162 {ECO:0000244|PDB:6F0U}.
STRAND 165 174 {ECO:0000244|PDB:3IGQ}.
STRAND 178 180 {ECO:0000244|PDB:4QH5}.
STRAND 182 186 {ECO:0000244|PDB:3IGQ}.
HELIX 188 190 {ECO:0000244|PDB:3IGQ}.
STRAND 192 194 {ECO:0000244|PDB:3IGQ}.
STRAND 196 199 {ECO:0000244|PDB:3IGQ}.
STRAND 202 212 {ECO:0000244|PDB:3IGQ}.
STRAND 214 218 {ECO:0000244|PDB:5OSA}.
STRAND 219 221 {ECO:0000244|PDB:3EI0}.
STRAND 225 234 {ECO:0000244|PDB:3IGQ}.
HELIX 236 238 {ECO:0000244|PDB:5IUX}.
HELIX 239 242 {ECO:0000244|PDB:6F0U}.
HELIX 244 254 {ECO:0000244|PDB:6F0U}.
HELIX 255 259 {ECO:0000244|PDB:6F0U}.
HELIX 263 287 {ECO:0000244|PDB:6F0U}.
HELIX 296 323 {ECO:0000244|PDB:6F0U}.
HELIX 327 356 {ECO:0000244|PDB:6F0U}.
SEQUENCE 359 AA; 40986 MW; 6F9009F96172C025 CRC64;
MFPTGWRPKL SESIAASRML WQPMAAVAVV QIGLLWFSPP VWGQDMVSPP PPIADEPLTV
NTGIYLIECY SLDDKAETFK VNAFLSLSWK DRRLAFDPVR SGVRVKTYEP EAIWIPEIRF
VNVENARDAD VVDISVSPDG TVQYLERFSA RVLSPLDFRR YPFDSQTLHI YLIVRSVDTR
NIVLAVDLEK VGKNDDVFLT GWDIESFTAV VKPANFALED RLESKLDYQL RISRQYFSYI
PNIILPMLFI LFISWTAFWS TSYEANVTLV VSTLIAHIAF NILVETNLPK TPYMTYTGAI
IFMIYLFYFV AVIEVTVQHY LKVESQPARA ASITRASRIA FPVVFLLANI ILAFLFFGF


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