GLIC_GLOVI
ID GLIC_GLOVI Reviewed; 359 AA.
AC Q7NDN8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Proton-gated ion channel;
DE AltName: Full=GLIC;
DE AltName: Full=Ligand-gated ion channel;
DE Short=LGIC;
DE Flags: Precursor;
GN Name=glvI; OrderedLocusNames=glr4197;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
RN [2]
RP FUNCTION AS A PROTON-GATED ION CHANNEL, ION SELECTIVITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=17167423; DOI=10.1038/nature05371;
RA Bocquet N., Prado de Carvalho L., Cartaud J., Neyton J., Le Poupon C.,
RA Taly A., Grutter T., Changeux J.P., Corringer P.J.;
RT "A prokaryotic proton-gated ion channel from the nicotinic acetylcholine
RT receptor family.";
RL Nature 445:116-119(2007).
RN [3]
RP MODULATION BY ANESTHETICS, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=19933531; DOI=10.1213/ane.0b013e3181c4bc69;
RA Weng Y., Yang L., Corringer P.J., Sonner J.M.;
RT "Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion
RT channel.";
RL Anesth. Analg. 110:59-63(2010).
RN [4]
RP ANESTHETIC-BINDING, MUTAGENESIS STUDIES, AND FLUORESCENCE QUENCHING
RP EXPERIMENTS.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=20858424; DOI=10.1016/j.bpj.2010.07.023;
RA Chen Q., Cheng M.H., Xu Y., Tang P.;
RT "Anesthetic binding in a pentameric ligand-gated ion channel: GLIC.";
RL Biophys. J. 99:1801-1809(2010).
RN [5]
RP REVIEW.
RX PubMed=19995852; DOI=10.1113/jphysiol.2009.183160;
RA Corringer P.J., Baaden M., Bocquet N., Delarue M., Dufresne V., Nury H.,
RA Prevost M., Van Renterghem C.;
RT "Atomic structure and dynamics of pentameric ligand-gated ion channels: new
RT insight from bacterial homologues.";
RL J. Physiol. (Lond.) 588:565-572(2010).
RN [6]
RP GATING MECHANISM.
RX PubMed=21041674; DOI=10.1073/pnas.1009313107;
RA Zhu F., Hummer G.;
RT "Pore opening and closing of a pentameric ligand-gated ion channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19814-19819(2010).
RN [7]
RP ION SELECTIVITY MECHANISM.
RX PubMed=21244835; DOI=10.1016/j.bpj.2010.11.077;
RA Fritsch S., Ivanov I., Wang H., Cheng X.;
RT "Ion selectivity mechanism in a bacterial pentameric ligand-gated ion
RT channel.";
RL Biophys. J. 100:390-398(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 44-359, AND SUBUNIT.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=18987633; DOI=10.1038/nature07462;
RA Bocquet N., Nury H., Baaden M., Le Poupon C., Changeux J.P., Delarue M.,
RA Corringer P.J.;
RT "X-ray structure of a pentameric ligand-gated ion channel in an apparently
RT open conformation.";
RL Nature 457:111-114(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 43-359 OF WILD-TYPE AND MUTANT
RP ALA-264, SUBUNIT, AND MUTAGENESIS OF GLU-264.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=18987630; DOI=10.1038/nature07461;
RA Hilf R.J., Dutzler R.;
RT "Structure of a potentially open state of a proton-activated pentameric
RT ligand-gated ion channel.";
RL Nature 457:115-118(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 44-235, AND GATING MECHANISM.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=19917292; DOI=10.1016/j.jmb.2009.11.024;
RA Nury H., Bocquet N., Le Poupon C., Raynal B., Haouz A., Corringer P.J.,
RA Delarue M.;
RT "Crystal structure of the extracellular domain of a bacterial ligand-gated
RT ion channel.";
RL J. Mol. Biol. 395:1114-1127(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 43-359 OF WILD-TYPE AND MUTANT
RP ASP-264 IN COMPLEXES WITH POSITIVELY CHARGED INHIBITORS, ACTIVITY
RP REGULATION, MUTAGENESIS OF GLU-264; THR-268 AND SER-272, AND MECHANISMS OF
RP OPEN CHANNEL BLOCK.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=21037567; DOI=10.1038/nsmb.1933;
RA Hilf R.J., Bertozzi C., Zimmermann I., Reiter A., Trauner D., Dutzler R.;
RT "Structural basis of open channel block in a prokaryotic pentameric ligand-
RT gated ion channel.";
RL Nat. Struct. Mol. Biol. 17:1330-1336(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 44-359 OF MUTANT PHE-279.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=20308576; DOI=10.1073/pnas.1001832107;
RA Nury H., Poitevin F., Van Renterghem C., Changeux J.P., Corringer P.J.,
RA Delarue M., Baaden M.;
RT "One-microsecond molecular dynamics simulation of channel gating in a
RT nicotinic receptor homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6275-6280(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 44-359 IN COMPLEXES WITH PROPOFOL
RP AND DESFLURANE ANESTHETICS, AND MUTAGENESIS OF ILE-244; VAL-284 AND
RP THR-297.
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=21248852; DOI=10.1038/nature09647;
RA Nury H., Van Renterghem C., Weng Y., Tran A., Baaden M., Dusfresne V.,
RA Changeux J.P., Sonner J.M., Delarue M., Corringer P.J.;
RT "X-ray structures of general anaesthetics bound to a pentameric ligand-
RT gated ion channel.";
RL Nature 469:428-431(2011).
CC -!- FUNCTION: Cationic channel with similar permeabilities for Na(+) and
CC K(+), that is activated by an increase of the proton concentration on
CC the extracellular side. Displays no permeability for chloride ions.
CC Shows slow kinetics of activation, no desensitization and a single
CC channel conductance of 8 pS. Might contribute to adaptation to external
CC pH change. {ECO:0000269|PubMed:17167423}.
CC -!- ACTIVITY REGULATION: Tetraethylammonium (TEA) and tetrabutylammonium
CC (TBA) inhibit the proton-activated currents in a dose- and voltage-
CC dependent manner in vitro, whereas the blocker of acid sensing ion
CC channels, amiloride, has no effect. Channel current of GLIC can be
CC inhibited by inhaled and intravenous general anesthetics at and below
CC concentrations used clinically. Ion conduction is also inhibited by
CC lidocaine and by divalent transition metal ions such as cadmium ions.
CC {ECO:0000269|PubMed:17167423, ECO:0000269|PubMed:19933531,
CC ECO:0000269|PubMed:21037567}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:17167423,
CC ECO:0000269|PubMed:18987630, ECO:0000269|PubMed:18987633}.
CC -!- INTERACTION:
CC Q7NDN8; Q7NDN8: glvI; NbExp=26; IntAct=EBI-8423601, EBI-8423601;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Consists of an N-terminal ligand-binding domain that encloses a
CC wide aqueous vestibule and a transmembrane domain that forms a narrow
CC channel.
CC -!- MISCELLANEOUS: The homologous nature of GLIC to eukaryotic nicotinic
CC acetylcholine receptors and other eukaryotic pentameric ligand-gated
CC ion channels, and its sensitivity to general anesthetics, define GLIC
CC as a structural and functional model of signal transduction in the
CC nervous system, also relevant for exploring the molecular basis of
CC anesthetic action.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000305}.
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DR EMBL; BA000045; BAC92138.1; -; Genomic_DNA.
DR RefSeq; NP_927143.1; NC_005125.1.
DR RefSeq; WP_011144181.1; NC_005125.1.
DR PDB; 2XQ3; X-ray; 3.50 A; A/B/C/D/E=43-359.
DR PDB; 2XQ4; X-ray; 3.60 A; A/B/C/D/E=43-359.
DR PDB; 2XQ5; X-ray; 3.50 A; A/B/C/D/E=43-359.
DR PDB; 2XQ6; X-ray; 3.70 A; A/B/C/D/E=43-359.
DR PDB; 2XQ7; X-ray; 3.40 A; A/B/C/D/E=43-359.
DR PDB; 2XQ8; X-ray; 3.60 A; A/B/C/D/E=43-359.
DR PDB; 2XQ9; X-ray; 3.20 A; A/B/C/D/E=43-359.
DR PDB; 2XQA; X-ray; 3.70 A; A/B/C/D/E=43-359.
DR PDB; 3EAM; X-ray; 2.90 A; A/B/C/D/E=44-359.
DR PDB; 3EHZ; X-ray; 3.10 A; A/B/C/D/E=50-359.
DR PDB; 3EI0; X-ray; 3.50 A; A/B/C/D/E=50-359.
DR PDB; 3IGQ; X-ray; 2.30 A; A/B/C/D/E/F=44-235.
DR PDB; 3LSV; X-ray; 3.15 A; A/B/C/D/E=44-359.
DR PDB; 3P4W; X-ray; 3.20 A; A/B/C/D/E=44-359.
DR PDB; 3P50; X-ray; 3.30 A; A/B/C/D/E=44-359.
DR PDB; 3TLS; X-ray; 3.20 A; A/B/C/D/E=44-359.
DR PDB; 3TLT; X-ray; 3.30 A; A/B/C/D/E=44-359.
DR PDB; 3TLU; X-ray; 2.85 A; A/B/C/D/E=44-359.
DR PDB; 3TLV; X-ray; 2.90 A; A/B/C/D/E=44-359.
DR PDB; 3TLW; X-ray; 2.60 A; A/B/C/D/E=44-359.
DR PDB; 3UU3; X-ray; 3.15 A; A/B/C/D/E=44-359.
DR PDB; 3UU4; X-ray; 3.05 A; A/B/C/D/E=44-359.
DR PDB; 3UU5; X-ray; 2.90 A; A/B/C/D/E=44-359.
DR PDB; 3UU6; X-ray; 2.98 A; A/B/C/D/E=44-359.
DR PDB; 3UU8; X-ray; 3.25 A; A/B/C/D/E=44-359.
DR PDB; 3UUB; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=44-359.
DR PDB; 4F8H; X-ray; 2.99 A; A/B/C/D/E=43-359.
DR PDB; 4HFB; X-ray; 2.75 A; A/B/C/D/E=44-359.
DR PDB; 4HFC; X-ray; 3.05 A; A/B/C/D/E=44-359.
DR PDB; 4HFD; X-ray; 3.10 A; A/B/C/D/E=44-359.
DR PDB; 4HFE; X-ray; 2.80 A; A/B/C/D/E=44-359.
DR PDB; 4HFH; X-ray; 2.65 A; A/B/C/D/E=44-359.
DR PDB; 4HFI; X-ray; 2.40 A; A/B/C/D/E=44-359.
DR PDB; 4IL4; X-ray; 3.30 A; A/B/C/D/E=44-359.
DR PDB; 4IL9; X-ray; 2.83 A; A/B/C/D/E=44-358.
DR PDB; 4ILA; X-ray; 3.50 A; A/B/C/D/E=44-358.
DR PDB; 4ILB; X-ray; 3.15 A; A/B/C/D/E=44-358.
DR PDB; 4ILC; X-ray; 2.99 A; A/B/C/D/E=44-358.
DR PDB; 4IRE; X-ray; 3.19 A; A/B/C/D/E=43-359.
DR PDB; 4LMJ; X-ray; 3.44 A; A/B/C/D/E=44-359.
DR PDB; 4LMK; X-ray; 3.22 A; A/B/C/D/E=44-359.
DR PDB; 4LML; X-ray; 3.80 A; A/B/C/D/E=44-359.
DR PDB; 4NPP; X-ray; 3.35 A; A/B/C/D/E=44-359.
DR 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.
DR PDB; 4QH1; X-ray; 3.40 A; A/B/C/D/E=44-359.
DR PDB; 4QH4; X-ray; 3.20 A; A/B/C/D/E=44-359.
DR PDB; 4QH5; X-ray; 3.00 A; A/B/C/D/E=44-359.
DR PDB; 4X5T; X-ray; 3.50 A; A/B/C/D/E=44-235.
DR PDB; 4YEU; X-ray; 4.60 A; A/B/C/D/E=236-357.
DR PDB; 4ZZB; X-ray; 3.40 A; A/B/C/D/E=44-359.
DR PDB; 4ZZC; X-ray; 3.10 A; A/B/C/D/E=43-359.
DR PDB; 5HCJ; X-ray; 2.95 A; A/B/C/D/E=44-359.
DR PDB; 5HCM; X-ray; 3.15 A; A/B/C/D/E=44-359.
DR PDB; 5HEG; X-ray; 3.21 A; A/B/C/D/E=44-359.
DR PDB; 5HEH; X-ray; 3.30 A; A/B/C/D/E=44-359.
DR PDB; 5IUX; X-ray; 2.60 A; A/B/C/D/E=43-359.
DR PDB; 5J0Z; X-ray; 3.25 A; A/B/C/D/E=47-357.
DR PDB; 5L47; X-ray; 3.30 A; A/B/C/D/E=43-359.
DR PDB; 5L4E; X-ray; 3.50 A; A/B/C/D/E=43-359.
DR PDB; 5L4H; X-ray; 3.30 A; A/B/C/D/E=43-359.
DR PDB; 5MUO; X-ray; 3.19 A; A/B/C/D/E=44-359.
DR PDB; 5MUR; X-ray; 3.10 A; A/B/C/D/E=43-359.
DR PDB; 5MVM; X-ray; 3.10 A; A/B/C/D/E=43-359.
DR PDB; 5MVN; X-ray; 3.49 A; A/B/C/D/E=43-359.
DR PDB; 5MZQ; X-ray; 2.80 A; A/B/C/D/E=43-359.
DR PDB; 5MZR; X-ray; 2.65 A; A/B/C/D/E=43-359.
DR PDB; 5MZT; X-ray; 2.65 A; A/B/C/D/E=43-359.
DR PDB; 5NJY; X-ray; 2.95 A; A/B/C/D/E=43-359.
DR PDB; 5NKJ; X-ray; 3.74 A; A/B/C/D/E=43-359.
DR PDB; 5OSA; X-ray; 2.75 A; A/B/C/D/E=44-236.
DR PDB; 5OSB; X-ray; 3.80 A; A/B/C/D/E=44-236.
DR PDB; 5OSC; X-ray; 3.10 A; A/B/C/D/E=44-236.
DR PDB; 5V6N; X-ray; 3.35 A; A/B/C/D/E=50-359.
DR PDB; 5V6O; X-ray; 3.12 A; A/B/C/D/E=50-359.
DR PDB; 6EMX; X-ray; 3.20 A; A/B/C/D/E=43-359.
DR PDB; 6F0I; X-ray; 3.00 A; A/B/C/D/E=43-359.
DR PDB; 6F0J; X-ray; 3.15 A; A/B/C/D/E=43-359.
DR PDB; 6F0M; X-ray; 2.65 A; A/B/C/D/E=43-359.
DR PDB; 6F0N; X-ray; 3.20 A; A/B/C/D/E=43-359.
DR PDB; 6F0R; X-ray; 2.50 A; A/B/C/D/E=43-359.
DR PDB; 6F0U; X-ray; 2.35 A; A/B/C/D/E=43-359.
DR PDB; 6F0V; X-ray; 2.85 A; A/B/C/D/E=43-359.
DR PDB; 6F0Z; X-ray; 2.50 A; A/B/C/D/E=43-359.
DR PDB; 6F10; X-ray; 2.85 A; A/B/C/D/E=43-359.
DR PDB; 6F11; X-ray; 2.95 A; A/B/C/D/E=43-359.
DR PDB; 6F12; X-ray; 3.20 A; A/B/C/D/E=43-359.
DR PDB; 6F13; X-ray; 2.70 A; A/B/C/D/E=43-359.
DR PDB; 6F15; X-ray; 2.85 A; A/B/C/D/E=43-359.
DR PDB; 6F16; X-ray; 2.60 A; A/B/C/D/E=43-359.
DR PDB; 6F7A; X-ray; 6.00 A; A/B/C/D/E=47-357.
DR PDB; 6HJ3; X-ray; 2.70 A; A/B/C/D/E=43-359.
DR PDB; 6HJA; X-ray; 2.70 A; A/B/C/D/E=1-359.
DR PDB; 6HJB; X-ray; 3.00 A; A/B/C/D/E=1-359.
DR PDB; 6HJI; X-ray; 2.80 A; A/B/C/D/E=43-359.
DR PDB; 6HJZ; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=43-359.
DR PDB; 6HPP; X-ray; 3.20 A; A/B/C/D/E=43-359.
DR PDB; 6HY5; X-ray; 2.58 A; A/B/C/D/E=47-357.
DR PDB; 6HY9; X-ray; 2.95 A; A/B/C/D/E=44-359.
DR PDB; 6HYA; X-ray; 3.39 A; A/B/C/D/E=43-359.
DR PDB; 6HYR; X-ray; 3.50 A; A/B/C/D/E=47-357.
DR PDB; 6HYV; X-ray; 2.80 A; A/B/C/D/E=43-359.
DR PDB; 6HYW; X-ray; 2.80 A; A/B/C/D/E=43-359.
DR PDB; 6HYX; X-ray; 3.00 A; A/B/C/D/E=43-359.
DR PDB; 6HYZ; X-ray; 3.05 A; A/B/C/D/E=43-359.
DR PDB; 6HZ0; X-ray; 2.75 A; A/B/C/D/E=43-359.
DR PDB; 6HZ1; X-ray; 2.50 A; A/B/C/D/E=44-359.
DR PDB; 6HZ3; X-ray; 3.15 A; A/B/C/D/E=43-359.
DR PDB; 6HZW; X-ray; 2.22 A; A/B/C/D/E=43-359.
DR PDB; 6I08; X-ray; 3.00 A; A/B/C/D/E=43-359.
DR PDB; 6ZGD; EM; 4.10 A; A/B/C/D/E=44-359.
DR PDB; 6ZGJ; EM; 3.40 A; A/B/C/D/E=44-359.
DR PDB; 6ZGK; EM; 3.60 A; A/B/C/D/E=44-359.
DR PDBsum; 2XQ3; -.
DR PDBsum; 2XQ4; -.
DR PDBsum; 2XQ5; -.
DR PDBsum; 2XQ6; -.
DR PDBsum; 2XQ7; -.
DR PDBsum; 2XQ8; -.
DR PDBsum; 2XQ9; -.
DR PDBsum; 2XQA; -.
DR PDBsum; 3EAM; -.
DR PDBsum; 3EHZ; -.
DR PDBsum; 3EI0; -.
DR PDBsum; 3IGQ; -.
DR PDBsum; 3LSV; -.
DR PDBsum; 3P4W; -.
DR PDBsum; 3P50; -.
DR PDBsum; 3TLS; -.
DR PDBsum; 3TLT; -.
DR PDBsum; 3TLU; -.
DR PDBsum; 3TLV; -.
DR PDBsum; 3TLW; -.
DR PDBsum; 3UU3; -.
DR PDBsum; 3UU4; -.
DR PDBsum; 3UU5; -.
DR PDBsum; 3UU6; -.
DR PDBsum; 3UU8; -.
DR PDBsum; 3UUB; -.
DR PDBsum; 4F8H; -.
DR PDBsum; 4HFB; -.
DR PDBsum; 4HFC; -.
DR PDBsum; 4HFD; -.
DR PDBsum; 4HFE; -.
DR PDBsum; 4HFH; -.
DR PDBsum; 4HFI; -.
DR PDBsum; 4IL4; -.
DR PDBsum; 4IL9; -.
DR PDBsum; 4ILA; -.
DR PDBsum; 4ILB; -.
DR PDBsum; 4ILC; -.
DR PDBsum; 4IRE; -.
DR PDBsum; 4LMJ; -.
DR PDBsum; 4LMK; -.
DR PDBsum; 4LML; -.
DR PDBsum; 4NPP; -.
DR PDBsum; 4NPQ; -.
DR PDBsum; 4QH1; -.
DR PDBsum; 4QH4; -.
DR PDBsum; 4QH5; -.
DR PDBsum; 4X5T; -.
DR PDBsum; 4YEU; -.
DR PDBsum; 4ZZB; -.
DR PDBsum; 4ZZC; -.
DR PDBsum; 5HCJ; -.
DR PDBsum; 5HCM; -.
DR PDBsum; 5HEG; -.
DR PDBsum; 5HEH; -.
DR PDBsum; 5IUX; -.
DR PDBsum; 5J0Z; -.
DR PDBsum; 5L47; -.
DR PDBsum; 5L4E; -.
DR PDBsum; 5L4H; -.
DR PDBsum; 5MUO; -.
DR PDBsum; 5MUR; -.
DR PDBsum; 5MVM; -.
DR PDBsum; 5MVN; -.
DR PDBsum; 5MZQ; -.
DR PDBsum; 5MZR; -.
DR PDBsum; 5MZT; -.
DR PDBsum; 5NJY; -.
DR PDBsum; 5NKJ; -.
DR PDBsum; 5OSA; -.
DR PDBsum; 5OSB; -.
DR PDBsum; 5OSC; -.
DR PDBsum; 5V6N; -.
DR PDBsum; 5V6O; -.
DR PDBsum; 6EMX; -.
DR PDBsum; 6F0I; -.
DR PDBsum; 6F0J; -.
DR PDBsum; 6F0M; -.
DR PDBsum; 6F0N; -.
DR PDBsum; 6F0R; -.
DR PDBsum; 6F0U; -.
DR PDBsum; 6F0V; -.
DR PDBsum; 6F0Z; -.
DR PDBsum; 6F10; -.
DR PDBsum; 6F11; -.
DR PDBsum; 6F12; -.
DR PDBsum; 6F13; -.
DR PDBsum; 6F15; -.
DR PDBsum; 6F16; -.
DR PDBsum; 6F7A; -.
DR PDBsum; 6HJ3; -.
DR PDBsum; 6HJA; -.
DR PDBsum; 6HJB; -.
DR PDBsum; 6HJI; -.
DR PDBsum; 6HJZ; -.
DR PDBsum; 6HPP; -.
DR PDBsum; 6HY5; -.
DR PDBsum; 6HY9; -.
DR PDBsum; 6HYA; -.
DR PDBsum; 6HYR; -.
DR PDBsum; 6HYV; -.
DR PDBsum; 6HYW; -.
DR PDBsum; 6HYX; -.
DR PDBsum; 6HYZ; -.
DR PDBsum; 6HZ0; -.
DR PDBsum; 6HZ1; -.
DR PDBsum; 6HZ3; -.
DR PDBsum; 6HZW; -.
DR PDBsum; 6I08; -.
DR PDBsum; 6ZGD; -.
DR PDBsum; 6ZGJ; -.
DR PDBsum; 6ZGK; -.
DR AlphaFoldDB; Q7NDN8; -.
DR BMRB; Q7NDN8; -.
DR SASBDB; Q7NDN8; -.
DR SMR; Q7NDN8; -.
DR DIP; DIP-59040N; -.
DR MINT; Q7NDN8; -.
DR STRING; 251221.35214771; -.
DR TCDB; 1.A.9.8.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR EnsemblBacteria; BAC92138; BAC92138; BAC92138.
DR KEGG; gvi:glr4197; -.
DR eggNOG; COG5361; Bacteria.
DR HOGENOM; CLU_010920_3_0_3; -.
DR InParanoid; Q7NDN8; -.
DR OMA; TTVTCNM; -.
DR OrthoDB; 1795552at2; -.
DR PhylomeDB; Q7NDN8; -.
DR EvolutionaryTrace; Q7NDN8; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Potassium;
KW Potassium channel; Potassium transport; Receptor; Reference proteome;
KW Signal; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..359
FT /note="Proton-gated ion channel"
FT /id="PRO_0000412722"
FT TOPO_DOM 44..235
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..258
FT /note="Helical"
FT TOPO_DOM 259..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..286
FT /note="Helical"
FT TOPO_DOM 287..294
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..323
FT /note="Helical"
FT TOPO_DOM 324..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..359
FT /note="Helical"
FT MUTAGEN 244
FT /note="I->Y: Marked gain of function, with a ten-fold shift
FT of the proton dose-response curve towards lower
FT concentrations."
FT /evidence="ECO:0000269|PubMed:21248852"
FT MUTAGEN 264
FT /note="E->A: Decreases cation selectivity. Decreases the
FT binding affinity of TEA and TBA. Nearly abolishes block by
FT Cd(2+)."
FT /evidence="ECO:0000269|PubMed:18987630,
FT ECO:0000269|PubMed:21037567"
FT MUTAGEN 264
FT /note="E->Q,D: Decreases binding affinity of TBA."
FT /evidence="ECO:0000269|PubMed:18987630,
FT ECO:0000269|PubMed:21037567"
FT MUTAGEN 268
FT /note="T->A: Increases the binding affinity of TBA. Weakens
FT block by Cd(2+)."
FT /evidence="ECO:0000269|PubMed:21037567"
FT MUTAGEN 272
FT /note="S->A: Increases the binding affinity of TBA."
FT /evidence="ECO:0000269|PubMed:21037567"
FT MUTAGEN 284
FT /note="V->M: Displays an increased sensitivity to propofol
FT but not to desflurane."
FT /evidence="ECO:0000269|PubMed:21248852"
FT MUTAGEN 297
FT /note="T->A: Marked gain of function, with a ten-fold shift
FT of the proton dose-response curve towards lower
FT concentrations. Shows also slower apparent rate constants
FT for activation and deactivation. Displays an increased
FT sensitivity to propofol but a decreased sensitivity to
FT desflurane."
FT /evidence="ECO:0000269|PubMed:21248852"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 58..73
FT /evidence="ECO:0007829|PDB:6HZW"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:6F0U"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6HZW"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6HZ0"
FT STRAND 141..153
FT /evidence="ECO:0007829|PDB:6HZW"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5NJY"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3IGQ"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3IGQ"
FT STRAND 202..218
FT /evidence="ECO:0007829|PDB:6HZW"
FT STRAND 221..234
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5IUX"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 263..286
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 296..323
FT /evidence="ECO:0007829|PDB:6HZW"
FT HELIX 327..356
FT /evidence="ECO:0007829|PDB:6HZW"
SQ 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
