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Q7NDN8 (GLIC_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proton-gated ion channel
Alternative name(s):
GLIC
Ligand-gated ion channel
Short name=LGIC
Gene names
Name:glvI
Ordered Locus Names:glr4197
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2

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. Ref.2 Ref.3 Ref.11

Subunit structure

Homopentamer. Ref.2 Ref.8 Ref.9

Subcellular location

Cell inner membrane; Multi-pass membrane protein Probable.

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.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343 Potential
Chain44 – 359316Proton-gated ion channel
PRO_0000412722

Regions

Topological domain44 – 235192Periplasmic Potential
Transmembrane236 – 25823Helical
Topological domain259 – 2613Cytoplasmic Potential
Transmembrane262 – 28625Helical
Topological domain287 – 2948Periplasmic Potential
Transmembrane295 – 32329Helical
Topological domain324 – 3263Cytoplasmic Potential
Transmembrane327 – 35933Helical

Experimental info

Mutagenesis2441I → Y: Marked gain of function, with a ten-fold shift of the proton dose-response curve towards lower concentrations. Ref.13
Mutagenesis2641E → A: Decreases cation selectivity. Decreases the binding affinity of TEA and TBA. Nearly abolishes block by Cd(2+). Ref.9 Ref.11
Mutagenesis2641E → Q or D: Decreases binding affinity of TBA. Ref.9 Ref.11
Mutagenesis2681T → A: Increases the binding affinity of TBA. Weakens block by Cd(2+). Ref.11
Mutagenesis2721S → A: Increases the binding affinity of TBA. Ref.11
Mutagenesis2841V → M: Displays an increased sensitivity to propofol but not to desflurane. Ref.13
Mutagenesis2971T → 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. Ref.13

Secondary structure

...................................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7NDN8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 6F9009F96172C025

FASTA35940,986
        10         20         30         40         50         60 
MFPTGWRPKL SESIAASRML WQPMAAVAVV QIGLLWFSPP VWGQDMVSPP PPIADEPLTV 

        70         80         90        100        110        120 
NTGIYLIECY SLDDKAETFK VNAFLSLSWK DRRLAFDPVR SGVRVKTYEP EAIWIPEIRF 

       130        140        150        160        170        180 
VNVENARDAD VVDISVSPDG TVQYLERFSA RVLSPLDFRR YPFDSQTLHI YLIVRSVDTR 

       190        200        210        220        230        240 
NIVLAVDLEK VGKNDDVFLT GWDIESFTAV VKPANFALED RLESKLDYQL RISRQYFSYI 

       250        260        270        280        290        300 
PNIILPMLFI LFISWTAFWS TSYEANVTLV VSTLIAHIAF NILVETNLPK TPYMTYTGAI 

       310        320        330        340        350 
IFMIYLFYFV AVIEVTVQHY LKVESQPARA ASITRASRIA FPVVFLLANI ILAFLFFGF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
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.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.
[2]"A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family."
Bocquet N., Prado de Carvalho L., Cartaud J., Neyton J., Le Poupon C., Taly A., Grutter T., Changeux J.P., Corringer P.J.
Nature 445:116-119(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PROTON-GATED ION CHANNEL, ION SELECTIVITY, ENZYME REGULATION, SUBUNIT.
Strain: PCC 7421.
[3]"Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel."
Weng Y., Yang L., Corringer P.J., Sonner J.M.
Anesth. Analg. 110:59-63(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MODULATION BY ANESTHETICS, ENZYME REGULATION.
Strain: PCC 7421.
[4]"Anesthetic binding in a pentameric ligand-gated ion channel: GLIC."
Chen Q., Cheng M.H., Xu Y., Tang P.
Biophys. J. 99:1801-1809(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ANESTHETIC-BINDING, MUTAGENESIS STUDIES, FLUORESCENCE QUENCHING EXPERIMENTS.
Strain: PCC 7421.
[5]"Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues."
Corringer P.J., Baaden M., Bocquet N., Delarue M., Dufresne V., Nury H., Prevost M., Van Renterghem C.
J. Physiol. (Lond.) 588:565-572(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Pore opening and closing of a pentameric ligand-gated ion channel."
Zhu F., Hummer G.
Proc. Natl. Acad. Sci. U.S.A. 107:19814-19819(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GATING MECHANISM.
[7]"Ion selectivity mechanism in a bacterial pentameric ligand-gated ion channel."
Fritsch S., Ivanov I., Wang H., Cheng X.
Biophys. J. 100:390-398(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ION SELECTIVITY MECHANISM.
[8]"X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation."
Bocquet N., Nury H., Baaden M., Le Poupon C., Changeux J.P., Delarue M., Corringer P.J.
Nature 457:111-114(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 44-359, SUBUNIT.
Strain: PCC 7421.
[9]"Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel."
Hilf R.J., Dutzler R.
Nature 457:115-118(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 43-359 OF WILD-TYPE AND MUTANT ALA-264, SUBUNIT, MUTAGENESIS OF GLU-264.
Strain: PCC 7421.
[10]"Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel."
Nury H., Bocquet N., Le Poupon C., Raynal B., Haouz A., Corringer P.J., Delarue M.
J. Mol. Biol. 395:1114-1127(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 44-235, GATING MECHANISM.
Strain: PCC 7421.
[11]"Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel."
Hilf R.J., Bertozzi C., Zimmermann I., Reiter A., Trauner D., Dutzler R.
Nat. Struct. Mol. Biol. 17:1330-1336(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, MECHANISMS OF OPEN CHANNEL BLOCK.
Strain: PCC 7421.
[12]"One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue."
Nury H., Poitevin F., Van Renterghem C., Changeux J.P., Corringer P.J., Delarue M., Baaden M.
Proc. Natl. Acad. Sci. U.S.A. 107:6275-6280(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 44-359 OF MUTANT PHE-279.
Strain: PCC 7421.
[13]"X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel."
Nury H., Van Renterghem C., Weng Y., Tran A., Baaden M., Dusfresne V., Changeux J.P., Sonner J.M., Delarue M., Corringer P.J.
Nature 469:428-431(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 44-359 IN COMPLEXES WITH PROPOFOL AND DESFLURANE ANESTHETICS, MUTAGENESIS OF ILE-244; VAL-284 AND THR-297.
Strain: PCC 7421.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC92138.1.
RefSeqNP_927143.1. NC_005125.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XQ3X-ray3.50A/B/C/D/E43-359[»]
2XQ4X-ray3.60A/B/C/D/E43-359[»]
2XQ5X-ray3.50A/B/C/D/E43-359[»]
2XQ6X-ray3.70A/B/C/D/E43-359[»]
2XQ7X-ray3.40A/B/C/D/E43-359[»]
2XQ8X-ray3.60A/B/C/D/E43-359[»]
2XQ9X-ray3.20A/B/C/D/E43-359[»]
2XQAX-ray3.70A/B/C/D/E43-359[»]
3EAMX-ray2.90A/B/C/D/E44-359[»]
3EHZX-ray3.10A/B/C/D/E43-359[»]
3EI0X-ray3.50A/B/C/D/E43-359[»]
3IGQX-ray2.30A/B/C/D/E/F44-235[»]
3LSVX-ray3.15A/B/C/D/E44-359[»]
3P4WX-ray3.20A/B/C/D/E44-359[»]
3P50X-ray3.30A/B/C/D/E44-359[»]
3TLSX-ray3.20A/B/C/D/E44-359[»]
3TLTX-ray3.30A/B/C/D/E44-359[»]
3TLUX-ray2.85A/B/C/D/E44-359[»]
3TLVX-ray2.90A/B/C/D/E44-359[»]
3TLWX-ray2.60A/B/C/D/E44-359[»]
3UU3X-ray3.15A/B/C/D/E44-359[»]
3UU4X-ray3.05A/B/C/D/E44-359[»]
3UU5X-ray2.90A/B/C/D/E44-359[»]
3UU6X-ray2.98A/B/C/D/E44-359[»]
3UU8X-ray3.25A/B/C/D/E44-359[»]
3UUBX-ray2.90A/B/C/D/E/F/G/H/I/J44-359[»]
4F8HX-ray2.99A/B/C/D/E43-359[»]
4HFBX-ray2.75A/B/C/D/E44-359[»]
4HFCX-ray3.05A/B/C/D/E44-359[»]
4HFDX-ray3.10A/B/C/D/E44-359[»]
4HFEX-ray2.80A/B/C/D/E44-359[»]
4HFHX-ray2.65A/B/C/D/E44-359[»]
4HFIX-ray2.40A/B/C/D/E44-359[»]
4IL4X-ray3.30A/B/C/D/E44-359[»]
4IL9X-ray2.83A/B/C/D/E44-358[»]
4ILAX-ray3.50A/B/C/D/E44-358[»]
4ILBX-ray3.15A/B/C/D/E44-358[»]
4ILCX-ray2.99A/B/C/D/E44-358[»]
4IREX-ray3.19A/B/C/D/E43-359[»]
4LMJX-ray3.44A/B/C/D/E44-359[»]
4LMKX-ray3.22A/B/C/D/E44-359[»]
4LMLX-ray3.80A/B/C/D/E44-359[»]
4NPPX-ray3.35A/B/C/D/E44-359[»]
4NPQX-ray4.35A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T44-359[»]
ProteinModelPortalQ7NDN8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59040N.
MINTMINT-8425450.
STRING251221.glr4197.

Protein family/group databases

TCDB1.A.9.8.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC92138; BAC92138; BAC92138.
GeneID2602600.
KEGGgvi:glr4197.
PATRIC22047895. VBIGloVio86258_4229.

Phylogenomic databases

OMAISFTYEA.
OrthoDBEOG6VF30W.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-4249-MONOMER.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006028. GABAA_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00253. GABAARECEPTR.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ7NDN8.

Entry information

Entry nameGLIC_GLOVI
AccessionPrimary (citable) accession number: Q7NDN8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references