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Protein

Proton-gated ion channel

Gene

glvI

Organism
Gloeobacter violaceus (strain PCC 7421)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

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.3 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Potassium channel, Receptor, Sodium channel

Keywords - Biological processi

Ion transport, Potassium transport, Sodium transport, Transport

Keywords - Ligandi

Potassium, Sodium

Protein family/group databases

TCDBi1.A.9.8.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Proton-gated ion channel
Alternative name(s):
GLIC
Ligand-gated ion channel
Short name:
LGIC
Gene namesi
Name:glvI
Ordered Locus Names:glr4197
OrganismiGloeobacter violaceus (strain PCC 7421)
Taxonomic identifieri251221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacteraceaeGloeobacter
Proteomesi
  • UP000000557 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini44 – 235PeriplasmicSequence analysisAdd BLAST192
Transmembranei236 – 258HelicalAdd BLAST23
Topological domaini259 – 261CytoplasmicSequence analysis3
Transmembranei262 – 286HelicalAdd BLAST25
Topological domaini287 – 294PeriplasmicSequence analysis8
Transmembranei295 – 323HelicalAdd BLAST29
Topological domaini324 – 326CytoplasmicSequence analysis3
Transmembranei327 – 359HelicalAdd BLAST33

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi244I → Y: Marked gain of function, with a ten-fold shift of the proton dose-response curve towards lower concentrations. 1 Publication1
Mutagenesisi264E → A: Decreases cation selectivity. Decreases the binding affinity of TEA and TBA. Nearly abolishes block by Cd(2+). 2 Publications1
Mutagenesisi264E → Q or D: Decreases binding affinity of TBA. 2 Publications1
Mutagenesisi268T → A: Increases the binding affinity of TBA. Weakens block by Cd(2+). 1 Publication1
Mutagenesisi272S → A: Increases the binding affinity of TBA. 1 Publication1
Mutagenesisi284V → M: Displays an increased sensitivity to propofol but not to desflurane. 1 Publication1
Mutagenesisi297T → 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. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 43Sequence analysisAdd BLAST43
ChainiPRO_000041272244 – 359Proton-gated ion channelAdd BLAST316

Interactioni

Subunit structurei

Homopentamer.3 Publications

Protein-protein interaction databases

DIPiDIP-59040N.
MINTiMINT-8425450.
STRINGi251221.glr4197.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi53 – 55Combined sources3
Beta strandi58 – 70Combined sources13
Beta strandi76 – 90Combined sources15
Helixi92 – 94Combined sources3
Helixi98 – 101Combined sources4
Beta strandi104 – 107Combined sources4
Helixi110 – 112Combined sources3
Beta strandi118 – 126Combined sources9
Beta strandi128 – 136Combined sources9
Turni138 – 140Combined sources3
Beta strandi141 – 153Combined sources13
Turni159 – 162Combined sources4
Beta strandi165 – 174Combined sources10
Beta strandi178 – 180Combined sources3
Beta strandi182 – 186Combined sources5
Helixi188 – 190Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi196 – 199Combined sources4
Beta strandi202 – 212Combined sources11
Beta strandi219 – 221Combined sources3
Beta strandi225 – 234Combined sources10
Helixi236 – 238Combined sources3
Helixi239 – 242Combined sources4
Helixi244 – 254Combined sources11
Helixi255 – 259Combined sources5
Helixi263 – 286Combined sources24
Helixi296 – 323Combined sources28
Helixi327 – 356Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/E50-359[»]
3EI0X-ray3.50A/B/C/D/E50-359[»]
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[»]
4QH1X-ray3.40A/B/C/D/E44-359[»]
4QH4X-ray3.20A/B/C/D/E44-359[»]
4QH5X-ray3.00A/B/C/D/E44-359[»]
4X5TX-ray3.50A/B/C/D/E44-235[»]
4YEUX-ray4.60A/B/C/D/E236-357[»]
4ZZBX-ray3.40A/B/C/D/E44-359[»]
4ZZCX-ray3.10A/B/C/D/E43-359[»]
5HCJX-ray2.95A/B/C/D/E44-359[»]
5HCMX-ray3.15A/B/C/D/E44-359[»]
5HEGX-ray3.21A/B/C/D/E44-359[»]
5HEHX-ray3.30A/B/C/D/E44-359[»]
ProteinModelPortaliQ7NDN8.
SMRiQ7NDN8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7NDN8.

Family & Domainsi

Domaini

Consists of an N-terminal ligand-binding domain that encloses a wide aqueous vestibule and a transmembrane domain that forms a narrow channel.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105TA1. Bacteria.
ENOG4111U8M. LUCA.
InParanoidiQ7NDN8.
OMAiRESWIDK.
OrthoDBiPOG091H13WE.
PhylomeDBiQ7NDN8.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
[Graphical view]
PRINTSiPR00253. GABAARECEPTR.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7NDN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPTGWRPKL SESIAASRML WQPMAAVAVV QIGLLWFSPP VWGQDMVSPP
60 70 80 90 100
PPIADEPLTV NTGIYLIECY SLDDKAETFK VNAFLSLSWK DRRLAFDPVR
110 120 130 140 150
SGVRVKTYEP EAIWIPEIRF VNVENARDAD VVDISVSPDG TVQYLERFSA
160 170 180 190 200
RVLSPLDFRR YPFDSQTLHI YLIVRSVDTR NIVLAVDLEK VGKNDDVFLT
210 220 230 240 250
GWDIESFTAV VKPANFALED RLESKLDYQL RISRQYFSYI PNIILPMLFI
260 270 280 290 300
LFISWTAFWS TSYEANVTLV VSTLIAHIAF NILVETNLPK TPYMTYTGAI
310 320 330 340 350
IFMIYLFYFV AVIEVTVQHY LKVESQPARA ASITRASRIA FPVVFLLANI

ILAFLFFGF
Length:359
Mass (Da):40,986
Last modified:December 15, 2003 - v1
Checksum:i6F9009F96172C025
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000045 Genomic DNA. Translation: BAC92138.1.
RefSeqiNP_927143.1. NC_005125.1.
WP_011144181.1. NC_005125.1.

Genome annotation databases

EnsemblBacteriaiBAC92138; BAC92138; BAC92138.
GeneIDi2602600.
KEGGigvi:glr4197.
PATRICi22047895. VBIGloVio86258_4229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000045 Genomic DNA. Translation: BAC92138.1.
RefSeqiNP_927143.1. NC_005125.1.
WP_011144181.1. NC_005125.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/E50-359[»]
3EI0X-ray3.50A/B/C/D/E50-359[»]
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[»]
4QH1X-ray3.40A/B/C/D/E44-359[»]
4QH4X-ray3.20A/B/C/D/E44-359[»]
4QH5X-ray3.00A/B/C/D/E44-359[»]
4X5TX-ray3.50A/B/C/D/E44-235[»]
4YEUX-ray4.60A/B/C/D/E236-357[»]
4ZZBX-ray3.40A/B/C/D/E44-359[»]
4ZZCX-ray3.10A/B/C/D/E43-359[»]
5HCJX-ray2.95A/B/C/D/E44-359[»]
5HCMX-ray3.15A/B/C/D/E44-359[»]
5HEGX-ray3.21A/B/C/D/E44-359[»]
5HEHX-ray3.30A/B/C/D/E44-359[»]
ProteinModelPortaliQ7NDN8.
SMRiQ7NDN8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59040N.
MINTiMINT-8425450.
STRINGi251221.glr4197.

Protein family/group databases

TCDBi1.A.9.8.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC92138; BAC92138; BAC92138.
GeneIDi2602600.
KEGGigvi:glr4197.
PATRICi22047895. VBIGloVio86258_4229.

Phylogenomic databases

eggNOGiENOG4105TA1. Bacteria.
ENOG4111U8M. LUCA.
InParanoidiQ7NDN8.
OMAiRESWIDK.
OrthoDBiPOG091H13WE.
PhylomeDBiQ7NDN8.

Miscellaneous databases

EvolutionaryTraceiQ7NDN8.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
[Graphical view]
PRINTSiPR00253. GABAARECEPTR.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLIC_GLOVI
AccessioniPrimary (citable) accession number: Q7NDN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.