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Q7NDN8

- GLIC_GLOVI

UniProt

Q7NDN8 - GLIC_GLOVI

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Protein

Proton-gated ion channel

Gene
glvI, glr4197
Organism
Gloeobacter violaceus (strain PCC 7421)
Status
Reviewed - 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

  1. extracellular ligand-gated ion channel activity Source: InterPro
  2. potassium channel activity Source: UniProtKB-KW
  3. sodium channel activity Source: UniProtKB-KW
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

Enzyme and pathway databases

BioCyciGVIO251221:GH9A-4249-MONOMER.

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 lineageiBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter
ProteomesiUP000000557: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini44 – 235192Periplasmic Reviewed predictionAdd
BLAST
Transmembranei236 – 25823HelicalAdd
BLAST
Topological domaini259 – 2613Cytoplasmic Reviewed prediction
Transmembranei262 – 28625HelicalAdd
BLAST
Topological domaini287 – 2948Periplasmic Reviewed prediction
Transmembranei295 – 32329HelicalAdd
BLAST
Topological domaini324 – 3263Cytoplasmic Reviewed prediction
Transmembranei327 – 35933HelicalAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441I → Y: Marked gain of function, with a ten-fold shift of the proton dose-response curve towards lower concentrations. 1 Publication
Mutagenesisi264 – 2641E → A: Decreases cation selectivity. Decreases the binding affinity of TEA and TBA. Nearly abolishes block by Cd(2+). 2 Publications
Mutagenesisi264 – 2641E → Q or D: Decreases binding affinity of TBA. 2 Publications
Mutagenesisi268 – 2681T → A: Increases the binding affinity of TBA. Weakens block by Cd(2+). 1 Publication
Mutagenesisi272 – 2721S → A: Increases the binding affinity of TBA. 1 Publication
Mutagenesisi284 – 2841V → M: Displays an increased sensitivity to propofol but not to desflurane. 1 Publication
Mutagenesisi297 – 2971T → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343 Reviewed predictionAdd
BLAST
Chaini44 – 359316Proton-gated ion channelPRO_0000412722Add
BLAST

Interactioni

Subunit structurei

Homopentamer.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi53 – 553
Beta strandi58 – 7013
Beta strandi76 – 9015
Helixi92 – 943
Helixi98 – 1014
Beta strandi104 – 1074
Helixi110 – 1123
Beta strandi118 – 1269
Beta strandi128 – 1369
Turni138 – 1403
Beta strandi141 – 15313
Turni159 – 1624
Beta strandi165 – 17410
Beta strandi177 – 1793
Beta strandi182 – 1865
Helixi188 – 1903
Beta strandi192 – 1943
Beta strandi196 – 1994
Beta strandi202 – 21211
Beta strandi219 – 2213
Beta strandi225 – 23410
Helixi236 – 2383
Helixi239 – 2424
Helixi244 – 25411
Helixi255 – 2595
Helixi263 – 28624
Helixi296 – 32328
Helixi327 – 35630

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ7NDN8.

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

OMAiFTYEASF.
OrthoDBiEOG6VF30W.
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.
PF02932. Neur_chan_memb. 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

MFPTGWRPKL SESIAASRML WQPMAAVAVV QIGLLWFSPP VWGQDMVSPP    50
PPIADEPLTV NTGIYLIECY SLDDKAETFK VNAFLSLSWK DRRLAFDPVR 100
SGVRVKTYEP EAIWIPEIRF VNVENARDAD VVDISVSPDG TVQYLERFSA 150
RVLSPLDFRR YPFDSQTLHI YLIVRSVDTR NIVLAVDLEK VGKNDDVFLT 200
GWDIESFTAV VKPANFALED RLESKLDYQL RISRQYFSYI PNIILPMLFI 250
LFISWTAFWS TSYEANVTLV VSTLIAHIAF NILVETNLPK TPYMTYTGAI 300
IFMIYLFYFV AVIEVTVQHY LKVESQPARA ASITRASRIA FPVVFLLANI 350
ILAFLFFGF 359
Length:359
Mass (Da):40,986
Last modified:December 15, 2003 - v1
Checksum:i6F9009F96172C025
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BA000045 Genomic DNA. Translation: BAC92138.1 .
RefSeqi NP_927143.1. NC_005125.1.
WP_011144181.1. NC_005125.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XQ3 X-ray 3.50 A/B/C/D/E 43-359 [» ]
2XQ4 X-ray 3.60 A/B/C/D/E 43-359 [» ]
2XQ5 X-ray 3.50 A/B/C/D/E 43-359 [» ]
2XQ6 X-ray 3.70 A/B/C/D/E 43-359 [» ]
2XQ7 X-ray 3.40 A/B/C/D/E 43-359 [» ]
2XQ8 X-ray 3.60 A/B/C/D/E 43-359 [» ]
2XQ9 X-ray 3.20 A/B/C/D/E 43-359 [» ]
2XQA X-ray 3.70 A/B/C/D/E 43-359 [» ]
3EAM X-ray 2.90 A/B/C/D/E 44-359 [» ]
3EHZ X-ray 3.10 A/B/C/D/E 50-359 [» ]
3EI0 X-ray 3.50 A/B/C/D/E 50-359 [» ]
3IGQ X-ray 2.30 A/B/C/D/E/F 44-235 [» ]
3LSV X-ray 3.15 A/B/C/D/E 44-359 [» ]
3P4W X-ray 3.20 A/B/C/D/E 44-359 [» ]
3P50 X-ray 3.30 A/B/C/D/E 44-359 [» ]
3TLS X-ray 3.20 A/B/C/D/E 44-359 [» ]
3TLT X-ray 3.30 A/B/C/D/E 44-359 [» ]
3TLU X-ray 2.85 A/B/C/D/E 44-359 [» ]
3TLV X-ray 2.90 A/B/C/D/E 44-359 [» ]
3TLW X-ray 2.60 A/B/C/D/E 44-359 [» ]
3UU3 X-ray 3.15 A/B/C/D/E 44-359 [» ]
3UU4 X-ray 3.05 A/B/C/D/E 44-359 [» ]
3UU5 X-ray 2.90 A/B/C/D/E 44-359 [» ]
3UU6 X-ray 2.98 A/B/C/D/E 44-359 [» ]
3UU8 X-ray 3.25 A/B/C/D/E 44-359 [» ]
3UUB X-ray 2.90 A/B/C/D/E/F/G/H/I/J 44-359 [» ]
4F8H X-ray 2.99 A/B/C/D/E 43-359 [» ]
4HFB X-ray 2.75 A/B/C/D/E 44-359 [» ]
4HFC X-ray 3.05 A/B/C/D/E 44-359 [» ]
4HFD X-ray 3.10 A/B/C/D/E 44-359 [» ]
4HFE X-ray 2.80 A/B/C/D/E 44-359 [» ]
4HFH X-ray 2.65 A/B/C/D/E 44-359 [» ]
4HFI X-ray 2.40 A/B/C/D/E 44-359 [» ]
4IL4 X-ray 3.30 A/B/C/D/E 44-359 [» ]
4IL9 X-ray 2.83 A/B/C/D/E 44-358 [» ]
4ILA X-ray 3.50 A/B/C/D/E 44-358 [» ]
4ILB X-ray 3.15 A/B/C/D/E 44-358 [» ]
4ILC X-ray 2.99 A/B/C/D/E 44-358 [» ]
4IRE X-ray 3.19 A/B/C/D/E 43-359 [» ]
4LMJ X-ray 3.44 A/B/C/D/E 44-359 [» ]
4LMK X-ray 3.22 A/B/C/D/E 44-359 [» ]
4LML X-ray 3.80 A/B/C/D/E 44-359 [» ]
4NPP X-ray 3.35 A/B/C/D/E 44-359 [» ]
4NPQ X-ray 4.35 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 44-359 [» ]
ProteinModelPortali Q7NDN8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59040N.
MINTi MINT-8425450.
STRINGi 251221.glr4197.

Protein family/group databases

TCDBi 1.A.9.8.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC92138 ; BAC92138 ; BAC92138 .
GeneIDi 2602600.
KEGGi gvi:glr4197.
PATRICi 22047895. VBIGloVio86258_4229.

Phylogenomic databases

OMAi FTYEASF.
OrthoDBi EOG6VF30W.
PhylomeDBi Q7NDN8.

Enzyme and pathway databases

BioCyci GVIO251221:GH9A-4249-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q7NDN8.

Family and domain databases

Gene3Di 2.70.170.10. 1 hit.
InterProi IPR006028. GABAA/Glycine_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
[Graphical view ]
PANTHERi PTHR18945. PTHR18945. 1 hit.
Pfami PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view ]
PRINTSi PR00253. GABAARECEPTR.
SUPFAMi SSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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: September 3, 2014
This is version 76 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

External Data

Dasty 3