K9UJK2 · TM175_CHAP6
- ProteinPotassium channel Cha6605_3372
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids203 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Potassium channel (PubMed:28723891).
The channel is permeable for K+, Rb+ and Cs+, while it is unable to conduct Na+ (PubMed:28723891).
The channel is permeable for K+, Rb+ and Cs+, while it is unable to conduct Na+ (PubMed:28723891).
Catalytic activity
- K+(in) = K+(out)
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 23 | Hydrophobic filter residue 1 | ||||
Sequence: I | ||||||
Site | 27 | Hydrophobic filter residue 2 | ||||
Sequence: L | ||||||
Site | 30 | Hydrophobic filter residue 3 | ||||
Sequence: L |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | identical protein binding | |
Molecular Function | potassium channel activity | |
Molecular Function | proton channel activity | |
Biological Process | potassium ion transmembrane transport | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePotassium channel Cha6605_3372
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Gomontiellales > Chamaesiphonaceae > Chamaesiphon
Accessions
- Primary accessionK9UJK2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MVEAPEQ | ||||||
Transmembrane | 8-31 | Helical; Name=TM1 | ||||
Sequence: SETGRIEAFSDGVFAIAITLLVLE | ||||||
Topological domain | 32-52 | Extracellular | ||||
Sequence: IKVPQHKIVETVGLVSSLLSL | ||||||
Transmembrane | 53-78 | Helical; Name=TM2 | ||||
Sequence: WPSYLAFLTSFASILVMWVNHHRIFS | ||||||
Topological domain | 79-84 | Cytoplasmic | ||||
Sequence: LVARTD | ||||||
Transmembrane | 85-110 | Helical; Name=TM3 | ||||
Sequence: HAFFYWNGLLLMLVTFVPFPTALLAE | ||||||
Topological domain | 111-117 | Extracellular | ||||
Sequence: YLIHPQA | ||||||
Transmembrane | 118-142 | Helical; Name=TM4 | ||||
Sequence: RVAASVYAGIFLAIAIVFNRLWKHA | ||||||
Topological domain | 143-154 | Cytoplasmic | ||||
Sequence: ATADRLLAQKAD | ||||||
Transmembrane | 155-181 | Helical; Name=TM5 | ||||
Sequence: RHEVDAITKQYRFGPGLYLVAFALSFI | ||||||
Topological domain | 182-183 | Extracellular | ||||
Sequence: SV | ||||||
Transmembrane | 184-199 | Helical; Name=TM6 | ||||
Sequence: WLSVGVCFVLAIYFAL | ||||||
Topological domain | 200-203 | Cytoplasmic | ||||
Sequence: RSNA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 23 | Impaired selectivity. Can conduct both K+ and Na+. | ||||
Sequence: I → A, C, or N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000442004 | 1-203 | Potassium channel Cha6605_3372 | |||
Sequence: MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA |
Interaction
Subunit
Homotetramer (PubMed:28723891).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | K9UJK2 | Cha6605_3372 K9UJK2 | 2 | EBI-20710438, EBI-20710438 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 12-18 | RxxxFSD motif | ||||
Sequence: RIEAFSD | ||||||
Region | 37-42 | Short helix H1 | ||||
Sequence: HKIVET | ||||||
Region | 44-50 | Short helix H2 | ||||
Sequence: GLVSSLL |
Domain
In contrast to canonical tetrameric potassium channels, lacks the TVGYG selectivity filter motif and presents a completely different structure. The six transmembrane regions are tightly packed within each subunit without undergoing domain swapping. Transmembranes TM1-TM3 are positioned on the inner circle of the channel tetramer and participate in inter-subunit interactions that are central to the assembly of the ion conduction pore. The RxxxFSD motif within transmembrane TM1 coordinates a network of specific inter- and intra-subunit interactions with other conserved residues on TM2 and TM3 and plays a key role in the tetrameric assembly of the channel. Transmembrane TM4-TM6 are positioned on the periphery of the channel and do not contribute to contacts with neighboring subunits. Transmembranes TM1 and TM2 are linked by an extended strand-like tail and two short helices (H1 and H2) which protrude outwards from the main body of the transmembrane domain and enclose the external open entrance of the ion conduction pore in the channel tetramer. Transmembrane TM3 is bent into two segments (TM3a and TM3b) due to the presence of a conserved proline (Pro-102). Transmembrane TM1 forms the pore-lining inner helix at the center of the channel, creating an hourglass-shaped ion permeation pathway in the channel tetramer. Three hydrophobic residues (Ile-23, Leu-27 and Leu-30) on the C-terminal half of the TM1 helix form a bottleneck along the ion conduction pathway and serve as the selectivity filter of the channel. Ile-23 is probably responsible for channel selectivity.
Sequence similarities
Belongs to the TMEM175 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length203
- Mass (Da)22,674
- Last updated2013-03-06 v1
- Checksum53D7E93F759FEBE4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003600 EMBL· GenBank· DDBJ | AFY94374.1 EMBL· GenBank· DDBJ | Genomic DNA |