P25122 · KCNC1_RAT
- ProteinVoltage-gated potassium channel KCNC1
- GeneKcnc1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids585 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Voltage-gated potassium channel that opens in response to the voltage difference across the membrane and through which potassium ions pass in accordance with their electrochemical gradient (Probable) (PubMed:10482766, PubMed:1378392, PubMed:14679187).
The mechanism is time-dependent and inactivation is slow (PubMed:10482766, PubMed:1378392).
Plays an important role in the rapid repolarization of fast-firing brain neurons (PubMed:10482766).
Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well (PubMed:10482766, PubMed:14679187).
Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons (PubMed:10482766).
The mechanism is time-dependent and inactivation is slow (PubMed:10482766, PubMed:1378392).
Plays an important role in the rapid repolarization of fast-firing brain neurons (PubMed:10482766).
Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNC2, and possibly other family members as well (PubMed:10482766, PubMed:14679187).
Contributes to fire sustained trains of very brief action potentials at high frequency in pallidal neurons (PubMed:10482766).
Catalytic activity
- K+(in) = K+(out)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 77 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 83 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 105 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 400 | K+ (UniProtKB | ChEBI); ligand shared between homotetrameric partners | ||||
Sequence: T | ||||||
Binding site | 401 | K+ (UniProtKB | ChEBI); ligand shared between homotetrameric partners | ||||
Sequence: L | ||||||
Binding site | 402 | K+ (UniProtKB | ChEBI); ligand shared between homotetrameric partners | ||||
Sequence: G | ||||||
Binding site | 403 | K+ (UniProtKB | ChEBI); ligand shared between homotetrameric partners | ||||
Sequence: Y |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVoltage-gated potassium channel KCNC1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP25122
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localizes in parallel fiber membranes, distributed on the perisynaptic and extrasynaptic membranes away from the active zones.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-190 | Cytoplasmic | ||||
Sequence: MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYAR | ||||||
Transmembrane | 191-209 | Helical; Name=Segment S1 | ||||
Sequence: YVAFASLFFILVSITTFCL | ||||||
Transmembrane | 248-267 | Helical; Name=Segment S2 | ||||
Sequence: IEGVCVVWFTFEFLMRVVFC | ||||||
Topological domain | 268-276 | Cytoplasmic | ||||
Sequence: PNKVEFIKN | ||||||
Transmembrane | 277-295 | Helical; Name=Segment S3 | ||||
Sequence: SLNIIDFVAILPFYLEVGL | ||||||
Transmembrane | 309-331 | Helical; Voltage-sensor; Name=Segment S4 | ||||
Sequence: FLRVVRFVRILRIFKLTRHFVGL | ||||||
Topological domain | 332-344 | Cytoplasmic | ||||
Sequence: RVLGHTLRASTNE | ||||||
Transmembrane | 345-366 | Helical; Name=Segment S5 | ||||
Sequence: FLLLIIFLALGVLIFATMIYYA | ||||||
Transmembrane | 415-436 | Helical; Name=Segment S6 | ||||
Sequence: LVGALCALAGVLTIAMPVPVIV | ||||||
Topological domain | 437-585 | Cytoplasmic | ||||
Sequence: NNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRADSKLNGEVAKAALANEDCPHIDQALTPDEGLPFTRSGTRERYGPCFLLSTGEYACPPGGGMRKDLCKESPVIAKYMPTEAVRVT |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 220 | Reduces extent of N-glycosylation. Abolishes N-glycosylation; when associated with Q-229. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 229 | Reduces extent of N-glycosylation. Abolishes N-glycosylation; when associated with Q-220. | ||||
Sequence: N → Q |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054053 | 1-585 | Voltage-gated potassium channel KCNC1 | |||
Sequence: MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRADSKLNGEVAKAALANEDCPHIDQALTPDEGLPFTRSGTRERYGPCFLLSTGEYACPPGGGMRKDLCKESPVIAKYMPTEAVRVT | ||||||
Modified residue | 44 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 142 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 158 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 160 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 220 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 229 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 474 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 483 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
N-glycosylated; contains sialylated glycans.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotetramer. Homomultimer (By similarity).
Heteromultimer with KCNG3, KCNG4 and KCNV2 (By similarity).
Heteromultimer with KCNC2 (PubMed:10482766, PubMed:14679187).
Heterotetramer with KCNC3 (By similarity).
Interacts with the ancillary subunits KCNE1 and KCNE2; the interaction modulates channel activity (PubMed:14679187).
Heteromultimer with KCNG3, KCNG4 and KCNV2 (By similarity).
Heteromultimer with KCNC2 (PubMed:10482766, PubMed:14679187).
Heterotetramer with KCNC3 (By similarity).
Interacts with the ancillary subunits KCNE1 and KCNE2; the interaction modulates channel activity (PubMed:14679187).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 121-147 | Disordered | ||||
Sequence: SFGGAPLDNSADDADADGPGDSGDGED | ||||||
Motif | 400-405 | Selectivity filter | ||||
Sequence: TLGYGD |
Domain
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The N-terminal cytoplasmic T1 domain is involved but not required for Zn2+-mediated tetramerization.
Sequence similarities
Belongs to the potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P25122-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length585
- Mass (Da)65,857
- Last updated1992-05-01 v1
- ChecksumDD4E2D32848E2DCF
P25122-2
- Name2
- SynonymsShort
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M68880 EMBL· GenBank· DDBJ | AAA41501.1 EMBL· GenBank· DDBJ | mRNA | ||
X62840 EMBL· GenBank· DDBJ | CAA44644.1 EMBL· GenBank· DDBJ | mRNA |