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K+ voltage-gated channel subfamily H member 4; brain-specific eag-like channel 2; BEC2; ether-a-go-go-like K+ channel 1; ELK channel 1; ELK1; voltage-gated K+ channel subunit Kv12.3 (KCNH4)
Function:
- pore-forming (alpha) subunit of voltage-gated K+ channel
- elicits an outward current, but shows no inactivation
- channel properties may be modulated by cAMP & subunit assembly
- the K+ channel is probably composed of a homo- or heterotetrameric complex of pore-forming alpha subunits that can associate with modulating beta subunits
Structure:
- the segment S4 is probably the voltage-sensor & is characterized by a series of positively charged amino acids at every third position
- belongs to the K+ channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv12.3/KCNH4 sub-subfamily
- contains 1 cyclic nucleotide-binding domain
- contains 1 PAC (PAS-associated C-terminal) domain
- contains 1 PAS (PER-ARNT-SIM) domain
Compartment: membrane
Expression:
- expressed only in brain, in particular in the telencephalon
- expressed in putamen & caudate nucleus
- expressed at lower levels in cerebral cortex, occipital & hippocampus
General
glycoprotein
K+ channel subfamily H
transmembrane 6 protein
Properties
SIZE: entity length = 1017 aa
MW = 112 kD
COMPARTMENT: plasma membrane
MOTIF: cytoplasmic domain {1-228}
MOTIF: PAS domain {14-90}
PAC domain {93-145}
transmembrane domain {229-249}
exoplasmic loop {250-259}
transmembrane domain {260-280}
cytoplasmic loop {281-302}
transmembrane domain {303-323}
exoplasmic loop {324-332}
MOTIF: N-glycosylation site {N326}
transmembrane domain {333-353}
cytoplasmic loop {354-361}
transmembrane domain {362-382}
exoplasmic loop {383-427}
MOTIF: N-glycosylation site {N414}
Selectivity filter {439-444}
exoplasmic loop {449-482}
MOTIF: N-glycosylation site {N473}
transmembrane domain {483-503}
cytoplasmic domain {504-1017}
MOTIF: cyclic nucleotide-binding site
SITE: 556-671
ION-PERMEABILITY: K+
Database Correlations
OMIM 604528
UniProt Q9UQ05
PFAM correlations
Entrez Gene 23415
Kegg hsa:23415
References
UniProt :accession Q9UQ05