Contents

Search


K+ voltage-gated channel subfamily H member 5; ether-a-go-go K+ channel 2; hEAG2; voltage-gated K+ channel subunit Kv10.2 (KCNH5 EAG2)

Function: - pore-forming (alpha) subunit of voltage-gated K+ channel - elicits a non-inactivating outward rectifying current - 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 - heteromultimer with KCNH1/EAG (probable) 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, Kv10.2/KCNH5 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 Alternative splicing: named isoforms=3 Expression: - expressed in brain, skeletal muscle, heart, placenta, lung & liver - expressed at low levels in kidney

General

glycoprotein K+ channel subfamily H transmembrane 6 protein

Properties

SIZE: entity length = 988 aa MW = 112 kD COMPARTMENT: plasma membrane MOTIF: cytoplasmic domain {1-217} MOTIF: PAS domain {12-90} PAC domain {91-143} transmembrane domain {218-238} exoplasmic loop {239-243} transmembrane domain {244-264} cytoplasmic loop {265-291} transmembrane domain {292-312} exoplasmic loop {313-319} transmembrane domain {320-340} cytoplasmic loop {341-346} transmembrane domain {347-367} exoplasmic loop {368-419} MOTIF: N-glycosylation site {N403} Selectivity filter {432-437} exoplasmic loop {441-446} transmembrane domain {447-467} cytoplasmic domain {468-988} MOTIF: cyclic nucleotide-binding site SITE: 550-667 calmodulin binding site SITE: 704-715 FOR-BINDING-OF: calmodulin CAD {909-948} ION-PERMEABILITY: K+

Database Correlations

OMIM 605716 UniProt Q8NCM2 PFAM correlations Entrez Gene 27133 Kegg hsa:27133

References

UniProt :accession Q8NCM2