Hcn2
entrez
114244
canonical
uniprot
Q9JKA9
canonical
ensembl
ENSRNOG00000008831
resolver
ensembl
ENSRNOG00055031041
resolver
ensembl
ENSRNOG00060027027
resolver
ensembl
ENSRNOG00065020456
resolver
ensp
ENSRNOP00000011837
resolver
ensp
ENSRNOP00055044538
resolver
ensp
ENSRNOP00060038962
resolver
ensp
ENSRNOP00065027726
resolver
enst
ENSRNOT00000011837
resolver
enst
ENSRNOT00055053819
resolver
enst
ENSRNOT00060046853
resolver
enst
ENSRNOT00065034581
resolver
genesymbol
Hcn2
resolver
uniprot
F1LRY7
resolver
uniprot
Q6BCT5
resolver
uniprot
Q9QZW6
resolver
uniprot_entry
HCN2_RAT
resolver
uniprot_sec
F1LRY7
resolver
uniprot_sec
Q6BCT5
resolver
uniprot_sec
Q9QZW6
resolver
activity_regulation
ACTIVITY REGULATION: Activated by cAMP, and at 10-100 times higher concentrations, also by cGMP. cAMP binding causes a conformation change that leads to the assembly of an active tetramer and channel opening (PubMed:21796099). In the absence of cAMP, the C-terminal region is thought to exert a tonic inhibition on the pore when HCN2 is in a non-tetrameric form (By similarity). Channel activity is modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages (By similarity). Phosphatidylinositol-4,5- bisphosphate (PIP(2)) acts as a ligand that allosterically opens HCN2 by shifting voltage-dependent channel activation toward depolarized potentials (By similarity). Inhibited by extracellular cesium ions (By similarity). {ECO:0000250|UniProtKB:O88703, ECO:0000250|UniProtKB:Q9UL51, ECO:0000269|PubMed:21796099}.
uniprot
proteins
amino_acid_sequence
MDARGGGGRPGDSPGATPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRSRLCSRDSSCTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPAAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGAPAPSPAASARPASSSTPRLGPAPTTRTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
uniprot
proteins
function
FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions (PubMed:21796099). Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron (PubMed:21796099). Involved in the initiation of neuropathic pain in sensory neurons. Produces a large instantaneous current (PubMed:21796099). {ECO:0000269|PubMed:21796099}.
uniprot
proteins
mass_dalton
94710
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-641 by PRKG2 shifts the voltage-dependence to more negative voltages, hence counteracting the stimulatory effect of cGMP on gating. {ECO:0000250|UniProtKB:O88703}.; PTM: N-glycosylated; required for cell surface trafficking of HCN2. {ECO:0000250|UniProtKB:O88703}.; PTM: S-palmitoylated. {ECO:0000250|UniProtKB:Q9UL51}.
uniprot
proteins
protein_family
Potassium channel HCN family
uniprot
proteins
pubmed
10400919
uniprot
proteins
pubmed
11000485
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15265006
uniprot
proteins
pubmed
21796099
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
863
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21796099}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 189..209; /note="Helical; Name=Segment S1"; /evidence="ECO:0000255"; TRANSMEM 214..234; /note="Helical; Name=Segment S2"; /evidence="ECO:0000255"; TRANSMEM 262..282; /note="Helical; Name=Segment S3"; /evidence="ECO:0000255"; TRANSMEM 291..311; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000255"; TRANSMEM 343..363; /note="Helical; Name=Segment S5"; /evidence="ECO:0000255"; TRANSMEM 414..434; /note="Helical; Name=Segment S6"; /evidence="ECO:0000255
uniprot
proteins