Primary Information | |
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BoMiProt ID | Bomi4948 |
Protein Name | Cyclic nucleotide-gated olfactory channel/Cyclic nucleotide-gated cation channel 2/Cyclic nucleotide-gated channel alpha-2 |
Organism | Bos taurus |
Uniprot ID | Q03041 |
Milk Fraction | Whey |
Ref Sequence ID | NP_001001139.1 |
Aminoacid Length | 663 |
Molecular Weight | 76014 |
FASTA Sequence | Download |
Gene Name | CNGA2/CNCG2 |
Gene ID | 407172 |
Protein Existence Status | reviewed |
Secondary Information | |
Protein Function | are excellent targets of various cellular signals to finely regulate neuronal responses to external stimuli. Numerous mechanisms, including transcriptional control, trafficking, as well as channel assembly and modification, underlie HCN channel regulation. |
Biochemical Properties | HCN channels belong to the superfamily of voltage-gated pore loop channels with four pore-forming subunits (HCN1-4) encoded by the HCN1-4 gene family in mammals . Each subunit has six transmembrane helices (S1-S6), with the positively charged voltage sensor (S4) and the pore region carrying the GYG motif between S5 and S6, which forms the ion selectivity filter. Following S6 is the 80-residue C-linker comprising six alpha-helices (A’-F’) and the cyclic nucleotide-binding domain (CNBD). The CNBD consists of three alpha-helices (A-C) and a β-roll between the A- and B-helices |
PTMs | N linked glycosylation at Aspn |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|Q03041|CNGA2_BOVIN Cyclic nucleotide-gated olfactory channel OS=Bos taurus OX=9913 GN=CNGA2 PE=1 SV=1 MTEKANGVKSSPANNHNHHAPPAIKASGKDDHRASSRPQSAAADDTSSELQQLAEMDAPQ QRRGGFRRIARLVGVLREWAYRNFREEEPRPDSFLERFRGPELHTVTTQQGDGKGDKDGE GKGTKKKFELFVLDPAGDWYYRWLFLIALPVLYNWCLLVARACFSDLQKGYYIVWLVLDY VSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTMQFKLDVASIIPTDLIYFAVGI HNPEVRFNRLLHFARMFEFFDRTETRTSYPNIFRISNLILYILIIIHWNACIYYAISKSI GFGVDTWVYPNITDPEYGYLSREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIG VLIFATIVGNVGSMISNMN*379ATRAEFQAKIDAVKHYMQFRKVSKEMEAKVIRWFDYLWTNK KSVDEREVLKNLPAKLRAEIAINVHLSTLKKVRIFQDCEAGLLVELVLKLRPQVFSPGDY ICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANI RSLGYSDLFCLSKDDLMEAVTEYPDAKRVLEERGREILMKEGLLDENEVAASMEVDVQEK LEQLETNMDTLYTRFARLLAEYTGAQQKLKQRITVLETKMKQNNEDDSLSDGMNSPEPPA EKP |
CATH | Matched CATH superfamily 1.10.238.10 |
Predicted Disorder Regions | 1-65, 104-123, 637-663 |
DisProt Annotation | |
TM Helix Prediction | 4TMHs; (143-161),(170-188),(275-297),(350-372) |
Significance of PTMs | The assembly of hippocampal HCN1/HCN2 heteromeric channels was increased following the febrile seizure, probably mediated by the increased abundance of HCN2 subunits relative to HCN1 and the network activity-dependent glycosylation of HCN1 channels |
PDB ID | 1SY9, |
Bibliography | 1.He C, Chen F, Li B, Hu Z. Neurophysiology of HCN channels: from cellular functions to multiple regulations. Prog Neurobiol. 2014 Jan;112:1-23. doi: 10.1016/j.pneurobio.2013.10.001. Epub 2013 Oct 29. PMID: 24184323. 2.Brewster, A. L., Bernard, J. A., Gall, C. M. and Baram, T. Z. (2005) Formation of heteromeric hyperpolarization-activated cyclic nucleotide-gated (HCN) channels in the hippocampus is regulated by developmental seizures. Neurobiol Dis 19, 200-207. 3.Zha, Q., Brewster, A. L., Richichi, C., Bender, R. A. and Baram, T. Z. (2008) Activity-dependent heteromerization of the hyperpolarization-activated, cyclic-nucleotide gated (HCN) channels: role of N-linked glycosylation. J Neurochem 105, 68-77. |