CNGB1
entrez
1258
canonical
uniprot
Q14028
canonical
ensembl
ENSG00000070729
resolver
ensp
ENSP00000251102
resolver
ensp
ENSP00000311670
resolver
ensp
ENSP00000454633
resolver
genesymbol
CNGB1
resolver
genesymbol_syn
CNCG2
resolver
genesymbol_syn
CNCG3L
resolver
genesymbol_syn
CNCG4
resolver
genesymbol_syn
RCNC2
resolver
hgnc
HGNC:2151
resolver
uniprot
H3BN09
resolver
uniprot
O43636
resolver
uniprot
Q13059
resolver
uniprot
Q14029
resolver
uniprot
Q9UMG2
resolver
uniprot_entry
CNGB1_HUMAN
resolver
uniprot_sec
H3BN09
resolver
uniprot_sec
O43636
resolver
uniprot_sec
Q13059
resolver
uniprot_sec
Q14029
resolver
uniprot_sec
Q9UMG2
resolver
amino_acid_sequence
MLGWVQRVLPQPPGTPRKTKMQEEEEVEPEPEMEAEVEPEPNPEEAETESESMPPEESFKEEEVAVADPSPQETKEAALTSTISLRAQGAEISEMNSPSRRVLTWLMKGVEKVIPQPVHSITEDPAQILGHGSTGDTGCTDEPNEALEAQDTRPGLRLLLWLEQNLERVLPQPPKSSEVWRDEPAVATGAASDPAPPGRPQEMGPKLQARETPSLPTPIPLQPKEEPKEAPAPEPQPGSQAQTSSLPPTRDPARLVAWVLHRLEMALPQPVLHGKIGEQEPDSPGICDVQTISILPGGQVEPDLVLEEVEPPWEDAHQDVSTSPQGTEVVPAYEEENKAVEKMPRELSRIEEEKEDEEEEEEEEEEEEEEEVTEVLLDSCVVSQVGVGQSEEDGTRPQSTSDQKLWEEVGEEAKKEAEEKAKEEAEEVAEEEAEKEPQDWAETKEEPEAEAEAASSGVPATKQHPEVQVEDTDADSCPLMAEENPPSTVLPPPSPAKSDTLIVPSSASGTHRKKLPSEDDEAEELKALSPAESPVVAWSDPTTPKDTDGQDRAASTASTNSAIINDRLQELVKLFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPEPAPDTKPAEAEPVEEEHYCDMLCCKFKHRPWKKYQFPQSIDPLTNLMYVLWLFFVVMAWNWNCWLIPVRWAFPYQTPDNIHHWLLMDYLCDLIYFLDITVFQTRLQFVRGGDIITDKKDMRNNYLKSRRFKMDLLSLLPLDFLYLKVGVNPLLRLPRCLKYMAFFEFNSRLESILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAYQGLGSTHWVYDGVGNSYIRCYYFAVKTLITIGGLPDPKTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPKSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYNIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKSVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRSNNKPKEEKSVLILPPRAGTPKLFNAALAMTGKMGGKGAKGGKLAHLRARLKELAALEAAAKQQELVEQAKSSQDVKGEEGSAAPDQHTHPKEAATDPPAPRTPPEPPGSPPSSPPPASLGRPEGEEEGPAEPEEHSVRICMSPGPEPGEQILSVKMPEEREEKAE
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 45 (RP45) [MIM:613767]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:11379879, ECO:0000269|PubMed:24339724, ECO:0000269|PubMed:28056120, ECO:0000269|PubMed:29800053}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming subunit of the rod cyclic nucleotide-gated channel. Mediates rod photoresponses at dim light converting transient changes in intracellular cGMP levels into electrical signals. In the dark, cGMP levels are high and keep the channel open enabling a steady inward current carried by Na(+) and Ca(2+) ions that leads to membrane depolarization and neurotransmitter release from synaptic terminals. Upon photon absorption cGMP levels decline leading to channel closure and membrane hyperpolarization that ultimately slows neurotransmitter release and signals the presence of light, the end point of the phototransduction cascade (By similarity) (PubMed:34699778). Pore-forming subunit of the olfactory cyclic nucleotide-gated channel. Operates in the cilia of olfactory sensory neurons where chemical stimulation of the odorant is converted to an electrical signal. Mediates odorant-induced cAMP-dependent Ca(2+) influx triggering neuron depolarization. The rise of intracellular Ca(2+) levels potentiates the olfactory response by activating Ca(2+)-dependent Cl(-) channels, but it also serves as a negative feedback signal to desensitize the channel for rapid adaptation to odorants (By similarity). Conducts cGMP- and cAMP-gated ion currents, with permeability for monovalent and divalent cations. The selectivity for Ca(2+) over Na(+) increases with cGMP concentrations, whereas the selectivity among monovalent ions is independent of the cGMP levels (By similarity) (PubMed:34699778). {ECO:0000250|UniProtKB:A0A8I5ZN27, ECO:0000250|UniProtKB:Q28181, ECO:0000250|UniProtKB:Q9NQW8, ECO:0000269|PubMed:34699778}.; FUNCTION: [Isoform GARP2]: High affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties: it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. {ECO:0000269|PubMed:16407240}.
uniprot
proteins
mass_dalton
139678
uniprot
proteins
mutagenesis
MUTAGEN 568; /note="L->E: Loss of calcium/calmodulin modulation."; /evidence="ECO:0000269|PubMed:15195096"; MUTAGEN 848; /note="G->E: Increases the affinity to Ca(2+) ions. Does not affect heterotetrameric channel assembly."; /evidence="ECO:0000269|PubMed:34699778"; MUTAGEN 880; /note="R->G: Increases channel conductance."; /evidence="ECO:0000269|PubMed:34699778"; MUTAGEN 1237..1238; /note="IL->AA: Loss of interaction with ANK3."; /evidence="ECO:0000269|PubMed:19299621
uniprot
proteins
protein_family
CNGB1 subfamily
uniprot
proteins
protein_family
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
uniprot
proteins
pubmed
10717482
uniprot
proteins
pubmed
11379879
uniprot
proteins
pubmed
11764791
uniprot
proteins
pubmed
15195096
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16280326
uniprot
proteins
pubmed
16407240
uniprot
proteins
pubmed
19299621
uniprot
proteins
pubmed
24339724
uniprot
proteins
pubmed
28056120
uniprot
proteins
pubmed
29800053
uniprot
proteins
pubmed
34699778
uniprot
proteins
pubmed
7590744
uniprot
proteins
pubmed
7682292
uniprot
proteins
pubmed
8766832
uniprot
proteins
pubmed
9535905
uniprot
proteins
sequence_length
1251
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:E1AZ71}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:A0A8I5ZN27, ECO:0000250|UniProtKB:E1AZ71}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in rod outer segment membranes. {ECO:0000250|UniProtKB:E1AZ71}.
uniprot
proteins
transmembrane_region
TRANSMEM 657..678; /note="Helical; Name=S1"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 688..709; /note="Helical; Name=S2"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 725..744; /note="Helical; Name=S3"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 761..773; /note="Helical; Name=S4"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 786..808; /note="Helical; Name=S5"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 832..858; /note="Helical; Name=P-helix"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 859..884; /note="Helical; Name=S6"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
uniprot
proteins