A0A8I5ZN27
uniprot
A0A8I5ZN27
canonical
amino_acid_sequence
MLGWVQRVLPQPPGTPQKTEEGAGPQPETESKPEANPQPEPEVQPEPEPEPEPAPEEAAPEVQTLPPEEPVEGEDVAEAGPSLQETQEADPPQPTSQAQVAVVKVNRPSSWMLSWFWKGMEKVVPQPVYSSSGGQNLAAGEGGPDQDGAQTLEPCGTGDPGSEDGSDKTSKTQDTEPSLWLLRWLELNLEKVLPQPPTPSQAWKVEPEGAVLEPDPPGTPMEVEPTENPSQPNPGPVEPEEEPAAEPQPGFQASSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPSCPGTCDVQTISILPVEQAEHDLVLEDVDSCWEDTQQEDGASLQETELAPIYEDESEAMVEMPRELPQIQEEEEEEKEEKEEKEEEEEKEEEEKREEEKKKEKEEEKKEKEKEEKEEKEEKEEEEKEEKEEEEKEEKEEEEKEEKEEEEEEEEEEEEEEPIVLLDSCLVVQADVDQCQLERAQPETASIQELPEEEEEKEEEKKEEEEEKEEEEEKEEEEEKEEEGEATNSTVPATKEHPELQVEDTDAEAGPLIPEETIPPPERPPVSPAKSDTLAVPGAATHRKKLPSQDDEAEELKALSPAESPVVAWSDPTTPQEADGEDRAASTASQNSAIINDRLQELVKMFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPDSAPAQKPAEAEAAEEEHYCDMLCCKFKRRPWKMYQFPQSIDPLTNLMYILWLFFVVLAWNWNCWLIPVRWAFPYQRADNIHLWLLMDYLCDFIYLLDITVFQMRLQFVKGGDIITDKKEMRNNYLKSQRFKMDLLCLLPLDFLYLKLGVNPLLRLPRCLKYMAFFEFNNRLEAILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAFQGIGSTHWVYDGVGNSYIRCYYWAVKTLITIGGLPDPQTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPRSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYNIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKAVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRNNNKPKEEKSVLILPPRAGTPKLFNAALAAAGKMGPRGAKGGKLAHLRARLKELAALEAAARQQQLLEQAKSSQEAGGEEGSGATDQPAPQEPSEPKEPPEPPAPSSPPPASAKPEGSTEEAAGPPEPSVRIRVSPGPDPGEQTLSVEMLEEKKEEVE
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. 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. {ECO:0000250|UniProtKB:Q28181}.; FUNCTION: [Isoform 2]: 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. {ECO:0000269|PubMed:10377344, ECO:0000269|PubMed:15134638, ECO:0000269|PubMed:27405959, ECO:0000269|PubMed:9539801, ECO:0000269|PubMed:9878057}.
uniprot
proteins
mass_dalton
147160
uniprot
proteins
mutagenesis
MUTAGEN A0A8I5ZN27-2:657; /note="R->E: Markedly reduces the affinity of the channel for cAMP."; /evidence="ECO:0000269|PubMed:27405959
uniprot
proteins
protein_family
CNGB1 subfamily
uniprot
proteins
protein_family
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
uniprot
proteins
pubmed
10377344
uniprot
proteins
pubmed
11764791
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15134638
uniprot
proteins
pubmed
27405959
uniprot
proteins
pubmed
9539801
uniprot
proteins
pubmed
9878057
uniprot
proteins
sequence_length
1307
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:E1AZ71}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in rod outer segment membranes. {ECO:0000250|UniProtKB:E1AZ71}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium membrane {ECO:0000269|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 721..742; /note="Helical; Name=S1"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 752..773; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 789..808; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 825..837; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 850..872; /note="Helical; Name=S5"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 896..922; /note="Helical; Name=P-helix"; /evidence="ECO:0000250|UniProtKB:Q14028"; TRANSMEM 923..948; /note="Helical; Name=S6"; /evidence="ECO:0000250|UniProtKB:Q14028
uniprot
proteins