CNGA1
entrez
1259
canonical
uniprot
P29973
canonical
ensembl
ENSG00000198515
resolver
ensp
ENSP00000384264
resolver
ensp
ENSP00000389881
resolver
ensp
ENSP00000426862
resolver
ensp
ENSP00000538298
resolver
ensp
ENSP00000538299
resolver
ensp
ENSP00000606954
resolver
ensp
ENSP00000629623
resolver
enst
ENST00000402813
resolver
enst
ENST00000420489
resolver
enst
ENST00000514170
resolver
enst
ENST00000868239
resolver
enst
ENST00000868240
resolver
enst
ENST00000936895
resolver
enst
ENST00000959564
resolver
genesymbol
CNGA1
resolver
genesymbol_syn
CNCG
resolver
genesymbol_syn
CNCG1
resolver
hgnc
HGNC:2148
resolver
uniprot
A8K7K6
resolver
uniprot
J3KPZ2
resolver
uniprot
Q16279
resolver
uniprot
Q16485
resolver
uniprot
Q4W5E3
resolver
uniprot_entry
CNGA1_HUMAN
resolver
uniprot_sec
A8K7K6
resolver
uniprot_sec
J3KPZ2
resolver
uniprot_sec
Q16279
resolver
uniprot_sec
Q16485
resolver
uniprot_sec
Q4W5E3
resolver
activity_regulation
ACTIVITY REGULATION: Channel opening is activated by cGMP and at a much lesser extent by cAMP. Ca(2+) binding concominantly blocks monovalent cation currents. Inhibited by L-cis-diltiazem. {ECO:0000269|PubMed:33651975, ECO:0000269|PubMed:34699778}.
uniprot
proteins
amino_acid_sequence
MKNNIINTQQSFVTMPNVIVPDIEKEIRRMENGACSSFSEDDDSASTSEESENENPHARGSFSYKSLRKGGPSQREQYLPGAIALFNVNNSSNKDQEPEEKKKKKKEKKSKSDDKNENKNDPEKKKKKKDKEKKKKEEKSKDKKEEEKKEVVVIDPSGNTYYNWLFCITLPVMYNWTMVIARACFDELQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLEQGLLVKEELKLINKYKSNLQFKLDVLSLIPTDLLYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPNIFRISNLVMYIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYVFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHFRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTMLEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIDTEFSSIEGPGAESGPIDST
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 49 (RP49) [MIM:613756]: 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:15570217, ECO:0000269|PubMed:7479749}. 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. 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:Q00194, ECO:0000269|PubMed:33651975, ECO:0000269|PubMed:34699778, ECO:0000269|PubMed:7479749}.
uniprot
proteins
mass_dalton
79126
uniprot
proteins
mutagenesis
MUTAGEN 361; /note="E->Q: Renders the channel voltage-gated in the presence of saturated concentrations of cGMP."; /evidence="ECO:0000269|PubMed:33651975
uniprot
proteins
protein_family
CNGA1 subfamily
uniprot
proteins
protein_family
Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family
uniprot
proteins
pubmed
11764791
uniprot
proteins
pubmed
1372902
uniprot
proteins
pubmed
1379636
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15570217
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
33651975
uniprot
proteins
pubmed
34699778
uniprot
proteins
pubmed
7479749
uniprot
proteins
pubmed
7532814
uniprot
proteins
sequence_length
686
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:P29974}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:7479749}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in rod outer segment membranes. {ECO:0000250|UniProtKB:P29974}.
uniprot
proteins
transmembrane_region
TRANSMEM 166..187; /note="Helical; Name=S1"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 198..218; /note="Helical; Name=S2"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 244..262; /note="Helical; Name=S3"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 268..286; /note="Helical; Name=S4"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 294..317; /note="Helical; Name=S5"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 341..375; /note="Helical; Name=P-helix"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9"; TRANSMEM 376..400; /note="Helical; Name=S6"; /evidence="ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
uniprot
proteins