CNGA3 is the ligand-binding and pore-forming alpha subunit of the cone photoreceptor cyclic nucleotide-gated cation channel. It assembles with CNGB3 in cone outer-segment membranes, where intracellular cGMP promotes cation entry; light-driven loss of cGMP closes the channel and contributes to the cone electrical response. Human reconstituted complexes contain three CNGA3 subunits and one CNGB3. CNGA3 can also form conductive homomers and respond less effectively to cAMP. Biallelic CNGA3 variants cause achromatopsia and related cone dysfunction. Ortholog studies additionally report neuronal, glial and sensory-tissue expression and context-dependent protein interactions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005216 monoatomic ion channel activity | IEA GO_REF:0000002 | MODIFY | Summary: CNGA3 forms cGMP-gated cation-conducting channels. Reason: The ion-transport domain mapping is correct but broad. Human CNGA3 homomers and CNGA3/CNGB3 heteromers produce ligand-evoked currents, and purified human heteromers retain cGMP activation after lipid reconstitution. The specific cGMP-gated activity captures the principal physiological capability. Proposed replacements: intracellularly cGMP-activated cation channel activity |
| GO:0005221 intracellularly cyclic nucleotide-activated monoatomic cation channel activity | IEA GO_REF:0000002 | MODIFY | Summary: cGMP is the principal activating ligand of the cone channel. Reason: Human functional measurements and ligand-bound structures support the cGMP-specific child of the cyclic-nucleotide-gated channel term. The separate positive cAMP capability is retained in its own rows; this refinement does not deny secondary agonism. Proposed replacements: intracellularly cGMP-activated cation channel activity |
| GO:0005222 intracellularly cAMP-activated cation channel activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: cAMP can activate CNGA3-containing channels. Reason: The original human expression experiments detect cAMP activation of both CNGA3 homomers and CNGA3/CNGB3 heteromers, with lower potency and efficacy than cGMP. This supports the transferred capability as secondary agonist scope. The historical PAINT node placement was not reconstructed; target self-inclusion and the number of listed descendants are not objections to the transfer. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000025806 UNRESOLVED Human cAMP activation corroborates this secondary ligand capability; historical IBD placement is not reconstructed. |
| GO:0005222 intracellularly cAMP-activated cation channel activity | IDA PMID:12815043 Achromatopsia-associated mutation in the human cone photorec... | KEEP AS NON CORE | Summary: Human CNGA3 channels have experimentally measured cAMP responses. Reason: The original study compares human CNGA3 alone with wild-type and mutant CNGB3 combinations in Xenopus oocytes. Wild-type homomers and heteromers both respond to cAMP, although less effectively than to cGMP. Retain that real activity without making cAMP the defining physiological ligand or assigning CNGB3-mutant behavior to wild-type CNGA3. The abstract anchor describes the mutant-versus-wild-type ligand comparison; the independently inspected external Results establish the wild-type homomer and heteromer controls. Supporting Evidence: PMID:12815043 affinity for both cAMP and cGMP |
| GO:0005223 intracellularly cGMP-activated cation channel activity | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved cGMP-gated channel activity is directly corroborated in human CNGA3. Reason: Human expression, purified-channel reconstitution and cGMP-bound structures independently support the activity inherited from PTN000811708. These target experiments corroborate the biological judgment without reconstructing every historical IBD premise or changing the original source relationship. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000811708 UNRESOLVED Human cGMP currents corroborate the inherited activity; historical IBD placement is not reconstructed. |
| GO:0005223 intracellularly cGMP-activated cation channel activity | IDA PMID:12815043 Achromatopsia-associated mutation in the human cone photorec... | ACCEPT | Summary: Human CNGA3 supplies functional cGMP-gated channel subunits. Reason: Actual Methods and Results assay human CNGA3 homomers and CNGA3/CNGB3 heteromers in Xenopus oocytes. Intracellular cGMP activates membrane currents; the physiological heteromeric channel and experimentally conductive homomer are distinguished. Supporting Evidence: PMID:12815043 homomeric hCNGA3 channels |
| GO:0005223 intracellularly cGMP-activated cation channel activity | IEA GO_REF:0000107 | ACCEPT | Summary: The rat ortholog has a direct cGMP-activated current premise. Reason: Current Q9ER33 records include IDA from PMID:11387380. Its complete abstract explicitly describes cloned rat gustatory CNGA3 expressed in Xenopus oocytes and direct cGMP activation; independent human experiments corroborate the conserved activity. This is not an inference that all human alternative products were tested. |
| GO:0005223 intracellularly cGMP-activated cation channel activity | IMP PMID:24164424 Cyclic nucleotide-gated channel subunit glycosylation regula... | ACCEPT | Summary: Human CNGA3-containing channels conduct current in response to cGMP. Reason: The study uses tagged human CNGA3 with or without human CNGB3 in Xenopus oocytes, including wild-type controls and the CNGA3 N339Q glycosylation mutant. Inside-out recordings establish cGMP-evoked currents and changes after MMP exposure. Proteolysis is performed by MMPs; it is not a catalytic activity of CNGA3. Supporting Evidence: PMID:24164424 We assessed CNG channel gating properties by measuring cGMP dose-response relationships |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: HuRI records a positive CNGA3–MIS18A interaction. Reason: Three exact human IntAct records identify Q16281 with Q9NYP9/MIS18A in array, prey-pooling and validated two-hybrid assays. CNGA3 is the prey in the first two records; the validated record assigns neutral roles. Retain the measured interaction as non-core without inferring an endogenous centromeric function, adaptor activity or shared native compartment. Supporting Evidence: |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma-membrane activity is consistent with the conserved channel role. Reason: Human expression experiments combine surface fluorescence with currents recorded from excised membrane patches. Mouse cone localization independently places the protein in outer-segment membrane folds. These observations corroborate the PAINT compartment; the historical ancestral placement itself remains uninspected. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000811708 UNRESOLVED Human surface localization and mouse outer-segment membranes corroborate the compartment; historical node placement remains uninspected. |
| GO:0005886 plasma membrane | IDA PMID:12815043 Achromatopsia-associated mutation in the human cone photorec... | ACCEPT | Summary: Expressed human CNGA3 reaches the plasma membrane. Reason: The original study measures GFP-tagged human CNGA3 at the oocyte surface with non-tagged controls and separately records functional membrane currents. CNGB3 coexpression changes surface fluorescence without substantially changing total CNGA3 protein in the tested comparison. Tags, expression ratios and disease mutants are not assumed to represent every natural product. Supporting Evidence: PMID:12815043 expression of green fluorescent protein-tagged hCNGA3 subunits |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt cell-membrane mapping is biologically supported. Reason: CNGA3 is an integral membrane channel subunit, and surface imaging and membrane-patch currents directly support the mapped plasma-membrane compartment. |
| GO:0006811 monoatomic ion transport | IEA GO_REF:0000002 | MODIFY | Summary: The transported species are cations crossing a membrane. Reason: Human channel recordings and purified-channel reconstitution establish transmembrane cation conduction. The specific process preserves both the transported-ion class and membrane crossing that are absent from the broad InterPro ion-transport mapping. Proposed replacements: monoatomic cation transmembrane transport |
| GO:0006812 monoatomic cation transport | IMP PMID:24164424 Cyclic nucleotide-gated channel subunit glycosylation regula... | MODIFY | Summary: The original experiment measures transmembrane cation current. Reason: Human CNGA3-containing channels in excised oocyte patches carry current in sodium-based solutions, with cGMP-dependent gating and MMP-dependent changes. Refine broad cation transport to cation transmembrane transport; calcium used to support MMP activity is not itself a calcium-permeation measurement. Proposed replacements: monoatomic cation transmembrane transport Supporting Evidence: |
| GO:0007165 signal transduction | TAS PMID:9517456 Cloning, chromosomal localization and functional expression ... | MODIFY | Summary: CNGA3 performs the cGMP-controlled channel step of cone phototransduction. Reason: The original human clone produces cGMP-activated currents and is expressed in retinal cones. Later human structures and reconstituted currents identify the performed effector step: CNGA3 supplies ligand-recognition and pore elements that change cation conductance as phototransduction changes cGMP. Phototransduction specifies this signaling context without asserting that CNGA3 absorbs photons. The original broad TAS source assertion remains unchanged. Proposed replacements: phototransduction |
| GO:0007601 visual perception | IMP PMID:10958649 Mutations in the CNGB3 gene encoding the beta-subunit of the... | UNDECIDED | Summary: The exact CNGA3 IMP linkage to this clinical paper remains unresolved. Reason: The recovered original Methods and selected Results study CNGB3 in achromatopsia families after excluding CNGA3 mutations or linkage; the paper also discusses previously established CNGA3 visual function. Those inspected passages do not establish the particular CNGA3 perturbation underlying this source object. Preserve the source-specific uncertainty without declaring the whole paper miscited or disputing the independently demonstrated CNGA3 visual role. |
| GO:0007601 visual perception | IMP PMID:11536077 CNGA3 mutations in hereditary cone photoreceptor disorders. | ACCEPT | Summary: Human CNGA3 defects impair cone-mediated vision. Reason: The original human mutation cohort combines clinical visual testing, ERGs, sequence analysis and segregation. Complete and incomplete achromatopsia and some cone-dystrophy presentations establish the visual consequence of CNGA3 dysfunction. This supports the sensory role without attributing every variant to the same molecular defect. Supporting Evidence: |
| GO:0007601 visual perception | IMP PMID:15712225 Cone cGMP-gated channel mutations and clinical findings in p... | ACCEPT | Summary: The clinical source positively links CNGA3 variants to cone dysfunction. Reason: The complete authentic abstract explicitly reports CNGA3 mutations in 12 of 36 achromats and accompanying acuity, color-vision and ERG findings. The original full body was not recovered; the positive human observation and independent full CNGA3 cohort support retention without inventing patient-level or assay details. |
| GO:0007601 visual perception | TAS PMID:9662398 Total colourblindness is caused by mutations in the gene enc... | ACCEPT | Summary: CNGA3 is required for normal cone color vision. Reason: The original complete abstract identifies segregating CNGA3 missense mutations in five families with complete achromatopsia, preserved rod responses and absent cone responses. Later functional studies identify the channel activity performed by CNGA3. The abstract-level access limit does not negate this explicitly reported positive result. |
| GO:0015276 ligand-gated monoatomic ion channel activity | TAS PMID:9517456 Cloning, chromosomal localization and functional expression ... | MODIFY | Summary: The ligand-gated activity can be specified as cGMP-gated. Reason: The original cloning abstract directly reports cGMP-activated currents from human CNGA3 in Xenopus oocytes. Later functional and structural sources corroborate this precise activity. Proposed replacements: intracellularly cGMP-activated cation channel activity |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Human CNGA3 reaches the plasma membrane. Reason: The broad membrane mapping can be refined using human surface imaging and functional membrane-patch recordings. The six-transmembrane architecture is consistent with this compartment; the original InterPro source object remains unchanged. The direct human surface-expression scope is retained; convergence with existing plasma-membrane assertions is allowed for MODIFY and is not a reason to replace this evidence with a more specific mouse compartment by default. Proposed replacements: plasma membrane |
| GO:0017022 myosin binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat donor directly binds the myosin VIIa tail. Reason: The actual rat study uses CNGA3 residues 1–146, rat organ-of-Corti constructs, GST pulldown and surface plasmon resonance with the myosin VIIa tail. These assays support the donor binding premise, including calcium-dependent changes. Retain the ortholog transfer as non-core; fragment binding does not establish human native hair-cell mechanotransduction or all-product interactions. |
| GO:0017071 intracellular cyclic nucleotide activated cation channel complex | IBA GO_REF:0000033 | ACCEPT | Summary: CNGA3 contributes to the cyclic-nucleotide-activated channel complex. Reason: Functional human CNGA3/CNGB3 coexpression and purified human structures corroborate complex membership. The full-length structural preparation contains three CNGA3 subunits and one CNGB3; that structural count is distinct from expression-plasmid or RNA ratios. The PAINT historical node was not independently reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000811708 UNRESOLVED Human assembled-channel measurements corroborate the complex; the historical family placement remains uninspected. |
| GO:0017071 intracellular cyclic nucleotide activated cation channel complex | IDA PMID:12815043 Achromatopsia-associated mutation in the human cone photorec... | ACCEPT | Summary: Human CNGA3 assembles with CNGB3 into functional channels. Reason: The original study compares homomeric CNGA3 with wild-type and mutant CNGB3 coexpression, measuring distinct ligand responses, rectification and surface behavior. These data support the specific complex; later structures resolve its composition without converting the old RNA mixing ratio into a stoichiometric measurement. The abstract anchor is a positive result for the S435F-containing heteromer; wild-type heteromers are the comparison. The independently inspected original Results establish the wild-type assembly context. |
| GO:0030425 dendrite | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise dendritic localization premise needs the original imaging. Reason: The live rat Q9ER33 donor has an IDA dendrite record from PMID:18434027, and the complete abstract positively reports CNGA3 in several olfactory-bulb neuronal populations. Full original Methods and subcellular panels were not recovered after publisher and repository searches, so the exact dendritic result and its transfer remain unverified here. This is an access limit, not evidence of absence. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q9ER33 · Rat Cnga3 UNRESOLVED The current exact donor annotation is recovered; the source-specific full-text compartment or historical reagent identity is not independently resolved. |
| GO:0030553 cGMP binding | IBA GO_REF:0000033 | ACCEPT | Summary: CNGA3 has a directly resolved cGMP-binding pocket. Reason: The PAINT binding assertion is corroborated by human CNGA3 cGMP density in the cytoplasmic cyclic-nucleotide-binding domains of assembled channels. Ligand occupancy can occur in closed as well as open states, so binding and pore opening are distinguished; the historical node placement was not reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000025806 UNRESOLVED Human cGMP pocket density corroborates ligand binding; the historical node placement remains uninspected. |
| GO:0030553 cGMP binding | IDA PMID:37463923 Conformational trajectory of allosteric gating of the human ... | ACCEPT | Summary: Human CNGA3 directly contacts cGMP in the assembled channel. Reason: The structural study resolves cGMP in the CNGA3 binding pockets. Full-length detergent preparations and engineered N-terminally truncated nanodisc preparations are separately described; the latter are not natural alternative products. This is physical ligand-binding evidence rather than an activation-curve affinity estimate alone. Supporting Evidence: PMID:37463923 cGMP is bound to all four subunits |
| GO:0030553 cGMP binding | IEA GO_REF:0000107 | ACCEPT | Summary: The rat transfer of cGMP recognition is corroborated by human structure. Reason: The current rat donor cites direct cGMP activation in PMID:11387380. Functional activation alone does not provide a purified binding constant, but independent human CNGA3 structures directly place cGMP in the binding pocket and support the conserved molecular recognition. |
| GO:0030553 cGMP binding | IMP PMID:24164424 Cyclic nucleotide-gated channel subunit glycosylation regula... | ACCEPT | Summary: The mutant-based binding inference agrees with independent structural evidence. Reason: The original human-channel experiments measure cGMP dose-response shifts after MMP treatment and glycosylation perturbation. Their half-activation concentration combines binding and gating and is not a purified dissociation constant. Direct cGMP density in later human CNGA3 structures independently supports retaining the binding capability. |
| GO:0032026 response to magnesium ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Magnesium modulates the rat CNGA3 channel current. Reason: The exact RGD donor IDA records rat tongue-derived CNGA3 expressed in Xenopus oocytes, with magnesium-dependent inhibition of channel-mediated sodium current from either membrane side. CNGA3 conducts the current whose change is measured. The response definition does not require an adaptive or homeostatic mechanism, so this existing experimental premise is retained as contextual, non-core regulation. Original full Methods and figures remain uninspected; the abstract does not establish a physiological human response, magnesium permeation or an automatic rule that every inhibited protein merits a response annotation. |
| GO:0034220 monoatomic ion transmembrane transport | IEA GO_REF:0000107 | MODIFY | Summary: CNGA3 mediates cation transmembrane conduction. Reason: Rat donor recordings show cyclic-nucleotide-evoked cation currents, and human channel measurements independently specify cation conduction. Refine the broad ion-transmembrane term to its cation-specific form without changing the original Ensembl source. Proposed replacements: monoatomic cation transmembrane transport |
| GO:0042622 photoreceptor outer segment membrane | ISS GO_REF:0000024 | ACCEPT | Summary: The mouse ortholog localizes to cone outer-segment membranes. Reason: The official MGI donor is mouse Cnga3. Actual antibody-controlled mouse immunolabeling and pre-embedding EM place the signal in outer-segment membrane folds. Preserve the ISS inference rather than describing this as an endogenous human localization experiment. |
| GO:0042622 photoreceptor outer segment membrane | ISS GO_REF:0000024 | ACCEPT | Summary: The sequence-resolved mouse donor supports outer-segment membrane localization. Reason: Q9JJZ8 identifies mouse Cnga3, consistent with the official MGI donor. The original study tests a cloned 631-residue mouse construct and a C-terminal antibody with transfected-cell specificity controls; native retinal EM provides the membrane premise. These historical mouse constructs do not define the distribution of every human alternative product. |
| GO:0043025 neuronal cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rat olfactory-bulb neurons provide a positive cell-body localization context. Reason: The current donor has an IDA neuronal-cell-body record from PMID:18434027, whose complete abstract explicitly reports CNGA3 immunoreactivity in principal neurons and interneurons. Retain this non-core ortholog context while noting that detailed original imaging controls and endogenous human subcellular localization were not independently inspected. |
| GO:0043194 axon initial segment | IEA GO_REF:0000107 | UNDECIDED | Summary: The axon-initial-segment assertion remains source-limited. Reason: The current rat donor preserves a genuine IDA premise from PMID:18434027. The accessible abstract establishes neuronal expression but does not resolve the precise axon-initial-segment labeling or its controls, and the full original article was not recovered. Retain uncertainty without treating the cone-channel specialization as evidence against neuronal localization. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q9ER33 · Rat Cnga3 UNRESOLVED The current exact donor annotation is recovered; the source-specific full-text compartment or historical reagent identity is not independently resolved. |
| GO:0043204 perikaryon | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact historical channel identity behind this perikaryon transfer is unresolved. Reason: The rat donor points to PMID:12021210. Its complete abstract reports olfactory CNG2, CNG4.3 and CNG5 in rat GnRH perikarya, using historical nomenclature. Original full probe and antibody details were not recovered, so a CNGA3-specific premise cannot be verified from those names alone. Preserve the source object without claiming a demonstrated paralog error. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q9ER33 · Rat Cnga3 UNRESOLVED The current exact donor annotation is recovered; the source-specific full-text compartment or historical reagent identity is not independently resolved. |
| GO:0045296 cadherin binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rat CNGA3 directly binds the exon-68-containing cadherin 23 fragment. Reason: The original rat study confirms the interaction by two-hybrid reversal and empty-vector controls, GST pulldown and surface plasmon resonance. CDH23 lacking exon 68 does not show the same binding. Retain the specific donor capability with its fragment and calcium dependence; neither a human full-length interaction nor a direct adhesion activity follows automatically. |
| GO:0051591 response to cAMP | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cAMP directly activates the rat donor channel under experimental conditions. Reason: The donor IDA source explicitly measures cAMP-evoked currents, and human CNGA3-containing channels independently exhibit lower-efficacy cAMP agonism. This supports the response capability as non-core; it does not establish cAMP as the principal physiological cone signal. |
| GO:0055085 transmembrane transport | IEA GO_REF:0000002 | MODIFY | Summary: Cation conduction specifies the broad transmembrane-transport mapping. Reason: Functional human CNGA3-containing channels carry cation currents through a membrane. The specific cation transmembrane transport term preserves the direct performed transport step rather than adding an unrelated process. Proposed replacements: monoatomic cation transmembrane transport |
| GO:0060041 retina development in camera-type eye | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The retinal-development transfer is retained as a downstream tissue context. Reason: The official mouse record contains experimental IGI premises from PMID:21124780 and a cone-development IMP premise associated with the cpfl5 model. The inspected triple-mutant study examines adult photoreception and cone-transducin localization, while the model-resource table lists Cnga3 cone-function loss. These positive retinal contexts do not establish a separate CNGA3-directed patterning mechanism. Preserve the curated PAINT judgment as non-core; the historical PTN002900733 placement was not reconstructed. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900733 UNRESOLVED Official mouse experimental retinal premises are recovered, but the historical developmental IBD placement and its exact rationale remain uninspected. |
| GO:0097386 glial cell projection | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact glial-projection compartment requires the original localization evidence. Reason: The current rat donor has an IDA glial-cell-projection annotation, and the original abstract positively reports CNGA3 in olfactory ensheathing glia. Full original subcellular images were not recovered, so this finer compartment and its transfer remain unverified in this review. No absence of glial expression is inferred. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q9ER33 · Rat Cnga3 UNRESOLVED The current exact donor annotation is recovered; the source-specific full-text compartment or historical reagent identity is not independently resolved. |
| GO:0098655 monoatomic cation transmembrane transport | IBA GO_REF:0000033 | ACCEPT | Summary: CNGA3 performs cation transmembrane transport as part of a gated channel. Reason: Human expression and purified-channel reconstitution provide direct cation-current evidence that corroborates the PAINT process assignment. The preserved ancestral node records curated inheritance; its complete historical reconstruction is distinct from the independently supported target transport activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000811708 UNRESOLVED Human membrane currents corroborate cation transport; the historical node placement remains uninspected. |
| GO:0098659 inorganic cation import across plasma membrane | IEA GO_REF:0000107 | ACCEPT | Summary: CNGA3-containing channels admit extracellular cations through the plasma membrane. Reason: The donor source reports rat CNGgust currents after expression in HEK cells, and later rat and human channel measurements confirm cation conduction in response to intracellular cyclic nucleotides. Inward current at negative membrane potentials supports import, while the same passive channel can conduct outward under reversed electrochemical conditions. This is not an active pump claim. |
| GO:0120201 cone photoreceptor disc membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Mouse cone-disc membrane localization supports the preserved ISS assertion. Reason: Actual pre-embedding EM Results place the mouse signal almost exclusively on layered plasma-membrane folds forming cone discs, and the Discussion explicitly distinguishes these cone infoldings from rod-disc compartmentalization. Retain the specific disc-membrane term at ortholog scope; it is not contradicted by the plasma-membrane annotation and is not a direct human experiment. |
| GO:1902495 transmembrane transporter complex | IDA PMID:24164424 Cyclic nucleotide-gated channel subunit glycosylation regula... | MODIFY | Summary: The assayed transporter complex is the cyclic-nucleotide-activated cation channel. Reason: The source coexpresses human CNGA3 with human CNGB3 and measures functional heteromeric currents. The specific channel-complex term is more informative than generic transmembrane transporter complex and is independently corroborated by purified human heteromer structures. Proposed replacements: intracellular cyclic nucleotide activated cation channel complex |
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Download this section (compressed HTML)Q: Which natural human CNGA3 alternative products are present in cones and in reported extra-retinal compartments, and how do their targeting and ligand responses differ?
Q: Which original probe and antibody sequences underlie the rat perikaryon and fine neuronal/glial compartment annotations, and how do their historical names map to current channel genes?
Q: Does the developmental PAINT placement reflect a direct role in cone maturation, a consequence of channel-dependent physiology, or a broader retinal phenotype?
Experiment: Compare sequence-verified human natural products with CNGB3 at controlled expression, measuring cGMP and cAMP responses and surface delivery separately from channel assembly.
Experiment: Use endogenous tagging and genetically controlled antibodies to test the reported neuronal and glial compartments, resolving cell-body, dendritic and axon-initial-segment signals.
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