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Protein

Cyclic nucleotide-gated cation channel alpha-3

Gene

CNGA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei549cGMPSequence analysis1
Binding sitei564cGMPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi482 – 605cGMPAdd BLAST124

GO - Molecular functioni

  • cGMP binding Source: UniProtKB
  • intracellular cAMP activated cation channel activity Source: GO_Central
  • intracellular cGMP activated cation channel activity Source: UniProtKB
  • ligand-gated ion channel activity Source: ProtInc
  • voltage-gated potassium channel activity Source: GO_Central

GO - Biological processi

  • cation transport Source: UniProtKB
  • regulation of membrane potential Source: GO_Central
  • response to cAMP Source: Ensembl
  • response to corticosteroid Source: Ensembl
  • response to magnesium ion Source: Ensembl
  • signal transduction Source: ProtInc
  • transport Source: ProtInc
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport, Vision

Keywords - Ligandi

cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000144191-MONOMER.

Protein family/group databases

TCDBi1.A.1.5.12. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic nucleotide-gated cation channel alpha-3
Alternative name(s):
Cone photoreceptor cGMP-gated channel subunit alpha
Cyclic nucleotide-gated channel alpha-3
Short name:
CNG channel alpha-3
Short name:
CNG-3
Short name:
CNG3
Gene namesi
Name:CNGA3
Synonyms:CNCG3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2150. CNGA3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 166CytoplasmicSequence analysisAdd BLAST166
Transmembranei167 – 187Helical; Name=H1Sequence analysisAdd BLAST21
Topological domaini188 – 199ExtracellularSequence analysisAdd BLAST12
Transmembranei200 – 220Helical; Name=H2Sequence analysisAdd BLAST21
Topological domaini221 – 252CytoplasmicSequence analysisAdd BLAST32
Transmembranei253 – 273Helical; Name=H3Sequence analysisAdd BLAST21
Topological domaini274 – 302ExtracellularSequence analysisAdd BLAST29
Transmembranei303 – 323Helical; Name=H4Sequence analysisAdd BLAST21
Topological domaini324 – 378CytoplasmicSequence analysisAdd BLAST55
Transmembranei379 – 399Helical; Name=H5Sequence analysisAdd BLAST21
Topological domaini400 – 481ExtracellularSequence analysisAdd BLAST82
Transmembranei482 – 502Helical; Name=H6Sequence analysisAdd BLAST21
Topological domaini503 – 694CytoplasmicSequence analysisAdd BLAST192

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Achromatopsia 2 (ACHM2)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn ocular stationary disorder due to the absence of functioning cone photoreceptors in the retina. It is characterized by total colorblindness, low visual acuity, photophobia and nystagmus.
See also OMIM:216900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047566162D → V in ACHM2. 1 PublicationCorresponds to variant rs747447519dbSNPEnsembl.1
Natural variantiVAR_010903163P → L in ACHM2. 2 PublicationsCorresponds to variant rs104893612dbSNPEnsembl.1
Natural variantiVAR_071436171W → C in ACHM2; also found in patients with cone-rod dystrophy. 1 PublicationCorresponds to variant rs762773298dbSNPEnsembl.1
Natural variantiVAR_047567181Y → C in ACHM2. 1 Publication1
Natural variantiVAR_047568182N → Y in ACHM2. 1 Publication1
Natural variantiVAR_047569186L → F in ACHM2. 1 Publication1
Natural variantiVAR_047570191C → Y in ACHM2. 1 PublicationCorresponds to variant rs761554853dbSNPEnsembl.1
Natural variantiVAR_047571194E → K in ACHM2. 1 Publication1
Natural variantiVAR_071438223R → Q in ACHM2. 1 PublicationCorresponds to variant rs762668060dbSNPEnsembl.1
Natural variantiVAR_047572223R → W in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs138958917dbSNPEnsembl.1
Natural variantiVAR_047573224T → R in ACHM2. 1 Publication1
Natural variantiVAR_047574228E → K in ACHM2; unknown pathological significance; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; the channel density into the cell membrane is considerably improved by decreasing the cultivation temperature. 1 PublicationCorresponds to variant rs147415641dbSNPEnsembl.1
Natural variantiVAR_047575249F → S in ACHM2. 1 Publication1
Natural variantiVAR_047576260D → N in ACHM2; also found in patients with cone-rod dystrophy. 2 PublicationsCorresponds to variant rs374258471dbSNPEnsembl.1
Natural variantiVAR_047577263Y → D in ACHM2. 1 Publication1
Natural variantiVAR_047578267G → D in ACHM2. 1 PublicationCorresponds to variant rs781673067dbSNPEnsembl.1
Natural variantiVAR_071442274R → K in ACHM2. 1 Publication1
Natural variantiVAR_047579277R → C in ACHM2; also found in patients with cone-rod dystrophy. 5 PublicationsCorresponds to variant rs104893620dbSNPEnsembl.1
Natural variantiVAR_047580277R → H in ACHM2; also found in patients with cone-rod dystrophy; does not form functional homomeric or heteromeric channels. 2 PublicationsCorresponds to variant rs778114016dbSNPEnsembl.1
Natural variantiVAR_071443278L → P in ACHM2. 1 PublicationCorresponds to variant rs763421555dbSNPEnsembl.1
Natural variantiVAR_010904283R → Q in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature. 3 PublicationsCorresponds to variant rs104893614dbSNPEnsembl.1
Natural variantiVAR_010905283R → W in ACHM2; also found in patients with cone-rod dystrophy. 3 PublicationsCorresponds to variant rs104893613dbSNPEnsembl.1
Natural variantiVAR_010906291T → R in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 1.8; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature. 3 PublicationsCorresponds to variant rs104893616dbSNPEnsembl.1
Natural variantiVAR_047581312Missing in ACHM2. 1 Publication1
Natural variantiVAR_071444322F → S in ACHM2. 1 Publication1
Natural variantiVAR_075493323A → D in ACHM2. 1 Publication1
Natural variantiVAR_047582341S → P in ACHM2. 2 Publications1
Natural variantiVAR_047583369T → S in ACHM2. 1 PublicationCorresponds to variant rs766637612dbSNPEnsembl.1
Natural variantiVAR_047584372P → S in ACHM2. 1 Publication1
Natural variantiVAR_047585380F → S in ACHM2. 1 Publication1
Natural variantiVAR_047586401S → P in ACHM2. 1 Publication1
Natural variantiVAR_047587406M → T in ACHM2. 1 Publication1
Natural variantiVAR_010910410R → W in ACHM2. 3 PublicationsCorresponds to variant rs137852608dbSNPEnsembl.1
Natural variantiVAR_047588427R → C in ACHM2. 2 PublicationsCorresponds to variant rs141386891dbSNPEnsembl.1
Natural variantiVAR_071447436R → Q in ACHM2. 1 PublicationCorresponds to variant rs767083685dbSNPEnsembl.1
Natural variantiVAR_047589436R → W in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs104893621dbSNPEnsembl.1
Natural variantiVAR_047590439R → W in ACHM2; also found in patients with cone-rod dystrophy; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius. 2 PublicationsCorresponds to variant rs749842881dbSNPEnsembl.1
Natural variantiVAR_047591469A → T in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; the left shift in the dose-response relationship of the mutant CNGA3 is less distinctive than in homomeric channels with this mutation indicating a partial rescue effect of the CNGB3 subunit; is in large part located in the cell membrane at 37 and 27 degrees Celsius. 1 PublicationCorresponds to variant rs117522010dbSNPEnsembl.1
Natural variantiVAR_047592471N → S in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is unchanged. 2 PublicationsCorresponds to variant rs373954146dbSNPEnsembl.1
Natural variantiVAR_047593485D → V in ACHM2. 1 Publication1
Natural variantiVAR_047594510C → S in ACHM2. 1 Publication1
Natural variantiVAR_047595513G → E in ACHM2. 1 Publication1
Natural variantiVAR_047596516G → E in ACHM2. 1 Publication1
Natural variantiVAR_047597522I → T in ACHM2. 1 Publication1
Natural variantiVAR_047598525G → D in ACHM2. 1 Publication1
Natural variantiVAR_010907529V → M in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs104893619dbSNPEnsembl.1
Natural variantiVAR_071449543 – 545Missing in ACHM2. 1 Publication3
Natural variantiVAR_010908547F → L in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; is in large part located in the cell membrane at 37 and 27 degrees Celsius. 4 PublicationsCorresponds to variant rs104893617dbSNPEnsembl.1
Natural variantiVAR_047599548G → R in ACHM2. 1 PublicationCorresponds to variant rs781227859dbSNPEnsembl.1
Natural variantiVAR_010909557G → R in ACHM2; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 3.0; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; average cGMP maximum current is decreased to half of the mean wild-type value for the mutant CNGA3 + CNGB3. 3 PublicationsCorresponds to variant rs104893615dbSNPEnsembl.1
Natural variantiVAR_047600563R → H in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is significantly reduced. 2 PublicationsCorresponds to variant rs552069173dbSNPEnsembl.1
Natural variantiVAR_047601565T → M in ACHM2. 2 PublicationsCorresponds to variant rs201747279dbSNPEnsembl.1
Natural variantiVAR_047602569R → H in ACHM2. 3 PublicationsCorresponds to variant rs201782746dbSNPEnsembl.1
Natural variantiVAR_047603573Y → C in ACHM2. 1 Publication1
Natural variantiVAR_047604590E → K in ACHM2; also found in patients with cone-rod dystrophy; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. 3 PublicationsCorresponds to variant rs763041373dbSNPEnsembl.1
Natural variantiVAR_047605593E → K in ACHM2. 1 PublicationCorresponds to variant rs774676415dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

DisGeNETi1261.
MalaCardsiCNGA3.
MIMi216900. phenotype.
OpenTargetsiENSG00000144191.
Orphaneti49382. Achromatopsia.
1872. Cone rod dystrophy.
PharmGKBiPA26660.

Chemistry databases

GuidetoPHARMACOLOGYi396.

Polymorphism and mutation databases

BioMutaiCNGA3.
DMDMi13959682.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002193171 – 694Cyclic nucleotide-gated cation channel alpha-3Add BLAST694

Proteomic databases

PaxDbiQ16281.
PeptideAtlasiQ16281.
PRIDEiQ16281.

PTM databases

iPTMnetiQ16281.
PhosphoSitePlusiQ16281.

Expressioni

Tissue specificityi

Prominently expressed in retina.

Gene expression databases

BgeeiENSG00000144191.
CleanExiHS_CNGA3.
GenevisibleiQ16281. HS.

Interactioni

Subunit structurei

Tetramer formed of three CNGA3 and one CNGB3 modulatory subunits.3 Publications

Protein-protein interaction databases

BioGridi107661. 25 interactors.
IntActiQ16281. 1 interactor.
STRINGi9606.ENSP00000272602.

Structurei

Secondary structure

1694
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi626 – 668Combined sources43

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SWYX-ray1.90A/B/C626-669[»]
ProteinModelPortaliQ16281.
SMRiQ16281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili626 – 669Add BLAST44

Domaini

The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits.

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0500. Eukaryota.
ENOG410YWWI. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiQ16281.
KOiK04950.
OMAiYLWANRK.
OrthoDBiEOG091G03EW.
PhylomeDBiQ16281.
TreeFamiTF319048.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16281-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKINTQYSH PSRTHLKVKT SDRDLNRAEN GLSRAHSSSE ETSSVLQPGI
60 70 80 90 100
AMETRGLADS GQGSFTGQGI ARLSRLIFLL RRWAARHVHH QDQGPDSFPD
110 120 130 140 150
RFRGAELKEV SSQESNAQAN VGSQEPADRG RSAWPLAKCN TNTSNNTEEE
160 170 180 190 200
KKTKKKDAIV VDPSSNLYYR WLTAIALPVF YNWYLLICRA CFDELQSEYL
210 220 230 240 250
MLWLVLDYSA DVLYVLDVLV RARTGFLEQG LMVSDTNRLW QHYKTTTQFK
260 270 280 290 300
LDVLSLVPTD LAYLKVGTNY PEVRFNRLLK FSRLFEFFDR TETRTNYPNM
310 320 330 340 350
FRIGNLVLYI LIIIHWNACI YFAISKFIGF GTDSWVYPNI SIPEHGRLSR
360 370 380 390 400
KYIYSLYWST LTLTTIGETP PPVKDEEYLF VVVDFLVGVL IFATIVGNVG
410 420 430 440 450
SMISNMNASR AEFQAKIDSI KQYMQFRKVT KDLETRVIRW FDYLWANKKT
460 470 480 490 500
VDEKEVLKSL PDKLKAEIAI NVHLDTLKKV RIFQDCEAGL LVELVLKLRP
510 520 530 540 550
TVFSPGDYIC KKGDIGKEMY IINEGKLAVV ADDGVTQFVV LSDGSYFGEI
560 570 580 590 600
SILNIKGSKS GNRRTANIRS IGYSDLFCLS KDDLMEALTE YPEAKKALEE
610 620 630 640 650
KGRQILMKDN LIDEELARAG ADPKDLEEKV EQLGSSLDTL QTRFARLLAE
660 670 680 690
YNATQMKMKQ RLSQLESQVK GGGDKPLADG EVPGDATKTE DKQQ
Length:694
Mass (Da):78,838
Last modified:May 4, 2001 - v2
Checksum:iAE00B4EE760D70A0
GO
Isoform 2 (identifier: Q16281-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     132-150: SAWPLAKCNTNTSNNTEEE → R

Note: No experimental confirmation available.
Show »
Length:676
Mass (Da):76,903
Checksum:iC6FB264BE7EB3D8D
GO
Isoform 3 (identifier: Q16281-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: MAKINTQYSH...QGSFTGQGIA → METRGLADSG...SPGCSSGPQG

Note: No experimental confirmation available.
Show »
Length:698
Mass (Da):79,062
Checksum:i77B8976209457738
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04756548P → L.1 PublicationCorresponds to variant rs62156348dbSNPEnsembl.1
Natural variantiVAR_071435120N → D.1 PublicationCorresponds to variant rs199859850dbSNPEnsembl.1
Natural variantiVAR_010902153T → M.2 PublicationsCorresponds to variant rs34314205dbSNPEnsembl.1
Natural variantiVAR_047566162D → V in ACHM2. 1 PublicationCorresponds to variant rs747447519dbSNPEnsembl.1
Natural variantiVAR_010903163P → L in ACHM2. 2 PublicationsCorresponds to variant rs104893612dbSNPEnsembl.1
Natural variantiVAR_071436171W → C in ACHM2; also found in patients with cone-rod dystrophy. 1 PublicationCorresponds to variant rs762773298dbSNPEnsembl.1
Natural variantiVAR_047567181Y → C in ACHM2. 1 Publication1
Natural variantiVAR_047568182N → Y in ACHM2. 1 Publication1
Natural variantiVAR_047569186L → F in ACHM2. 1 Publication1
Natural variantiVAR_047570191C → Y in ACHM2. 1 PublicationCorresponds to variant rs761554853dbSNPEnsembl.1
Natural variantiVAR_047571194E → K in ACHM2. 1 Publication1
Natural variantiVAR_071437198E → K.1 Publication1
Natural variantiVAR_021963198E → K.1 PublicationCorresponds to variant rs2271041dbSNPEnsembl.1
Natural variantiVAR_071438223R → Q in ACHM2. 1 PublicationCorresponds to variant rs762668060dbSNPEnsembl.1
Natural variantiVAR_047572223R → W in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs138958917dbSNPEnsembl.1
Natural variantiVAR_071439224T → I Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 Publication1
Natural variantiVAR_047573224T → R in ACHM2. 1 Publication1
Natural variantiVAR_047574228E → K in ACHM2; unknown pathological significance; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; the channel density into the cell membrane is considerably improved by decreasing the cultivation temperature. 1 PublicationCorresponds to variant rs147415641dbSNPEnsembl.1
Natural variantiVAR_071440247T → M.1 PublicationCorresponds to variant rs148616345dbSNPEnsembl.1
Natural variantiVAR_047575249F → S in ACHM2. 1 Publication1
Natural variantiVAR_071441258P → R Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 Publication1
Natural variantiVAR_047576260D → N in ACHM2; also found in patients with cone-rod dystrophy. 2 PublicationsCorresponds to variant rs374258471dbSNPEnsembl.1
Natural variantiVAR_047577263Y → D in ACHM2. 1 Publication1
Natural variantiVAR_047578267G → D in ACHM2. 1 PublicationCorresponds to variant rs781673067dbSNPEnsembl.1
Natural variantiVAR_071442274R → K in ACHM2. 1 Publication1
Natural variantiVAR_047579277R → C in ACHM2; also found in patients with cone-rod dystrophy. 5 PublicationsCorresponds to variant rs104893620dbSNPEnsembl.1
Natural variantiVAR_047580277R → H in ACHM2; also found in patients with cone-rod dystrophy; does not form functional homomeric or heteromeric channels. 2 PublicationsCorresponds to variant rs778114016dbSNPEnsembl.1
Natural variantiVAR_071443278L → P in ACHM2. 1 PublicationCorresponds to variant rs763421555dbSNPEnsembl.1
Natural variantiVAR_010904283R → Q in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature. 3 PublicationsCorresponds to variant rs104893614dbSNPEnsembl.1
Natural variantiVAR_010905283R → W in ACHM2; also found in patients with cone-rod dystrophy. 3 PublicationsCorresponds to variant rs104893613dbSNPEnsembl.1
Natural variantiVAR_010906291T → R in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 1.8; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature. 3 PublicationsCorresponds to variant rs104893616dbSNPEnsembl.1
Natural variantiVAR_047581312Missing in ACHM2. 1 Publication1
Natural variantiVAR_071444322F → S in ACHM2. 1 Publication1
Natural variantiVAR_075493323A → D in ACHM2. 1 Publication1
Natural variantiVAR_071445330F → S Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 Publication1
Natural variantiVAR_071446334S → F Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 Publication1
Natural variantiVAR_069398335W → C.1 Publication1
Natural variantiVAR_047582341S → P in ACHM2. 2 Publications1
Natural variantiVAR_047583369T → S in ACHM2. 1 PublicationCorresponds to variant rs766637612dbSNPEnsembl.1
Natural variantiVAR_047584372P → S in ACHM2. 1 Publication1
Natural variantiVAR_047585380F → S in ACHM2. 1 Publication1
Natural variantiVAR_047586401S → P in ACHM2. 1 Publication1
Natural variantiVAR_047587406M → T in ACHM2. 1 Publication1
Natural variantiVAR_010910410R → W in ACHM2. 3 PublicationsCorresponds to variant rs137852608dbSNPEnsembl.1
Natural variantiVAR_047588427R → C in ACHM2. 2 PublicationsCorresponds to variant rs141386891dbSNPEnsembl.1
Natural variantiVAR_071447436R → Q in ACHM2. 1 PublicationCorresponds to variant rs767083685dbSNPEnsembl.1
Natural variantiVAR_047589436R → W in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs104893621dbSNPEnsembl.1
Natural variantiVAR_047590439R → W in ACHM2; also found in patients with cone-rod dystrophy; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius. 2 PublicationsCorresponds to variant rs749842881dbSNPEnsembl.1
Natural variantiVAR_047591469A → T in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; the left shift in the dose-response relationship of the mutant CNGA3 is less distinctive than in homomeric channels with this mutation indicating a partial rescue effect of the CNGB3 subunit; is in large part located in the cell membrane at 37 and 27 degrees Celsius. 1 PublicationCorresponds to variant rs117522010dbSNPEnsembl.1
Natural variantiVAR_047592471N → S in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is unchanged. 2 PublicationsCorresponds to variant rs373954146dbSNPEnsembl.1
Natural variantiVAR_047593485D → V in ACHM2. 1 Publication1
Natural variantiVAR_047594510C → S in ACHM2. 1 Publication1
Natural variantiVAR_047595513G → E in ACHM2. 1 Publication1
Natural variantiVAR_047596516G → E in ACHM2. 1 Publication1
Natural variantiVAR_047597522I → T in ACHM2. 1 Publication1
Natural variantiVAR_047598525G → D in ACHM2. 1 Publication1
Natural variantiVAR_066860527L → M Found in a patient with Leber congenital amaurosis; unknown pathological significance. 1 Publication1
Natural variantiVAR_010907529V → M in ACHM2; also found in patients with cone-rod dystrophy. 4 PublicationsCorresponds to variant rs104893619dbSNPEnsembl.1
Natural variantiVAR_071448533D → H Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 PublicationCorresponds to variant rs775332304dbSNPEnsembl.1
Natural variantiVAR_071449543 – 545Missing in ACHM2. 1 Publication3
Natural variantiVAR_010908547F → L in ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; is in large part located in the cell membrane at 37 and 27 degrees Celsius. 4 PublicationsCorresponds to variant rs104893617dbSNPEnsembl.1
Natural variantiVAR_047599548G → R in ACHM2. 1 PublicationCorresponds to variant rs781227859dbSNPEnsembl.1
Natural variantiVAR_010909557G → R in ACHM2; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 3.0; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; average cGMP maximum current is decreased to half of the mean wild-type value for the mutant CNGA3 + CNGB3. 3 PublicationsCorresponds to variant rs104893615dbSNPEnsembl.1
Natural variantiVAR_047600563R → H in ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is significantly reduced. 2 PublicationsCorresponds to variant rs552069173dbSNPEnsembl.1
Natural variantiVAR_047601565T → M in ACHM2. 2 PublicationsCorresponds to variant rs201747279dbSNPEnsembl.1
Natural variantiVAR_047602569R → H in ACHM2. 3 PublicationsCorresponds to variant rs201782746dbSNPEnsembl.1
Natural variantiVAR_071450570S → N Probable disease-associated mutation found in patients with cone-rod dystrophy. 1 Publication1
Natural variantiVAR_047603573Y → C in ACHM2. 1 Publication1
Natural variantiVAR_047604590E → K in ACHM2; also found in patients with cone-rod dystrophy; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. 3 PublicationsCorresponds to variant rs763041373dbSNPEnsembl.1
Natural variantiVAR_047605593E → K in ACHM2. 1 PublicationCorresponds to variant rs774676415dbSNPEnsembl.1
Natural variantiVAR_071451646R → H.1 PublicationCorresponds to variant rs141577844dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0570751 – 71MAKIN…GQGIA → METRGLADSGQGSFTGQGIA RFGRIQKKSQPEKVVRAASR GRPLIGWTQWCAEDGGDESE MALAGSPGCSSGPQG in isoform 3. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_042525132 – 150SAWPL…NTEEE → R in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065314 mRNA. Translation: AAC17440.1.
AK131300 mRNA. Translation: BAD18468.1.
AC092675 Genomic DNA. Translation: AAY24181.1.
BC096298 mRNA. Translation: AAH96298.1.
BC096299 mRNA. Translation: AAH96299.1.
BC096300 mRNA. Translation: AAH96300.1.
S76069 Genomic DNA. Translation: AAD14208.1.
CCDSiCCDS2034.1. [Q16281-1]
CCDS42719.1. [Q16281-2]
PIRiI78560.
S74179.
RefSeqiNP_001073347.1. NM_001079878.1. [Q16281-2]
NP_001289.1. NM_001298.2. [Q16281-1]
UniGeneiHs.234785.

Genome annotation databases

EnsembliENST00000272602; ENSP00000272602; ENSG00000144191. [Q16281-1]
ENST00000393504; ENSP00000377140; ENSG00000144191. [Q16281-1]
ENST00000409937; ENSP00000386761; ENSG00000144191. [Q16281-3]
ENST00000436404; ENSP00000410070; ENSG00000144191. [Q16281-2]
GeneIDi1261.
KEGGihsa:1261.
UCSCiuc002syt.4. human. [Q16281-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the CNGA3 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF065314 mRNA. Translation: AAC17440.1.
AK131300 mRNA. Translation: BAD18468.1.
AC092675 Genomic DNA. Translation: AAY24181.1.
BC096298 mRNA. Translation: AAH96298.1.
BC096299 mRNA. Translation: AAH96299.1.
BC096300 mRNA. Translation: AAH96300.1.
S76069 Genomic DNA. Translation: AAD14208.1.
CCDSiCCDS2034.1. [Q16281-1]
CCDS42719.1. [Q16281-2]
PIRiI78560.
S74179.
RefSeqiNP_001073347.1. NM_001079878.1. [Q16281-2]
NP_001289.1. NM_001298.2. [Q16281-1]
UniGeneiHs.234785.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SWYX-ray1.90A/B/C626-669[»]
ProteinModelPortaliQ16281.
SMRiQ16281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107661. 25 interactors.
IntActiQ16281. 1 interactor.
STRINGi9606.ENSP00000272602.

Chemistry databases

GuidetoPHARMACOLOGYi396.

Protein family/group databases

TCDBi1.A.1.5.12. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiQ16281.
PhosphoSitePlusiQ16281.

Polymorphism and mutation databases

BioMutaiCNGA3.
DMDMi13959682.

Proteomic databases

PaxDbiQ16281.
PeptideAtlasiQ16281.
PRIDEiQ16281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272602; ENSP00000272602; ENSG00000144191. [Q16281-1]
ENST00000393504; ENSP00000377140; ENSG00000144191. [Q16281-1]
ENST00000409937; ENSP00000386761; ENSG00000144191. [Q16281-3]
ENST00000436404; ENSP00000410070; ENSG00000144191. [Q16281-2]
GeneIDi1261.
KEGGihsa:1261.
UCSCiuc002syt.4. human. [Q16281-1]

Organism-specific databases

CTDi1261.
DisGeNETi1261.
GeneCardsiCNGA3.
GeneReviewsiCNGA3.
HGNCiHGNC:2150. CNGA3.
MalaCardsiCNGA3.
MIMi216900. phenotype.
600053. gene.
neXtProtiNX_Q16281.
OpenTargetsiENSG00000144191.
Orphaneti49382. Achromatopsia.
1872. Cone rod dystrophy.
PharmGKBiPA26660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0500. Eukaryota.
ENOG410YWWI. LUCA.
GeneTreeiENSGT00760000118772.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiQ16281.
KOiK04950.
OMAiYLWANRK.
OrthoDBiEOG091G03EW.
PhylomeDBiQ16281.
TreeFamiTF319048.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000144191-MONOMER.

Miscellaneous databases

GeneWikiiCyclic_nucleotide-gated_channel_alpha_3.
GenomeRNAii1261.
PROiQ16281.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000144191.
CleanExiHS_CNGA3.
GenevisibleiQ16281. HS.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCNGA3_HUMAN
AccessioniPrimary (citable) accession number: Q16281
Secondary accession number(s): E9PF93
, Q4VAP7, Q53RD2, Q6ZNA7, Q9UP64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 4, 2001
Last modified: November 30, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.