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Q16281 (CNGA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CNGA3
Synonyms:CNCG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Tetramer formed of three CNGA3 and one CNGB3 modulatory subunits. Ref.5 Ref.6 Ref.7

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Prominently expressed in retina.

Domain

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

Involvement in disease

Achromatopsia 2 (ACHM2) [MIM:216900]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Defects in CNGA3 may be a cause of Leber congenital amaurosis (LCA), a severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. Ref.14

Sequence similarities

Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA3 subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Ontologies

Keywords
   Biological processIon transport
Sensory transduction
Transport
Vision
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Leber congenital amaurosis
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandcGMP
cGMP-binding
Nucleotide-binding
   Molecular functionIon channel
Ligand-gated ion channel
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphototransduction, visible light

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of membrane potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to corticosteroid

Inferred from electronic annotation. Source: Ensembl

response to magnesium ion

Inferred from electronic annotation. Source: Ensembl

retinal cone cell development

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transport

Traceable author statement Ref.1. Source: ProtInc

visual perception

Traceable author statement Ref.8. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

perikaryon

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncGMP binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cAMP activated cation channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cGMP activated cation channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ligand-gated ion channel activity

Traceable author statement Ref.1. Source: ProtInc

voltage-gated potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16281-1)

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.
Isoform 2 (identifier: Q16281-2)

The sequence of this isoform differs from the canonical sequence as follows:
     132-150: SAWPLAKCNTNTSNNTEEE → R
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694Cyclic nucleotide-gated cation channel alpha-3
PRO_0000219317

Regions

Transmembrane171 – 19222Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane378 – 39720Helical; Potential
Nucleotide binding482 – 605124cGMP
Coiled coil626 – 66944

Sites

Binding site5491cGMP Potential
Binding site5641cGMP Potential

Natural variations

Alternative sequence132 – 15019SAWPL…NTEEE → R in isoform 2.
VSP_042525
Natural variant481P → L. Ref.12
Corresponds to variant rs62156348 [ dbSNP | Ensembl ].
VAR_047565
Natural variant1531T → M. Ref.8 Ref.12
Corresponds to variant rs34314205 [ dbSNP | Ensembl ].
VAR_010902
Natural variant1621D → V in ACHM2. Ref.9
VAR_047566
Natural variant1631P → L in ACHM2. Ref.8 Ref.9
VAR_010903
Natural variant1811Y → C in ACHM2. Ref.9
VAR_047567
Natural variant1821N → Y in ACHM2. Ref.9
VAR_047568
Natural variant1861L → F in ACHM2. Ref.9
VAR_047569
Natural variant1911C → Y in ACHM2. Ref.9
VAR_047570
Natural variant1941E → K in ACHM2. Ref.9
VAR_047571
Natural variant1981E → K.
Corresponds to variant rs2271041 [ dbSNP | Ensembl ].
VAR_021963
Natural variant2231R → W in ACHM2. Ref.9 Ref.10 Ref.12
VAR_047572
Natural variant2241T → R in ACHM2. Ref.9
VAR_047573
Natural variant2281E → K in ACHM2; 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 temparature. Ref.13
Corresponds to variant rs147415641 [ dbSNP | Ensembl ].
VAR_047574
Natural variant2491F → S in ACHM2. Ref.12
VAR_047575
Natural variant2601D → N in ACHM2. Ref.9
VAR_047576
Natural variant2631Y → D in ACHM2. Ref.12
VAR_047577
Natural variant2671G → D in ACHM2. Ref.9
VAR_047578
Natural variant2771R → C in ACHM2. Ref.9 Ref.11 Ref.12 Ref.13
VAR_047579
Natural variant2771R → H in ACHM2; does not form functional homomeric or heteromeric channels; cell surface expression levels is significantly reduced. Ref.9
VAR_047580
Natural variant2831R → 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. Ref.8 Ref.9 Ref.13
VAR_010904
Natural variant2831R → W in ACHM2. Ref.8 Ref.9
VAR_010905
Natural variant2911T → 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. Ref.8 Ref.9 Ref.13
VAR_010906
Natural variant3121Missing in ACHM2. Ref.9
VAR_047581
Natural variant3351W → C. Ref.15
VAR_069398
Natural variant3411S → P in ACHM2. Ref.9 Ref.12
VAR_047582
Natural variant3691T → S in ACHM2. Ref.9
VAR_047583
Natural variant3721P → S in ACHM2. Ref.9
VAR_047584
Natural variant3801F → S in ACHM2. Ref.9
VAR_047585
Natural variant4011S → P in ACHM2. Ref.12
VAR_047586
Natural variant4061M → T in ACHM2. Ref.9
VAR_047587
Natural variant4101R → W in ACHM2. Ref.8 Ref.9 Ref.12
VAR_010910
Natural variant4271R → C in ACHM2. Ref.9 Ref.12
Corresponds to variant rs141386891 [ dbSNP | Ensembl ].
VAR_047588
Natural variant4361R → W in ACHM2. Ref.9 Ref.10 Ref.12
VAR_047589
Natural variant4391R → W 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; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; coexpression of the CNGB3 subunit compensate completely for the slightly higher apparent cGMP sensitivity of homomers; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature. Ref.13
VAR_047590
Natural variant4691A → 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. Ref.13
Corresponds to variant rs117522010 [ dbSNP | Ensembl ].
VAR_047591
Natural variant4711N → 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. Ref.9 Ref.11
VAR_047592
Natural variant4851D → V in ACHM2. Ref.9
VAR_047593
Natural variant5101C → S in ACHM2. Ref.9
VAR_047594
Natural variant5131G → E in ACHM2. Ref.9
VAR_047595
Natural variant5161G → E in ACHM2. Ref.9
VAR_047596
Natural variant5221I → T in ACHM2. Ref.9
VAR_047597
Natural variant5251G → D in ACHM2. Ref.9
VAR_047598
Natural variant5271L → M in LCA. Ref.14
VAR_066860
Natural variant5291V → M in ACHM2. Ref.8 Ref.9 Ref.12
VAR_010907
Natural variant5471F → 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. Ref.8 Ref.9 Ref.10 Ref.13
VAR_010908
Natural variant5481G → R in ACHM2. Ref.10
VAR_047599
Natural variant5571G → 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. Ref.8 Ref.9 Ref.13
VAR_010909
Natural variant5631R → 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. Ref.9 Ref.11
VAR_047600
Natural variant5651T → M in ACHM2. Ref.9 Ref.12
VAR_047601
Natural variant5691R → H in ACHM2. Ref.9 Ref.10
VAR_047602
Natural variant5731Y → C in ACHM2. Ref.9
VAR_047603
Natural variant5901E → K in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. Ref.12 Ref.13
VAR_047604
Natural variant5931E → K in ACHM2. Ref.9
VAR_047605

Secondary structure

... 694
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 4, 2001. Version 2.
Checksum: AE00B4EE760D70A0

FASTA69478,838
        10         20         30         40         50         60 
MAKINTQYSH PSRTHLKVKT SDRDLNRAEN GLSRAHSSSE ETSSVLQPGI AMETRGLADS 

        70         80         90        100        110        120 
GQGSFTGQGI ARLSRLIFLL RRWAARHVHH QDQGPDSFPD RFRGAELKEV SSQESNAQAN 

       130        140        150        160        170        180 
VGSQEPADRG RSAWPLAKCN TNTSNNTEEE KKTKKKDAIV VDPSSNLYYR WLTAIALPVF 

       190        200        210        220        230        240 
YNWYLLICRA CFDELQSEYL MLWLVLDYSA DVLYVLDVLV RARTGFLEQG LMVSDTNRLW 

       250        260        270        280        290        300 
QHYKTTTQFK LDVLSLVPTD LAYLKVGTNY PEVRFNRLLK FSRLFEFFDR TETRTNYPNM 

       310        320        330        340        350        360 
FRIGNLVLYI LIIIHWNACI YFAISKFIGF GTDSWVYPNI SIPEHGRLSR KYIYSLYWST 

       370        380        390        400        410        420 
LTLTTIGETP PPVKDEEYLF VVVDFLVGVL IFATIVGNVG SMISNMNASR AEFQAKIDSI 

       430        440        450        460        470        480 
KQYMQFRKVT KDLETRVIRW FDYLWANKKT VDEKEVLKSL PDKLKAEIAI NVHLDTLKKV 

       490        500        510        520        530        540 
RIFQDCEAGL LVELVLKLRP TVFSPGDYIC KKGDIGKEMY IINEGKLAVV ADDGVTQFVV 

       550        560        570        580        590        600 
LSDGSYFGEI SILNIKGSKS GNRRTANIRS IGYSDLFCLS KDDLMEALTE YPEAKKALEE 

       610        620        630        640        650        660 
KGRQILMKDN LIDEELARAG ADPKDLEEKV EQLGSSLDTL QTRFARLLAE YNATQMKMKQ 

       670        680        690 
RLSQLESQVK GGGDKPLADG EVPGDATKTE DKQQ 

« Hide

Isoform 2 [UniParc].

Checksum: C6FB264BE7EB3D8D
Show »

FASTA67676,903

References

« Hide 'large scale' references
[1]"Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors."
Wissinger B., Mueller F., Weyand I., Schuffenhauer S., Thanos S., Kaupp U.B., Zrenner E.
Eur. J. Neurosci. 9:2512-2521(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[4]"Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells."
Distler M., Biel M., Flockerzi V., Hofmann F.
Neuropharmacology 33:1275-1282(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-580.
[5]"Genetic basis of total colourblindness among the Pingelapese islanders."
Sundin O.H., Yang J.-M., Li Y., Zhu D., Hurd J.N., Mitchell T.N., Silva E.D., Maumenee I.H.
Nat. Genet. 25:289-293(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[6]"Subunit configuration of heteromeric cone cyclic nucleotide-gated channels."
Peng C., Rich E.D., Varnum M.D.
Neuron 42:401-410(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[7]"Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels."
Shuart N.G., Haitin Y., Camp S.S., Black K.D., Zagotta W.N.
Nat. Commun. 2:457-457(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 626-669, SUBUNIT STOICHIOMETRY.
[8]"Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel."
Kohl S., Marx T., Giddings I., Jaegle H., Jacobson S.G., Apfelstedt-Sylla E., Zrenner E., Sharpe L.T., Wissinger B.
Nat. Genet. 19:257-259(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACHM2 LEU-163; GLN-283; TRP-283; ARG-291; TRP-410; MET-529; LEU-547 AND ARG-557, VARIANT MET-153.
[9]"CNGA3 mutations in hereditary cone photoreceptor disorders."
Wissinger B., Gamer D., Jaegle H., Giorda R., Marx T., Mayer S., Tippmann S., Broghammer M., Jurklies B., Rosenberg T., Jacobson S.G., Sener E.C., Tatlipinar S., Hoyng C.B., Castellan C., Bitoun P., Andreasson S., Rudolph G. expand/collapse author list , Kellner U., Lorenz B., Wolff G., Verellen-Dumoulin C., Schwartz M., Cremers F.P.M., Apfelstedt-Sylla E., Zrenner E., Salati R., Sharpe L.T., Kohl S.
Am. J. Hum. Genet. 69:722-737(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACHM2 VAL-162; LEU-163; CYS-181; TYR-182; PHE-186; TYR-191; LYS-194; TRP-223; ARG-224; ASN-260; ASP-267; CYS-277; HIS-277; TRP-283; GLN-283; ARG-291; ILE-312 DEL; PRO-341; SER-369; SER-372; SER-380; THR-406; TRP-410; CYS-427; TRP-436; SER-471; VAL-485; SER-510; GLU-513; GLU-516; THR-522; ASP-525; MET-529; LEU-547; ARG-557; HIS-563; MET-565; HIS-569; CYS-573 AND LYS-593.
[10]"Achromatopsia caused by novel mutations in both CNGA3 and CNGB3."
Johnson S., Michaelides M., Aligianis I.A., Ainsworth J.R., Mollon J.D., Maher E.R., Moore A.T., Hunt D.M.
J. Med. Genet. 41:E20-E20(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACHM2 TRP-223; TRP-436; LEU-547; ARG-548 AND HIS-569.
[11]"Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit."
Liu C., Varnum M.D.
Am. J. Physiol. 289:C187-C198(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ACHM2 CYS-277; SER-471 AND HIS-563.
[12]"Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases."
Nishiguchi K.M., Sandberg M.A., Gorji N., Berson E.L., Dryja T.P.
Hum. Mutat. 25:248-258(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACHM2 TRP-223; SER-249; ASP-263; CYS-277; PRO-341; PRO-401; TRP-410; CYS-427; TRP-436; MET-529; MET-565 AND LYS-590, VARIANTS LEU-48 AND MET-153.
[13]"Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia."
Achromatopsia clinical study group
Reuter P., Koeppen K., Ladewig T., Kohl S., Baumann B., Wissinger B.
Hum. Mutat. 29:1228-1236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACHM2 LYS-228; CYS-277; GLN-283; TRP-439; THR-469; LEU-547 AND ARG-557, CHARACTERIZATION OF VARIANTS ACHM2 LYS-228; GLN-283; ARG-291; TRP-439; THR-469; LEU-547; ARG-557 AND LYS-590.
[14]"Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A mutations in patients with Leber congenital amaurosis."
Wang X., Wang H., Cao M., Li Z., Chen X., Patenia C., Gore A., Abboud E.B., Al-Rajhi A.A., Lewis A.R., Lupski J.R., Mardon G., Zhang K., Muzny D., Gibbs R.A., Chen R.
Hum. Mutat. 32:1450-1459(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCA MET-527.
[15]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-335.
+Additional computationally mapped references.

Web resources

Mutations of the CNGA3 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF065314 mRNA. Translation: AAC17440.1.
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.
PIRI78560.
S74179.
RefSeqNP_001073347.1. NM_001079878.1.
NP_001289.1. NM_001298.2.
UniGeneHs.234785.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SWYX-ray1.90A/B/C626-669[»]
ProteinModelPortalQ16281.
SMRQ16281. Positions 351-682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107661. 1 interaction.
IntActQ16281. 1 interaction.
STRING9606.ENSP00000272602.

Chemistry

ChEMBLCHEMBL1628463.
GuidetoPHARMACOLOGY396.

Protein family/group databases

TCDB1.A.1.5.12. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ16281.

Polymorphism databases

DMDM13959682.

Proteomic databases

PaxDbQ16281.
PRIDEQ16281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272602; ENSP00000272602; ENSG00000144191. [Q16281-1]
ENST00000393504; ENSP00000377140; ENSG00000144191. [Q16281-1]
ENST00000436404; ENSP00000410070; ENSG00000144191. [Q16281-2]
GeneID1261.
KEGGhsa:1261.
UCSCuc002syt.3. human. [Q16281-1]
uc002syu.3. human. [Q16281-2]

Organism-specific databases

CTD1261.
GeneCardsGC02P098962.
HGNCHGNC:2150. CNGA3.
MIM216900. phenotype.
600053. gene.
neXtProtNX_Q16281.
Orphanet49382. Achromatopsia.
PharmGKBPA26660.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300025.
HOGENOMHOG000007898.
HOVERGENHBG000281.
KOK04950.
OrthoDBEOG771268.
PhylomeDBQ16281.
TreeFamTF319048.

Gene expression databases

ArrayExpressQ16281.
BgeeQ16281.
CleanExHS_CNGA3.
GenevestigatorQ16281.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
PROSITEPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCyclic_nucleotide-gated_channel_alpha_3.
GenomeRNAi1261.
NextBio5101.
PROQ16281.
SOURCESearch...

Entry information

Entry nameCNGA3_HUMAN
AccessionPrimary (citable) accession number: Q16281
Secondary accession number(s): Q4VAP7, Q53RD2, Q9UP64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 4, 2001
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM