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Q16281

- CNGA3_HUMAN

UniProt

Q16281 - CNGA3_HUMAN

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Protein
Cyclic nucleotide-gated cation channel alpha-3
Gene
CNGA3, CNCG3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei549 – 5491cGMP Reviewed prediction
Binding sitei564 – 5641cGMP Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi482 – 605124cGMP
Add
BLAST

GO - Molecular functioni

  1. cGMP binding Source: UniProt
  2. intracellular cAMP activated cation channel activity Source: RefGenome
  3. intracellular cGMP activated cation channel activity Source: UniProt
  4. ligand-gated ion channel activity Source: ProtInc
  5. voltage-gated potassium channel activity Source: RefGenome

GO - Biological processi

  1. cation transport Source: UniProt
  2. phototransduction, visible light Source: RefGenome
  3. potassium ion transmembrane transport Source: RefGenome
  4. regulation of membrane potential Source: RefGenome
  5. response to cAMP Source: Ensembl
  6. response to corticosteroid Source: Ensembl
  7. response to magnesium ion Source: Ensembl
  8. retinal cone cell development Source: Ensembl
  9. signal transduction Source: ProtInc
  10. transport Source: ProtInc
  11. 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

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2150. CNGA3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei171 – 19222Helical; Reviewed prediction
Add
BLAST
Transmembranei305 – 32521Helical; Reviewed prediction
Add
BLAST
Transmembranei378 – 39720Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. dendrite Source: Ensembl
  3. integral component of plasma membrane Source: RefGenome
  4. perikaryon Source: Ensembl
  5. photoreceptor outer segment membrane Source: Ensembl
  6. transmembrane transporter complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621D → V in ACHM2. 1 Publication
VAR_047566
Natural varianti163 – 1631P → L in ACHM2. 2 Publications
VAR_010903
Natural varianti181 – 1811Y → C in ACHM2. 1 Publication
VAR_047567
Natural varianti182 – 1821N → Y in ACHM2. 1 Publication
VAR_047568
Natural varianti186 – 1861L → F in ACHM2. 1 Publication
VAR_047569
Natural varianti191 – 1911C → Y in ACHM2. 1 Publication
VAR_047570
Natural varianti194 – 1941E → K in ACHM2. 1 Publication
VAR_047571
Natural varianti223 – 2231R → W in ACHM2. 3 Publications
VAR_047572
Natural varianti224 – 2241T → R in ACHM2. 1 Publication
VAR_047573
Natural varianti228 – 2281E → 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. 1 Publication
Corresponds to variant rs147415641 [ dbSNP | Ensembl ].
VAR_047574
Natural varianti249 – 2491F → S in ACHM2. 1 Publication
VAR_047575
Natural varianti260 – 2601D → N in ACHM2. 1 Publication
VAR_047576
Natural varianti263 – 2631Y → D in ACHM2. 1 Publication
VAR_047577
Natural varianti267 – 2671G → D in ACHM2. 1 Publication
VAR_047578
Natural varianti277 – 2771R → C in ACHM2. 4 Publications
VAR_047579
Natural varianti277 – 2771R → H in ACHM2; does not form functional homomeric or heteromeric channels; cell surface expression levels is significantly reduced. 1 Publication
VAR_047580
Natural varianti283 – 2831R → 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 Publications
VAR_010904
Natural varianti283 – 2831R → W in ACHM2. 2 Publications
VAR_010905
Natural varianti291 – 2911T → 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 Publications
VAR_010906
Natural varianti312 – 3121Missing in ACHM2. 1 Publication
VAR_047581
Natural varianti341 – 3411S → P in ACHM2. 2 Publications
VAR_047582
Natural varianti369 – 3691T → S in ACHM2. 1 Publication
VAR_047583
Natural varianti372 – 3721P → S in ACHM2. 1 Publication
VAR_047584
Natural varianti380 – 3801F → S in ACHM2. 1 Publication
VAR_047585
Natural varianti401 – 4011S → P in ACHM2. 1 Publication
VAR_047586
Natural varianti406 – 4061M → T in ACHM2. 1 Publication
VAR_047587
Natural varianti410 – 4101R → W in ACHM2. 3 Publications
VAR_010910
Natural varianti427 – 4271R → C in ACHM2. 2 Publications
Corresponds to variant rs141386891 [ dbSNP | Ensembl ].
VAR_047588
Natural varianti436 – 4361R → W in ACHM2. 3 Publications
VAR_047589
Natural varianti439 – 4391R → 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. 1 Publication
VAR_047590
Natural varianti469 – 4691A → 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 Publication
Corresponds to variant rs117522010 [ dbSNP | Ensembl ].
VAR_047591
Natural varianti471 – 4711N → 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 Publications
VAR_047592
Natural varianti485 – 4851D → V in ACHM2. 1 Publication
VAR_047593
Natural varianti510 – 5101C → S in ACHM2. 1 Publication
VAR_047594
Natural varianti513 – 5131G → E in ACHM2. 1 Publication
VAR_047595
Natural varianti516 – 5161G → E in ACHM2. 1 Publication
VAR_047596
Natural varianti522 – 5221I → T in ACHM2. 1 Publication
VAR_047597
Natural varianti525 – 5251G → D in ACHM2. 1 Publication
VAR_047598
Natural varianti529 – 5291V → M in ACHM2. 3 Publications
VAR_010907
Natural varianti547 – 5471F → 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 Publications
VAR_010908
Natural varianti548 – 5481G → R in ACHM2. 1 Publication
VAR_047599
Natural varianti557 – 5571G → 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 Publications
VAR_010909
Natural varianti563 – 5631R → 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 Publications
VAR_047600
Natural varianti565 – 5651T → M in ACHM2. 2 Publications
VAR_047601
Natural varianti569 – 5691R → H in ACHM2. 2 Publications
VAR_047602
Natural varianti573 – 5731Y → C in ACHM2. 1 Publication
VAR_047603
Natural varianti590 – 5901E → K in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. 2 Publications
VAR_047604
Natural varianti593 – 5931E → K in ACHM2. 1 Publication
VAR_047605
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.1 Publication

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis

Organism-specific databases

MIMi216900. phenotype.
Orphaneti49382. Achromatopsia.
PharmGKBiPA26660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 694694Cyclic nucleotide-gated cation channel alpha-3
PRO_0000219317Add
BLAST

Proteomic databases

PaxDbiQ16281.
PRIDEiQ16281.

PTM databases

PhosphoSiteiQ16281.

Expressioni

Tissue specificityi

Prominently expressed in retina.

Gene expression databases

ArrayExpressiQ16281.
BgeeiQ16281.
CleanExiHS_CNGA3.
GenevestigatoriQ16281.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107661. 1 interaction.
IntActiQ16281. 1 interaction.
STRINGi9606.ENSP00000272602.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi626 – 66843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SWYX-ray1.90A/B/C626-669[»]
ProteinModelPortaliQ16281.
SMRiQ16281. Positions 351-669.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili626 – 66944
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300025.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
KOiK04950.
OrthoDBiEOG771268.
PhylomeDBiQ16281.
TreeFamiTF319048.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MAKINTQYSH PSRTHLKVKT SDRDLNRAEN GLSRAHSSSE ETSSVLQPGI    50
AMETRGLADS GQGSFTGQGI ARLSRLIFLL RRWAARHVHH QDQGPDSFPD 100
RFRGAELKEV SSQESNAQAN VGSQEPADRG RSAWPLAKCN TNTSNNTEEE 150
KKTKKKDAIV VDPSSNLYYR WLTAIALPVF YNWYLLICRA CFDELQSEYL 200
MLWLVLDYSA DVLYVLDVLV RARTGFLEQG LMVSDTNRLW QHYKTTTQFK 250
LDVLSLVPTD LAYLKVGTNY PEVRFNRLLK FSRLFEFFDR TETRTNYPNM 300
FRIGNLVLYI LIIIHWNACI YFAISKFIGF GTDSWVYPNI SIPEHGRLSR 350
KYIYSLYWST LTLTTIGETP PPVKDEEYLF VVVDFLVGVL IFATIVGNVG 400
SMISNMNASR AEFQAKIDSI KQYMQFRKVT KDLETRVIRW FDYLWANKKT 450
VDEKEVLKSL PDKLKAEIAI NVHLDTLKKV RIFQDCEAGL LVELVLKLRP 500
TVFSPGDYIC KKGDIGKEMY IINEGKLAVV ADDGVTQFVV LSDGSYFGEI 550
SILNIKGSKS GNRRTANIRS IGYSDLFCLS KDDLMEALTE YPEAKKALEE 600
KGRQILMKDN LIDEELARAG ADPKDLEEKV EQLGSSLDTL QTRFARLLAE 650
YNATQMKMKQ RLSQLESQVK GGGDKPLADG EVPGDATKTE DKQQ 694
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481P → L.1 Publication
Corresponds to variant rs62156348 [ dbSNP | Ensembl ].
VAR_047565
Natural varianti153 – 1531T → M.2 Publications
Corresponds to variant rs34314205 [ dbSNP | Ensembl ].
VAR_010902
Natural varianti162 – 1621D → V in ACHM2. 1 Publication
VAR_047566
Natural varianti163 – 1631P → L in ACHM2. 2 Publications
VAR_010903
Natural varianti181 – 1811Y → C in ACHM2. 1 Publication
VAR_047567
Natural varianti182 – 1821N → Y in ACHM2. 1 Publication
VAR_047568
Natural varianti186 – 1861L → F in ACHM2. 1 Publication
VAR_047569
Natural varianti191 – 1911C → Y in ACHM2. 1 Publication
VAR_047570
Natural varianti194 – 1941E → K in ACHM2. 1 Publication
VAR_047571
Natural varianti198 – 1981E → K.
Corresponds to variant rs2271041 [ dbSNP | Ensembl ].
VAR_021963
Natural varianti223 – 2231R → W in ACHM2. 3 Publications
VAR_047572
Natural varianti224 – 2241T → R in ACHM2. 1 Publication
VAR_047573
Natural varianti228 – 2281E → 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. 1 Publication
Corresponds to variant rs147415641 [ dbSNP | Ensembl ].
VAR_047574
Natural varianti249 – 2491F → S in ACHM2. 1 Publication
VAR_047575
Natural varianti260 – 2601D → N in ACHM2. 1 Publication
VAR_047576
Natural varianti263 – 2631Y → D in ACHM2. 1 Publication
VAR_047577
Natural varianti267 – 2671G → D in ACHM2. 1 Publication
VAR_047578
Natural varianti277 – 2771R → C in ACHM2. 4 Publications
VAR_047579
Natural varianti277 – 2771R → H in ACHM2; does not form functional homomeric or heteromeric channels; cell surface expression levels is significantly reduced. 1 Publication
VAR_047580
Natural varianti283 – 2831R → 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 Publications
VAR_010904
Natural varianti283 – 2831R → W in ACHM2. 2 Publications
VAR_010905
Natural varianti291 – 2911T → 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 Publications
VAR_010906
Natural varianti312 – 3121Missing in ACHM2. 1 Publication
VAR_047581
Natural varianti335 – 3351W → C.1 Publication
VAR_069398
Natural varianti341 – 3411S → P in ACHM2. 2 Publications
VAR_047582
Natural varianti369 – 3691T → S in ACHM2. 1 Publication
VAR_047583
Natural varianti372 – 3721P → S in ACHM2. 1 Publication
VAR_047584
Natural varianti380 – 3801F → S in ACHM2. 1 Publication
VAR_047585
Natural varianti401 – 4011S → P in ACHM2. 1 Publication
VAR_047586
Natural varianti406 – 4061M → T in ACHM2. 1 Publication
VAR_047587
Natural varianti410 – 4101R → W in ACHM2. 3 Publications
VAR_010910
Natural varianti427 – 4271R → C in ACHM2. 2 Publications
Corresponds to variant rs141386891 [ dbSNP | Ensembl ].
VAR_047588
Natural varianti436 – 4361R → W in ACHM2. 3 Publications
VAR_047589
Natural varianti439 – 4391R → 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. 1 Publication
VAR_047590
Natural varianti469 – 4691A → 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 Publication
Corresponds to variant rs117522010 [ dbSNP | Ensembl ].
VAR_047591
Natural varianti471 – 4711N → 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 Publications
VAR_047592
Natural varianti485 – 4851D → V in ACHM2. 1 Publication
VAR_047593
Natural varianti510 – 5101C → S in ACHM2. 1 Publication
VAR_047594
Natural varianti513 – 5131G → E in ACHM2. 1 Publication
VAR_047595
Natural varianti516 – 5161G → E in ACHM2. 1 Publication
VAR_047596
Natural varianti522 – 5221I → T in ACHM2. 1 Publication
VAR_047597
Natural varianti525 – 5251G → D in ACHM2. 1 Publication
VAR_047598
Natural varianti527 – 5271L → M in LCA. 1 Publication
VAR_066860
Natural varianti529 – 5291V → M in ACHM2. 3 Publications
VAR_010907
Natural varianti547 – 5471F → 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 Publications
VAR_010908
Natural varianti548 – 5481G → R in ACHM2. 1 Publication
VAR_047599
Natural varianti557 – 5571G → 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 Publications
VAR_010909
Natural varianti563 – 5631R → 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 Publications
VAR_047600
Natural varianti565 – 5651T → M in ACHM2. 2 Publications
VAR_047601
Natural varianti569 – 5691R → H in ACHM2. 2 Publications
VAR_047602
Natural varianti573 – 5731Y → C in ACHM2. 1 Publication
VAR_047603
Natural varianti590 – 5901E → K in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. 2 Publications
VAR_047604
Natural varianti593 – 5931E → K in ACHM2. 1 Publication
VAR_047605

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei132 – 15019SAWPL…NTEEE → R in isoform 2.
VSP_042525Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
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]
ENST00000436404; ENSP00000410070; ENSG00000144191. [Q16281-2]
GeneIDi1261.
KEGGihsa:1261.
UCSCiuc002syt.3. human. [Q16281-1]
uc002syu.3. human. [Q16281-2]

Polymorphism databases

DMDMi13959682.

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:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2034.1. [Q16281-1 ]
CCDS42719.1. [Q16281-2 ]
PIRi I78560.
S74179.
RefSeqi NP_001073347.1. NM_001079878.1. [Q16281-2 ]
NP_001289.1. NM_001298.2. [Q16281-1 ]
UniGenei Hs.234785.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SWY X-ray 1.90 A/B/C 626-669 [» ]
ProteinModelPortali Q16281.
SMRi Q16281. Positions 351-669.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107661. 1 interaction.
IntActi Q16281. 1 interaction.
STRINGi 9606.ENSP00000272602.

Chemistry

ChEMBLi CHEMBL1628463.
GuidetoPHARMACOLOGYi 396.

Protein family/group databases

TCDBi 1.A.1.5.12. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei Q16281.

Polymorphism databases

DMDMi 13959682.

Proteomic databases

PaxDbi Q16281.
PRIDEi Q16281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000272602 ; ENSP00000272602 ; ENSG00000144191 . [Q16281-1 ]
ENST00000393504 ; ENSP00000377140 ; ENSG00000144191 . [Q16281-1 ]
ENST00000436404 ; ENSP00000410070 ; ENSG00000144191 . [Q16281-2 ]
GeneIDi 1261.
KEGGi hsa:1261.
UCSCi uc002syt.3. human. [Q16281-1 ]
uc002syu.3. human. [Q16281-2 ]

Organism-specific databases

CTDi 1261.
GeneCardsi GC02P098962.
GeneReviewsi CNGA3.
HGNCi HGNC:2150. CNGA3.
MIMi 216900. phenotype.
600053. gene.
neXtProti NX_Q16281.
Orphaneti 49382. Achromatopsia.
PharmGKBi PA26660.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300025.
HOGENOMi HOG000007898.
HOVERGENi HBG000281.
KOi K04950.
OrthoDBi EOG771268.
PhylomeDBi Q16281.
TreeFami TF319048.

Miscellaneous databases

GeneWikii Cyclic_nucleotide-gated_channel_alpha_3.
GenomeRNAii 1261.
NextBioi 5101.
PROi Q16281.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16281.
Bgeei Q16281.
CleanExi HS_CNGA3.
Genevestigatori Q16281.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
InterProi IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view ]
Pfami PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
SMARTi SM00100. cNMP. 1 hit.
[Graphical view ]
SUPFAMi SSF51206. SSF51206. 1 hit.
PROSITEi PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANT CYS-335.

Entry informationi

Entry nameiCNGA3_HUMAN
AccessioniPrimary (citable) accession number: Q16281
Secondary accession number(s): Q4VAP7, Q53RD2, Q9UP64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 4, 2001
Last modified: July 9, 2014
This is version 137 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

External Data

Dasty 3

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