Q16281 (CNGA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CNGA3
Synonyms:	CNCG3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	694 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ion transport Sensory transduction Transport Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Leber congenital amaurosis
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Nucleotide-binding cGMP cGMP-binding
Molecular function	Ion channel Ligand-gated ion channel
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	retinal cone cell development Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.1. Source: ProtInc visual perception Traceable author statement Ref.8. Source: ProtInc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor outer segment Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	cGMP binding Inferred from electronic annotation. Source: UniProtKB-KW intracellular cyclic nucleotide activated cation channel activity Inferred from electronic annotation. Source: Compara ligand-gated ion channel activity Traceable author statement Ref.1. Source: ProtInc
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 694

694

Cyclic nucleotide-gated cation channel alpha-3

PRO_0000219317

Regions

Transmembrane

171 – 192

22

Helical; Potential

Transmembrane

305 – 325

21

Helical; Potential

Transmembrane

378 – 397

20

Helical; Potential

Nucleotide binding

482 – 605

124

cGMP

Coiled coil

626 – 669

44

Sites

Binding site

549

1

cGMP Potential

Binding site

564

1

cGMP Potential

Natural variations

Alternative sequence

132 – 150

19

SAWPL…NTEEE → R in isoform 2.

VSP_042525

Natural variant

48

1

P → L. Ref.12

VAR_047565

Natural variant

153

1

T → M. Ref.8 Ref.12
Corresponds to variant rs34314205 [ dbSNP | Ensembl ].

VAR_010902

Natural variant

162

1

D → V in ACHM2. Ref.9

VAR_047566

Natural variant

163

1

P → L in ACHM2. Ref.8 Ref.9

VAR_010903

Natural variant

181

1

Y → C in ACHM2. Ref.9

VAR_047567

Natural variant

182

1

N → Y in ACHM2. Ref.9

VAR_047568

Natural variant

186

1

L → F in ACHM2. Ref.9

VAR_047569

Natural variant

191

1

C → Y in ACHM2. Ref.9

VAR_047570

Natural variant

194

1

E → K in ACHM2. Ref.9

VAR_047571

Natural variant

198

1

E → K.
Corresponds to variant rs2271041 [ dbSNP | Ensembl ].

VAR_021963

Natural variant

223

1

R → W in ACHM2. Ref.9 Ref.10 Ref.12

VAR_047572

Natural variant

224

1

T → R in ACHM2. Ref.9

VAR_047573

Natural variant

228

1

E → 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

VAR_047574

Natural variant

249

1

F → S in ACHM2. Ref.12

VAR_047575

Natural variant

260

1

D → N in ACHM2. Ref.9

VAR_047576

Natural variant

263

1

Y → D in ACHM2. Ref.12

VAR_047577

Natural variant

267

1

G → D in ACHM2. Ref.9

VAR_047578

Natural variant

277

1

R → C in ACHM2. Ref.9 Ref.11 Ref.12 Ref.13

VAR_047579

Natural variant

277

1

R → H in ACHM2; does not form functional homomeric or heteromeric channels; cell surface expression levels is significantly reduced. Ref.9

VAR_047580

Natural variant

283

1

R → 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 variant

283

1

R → W in ACHM2. Ref.8 Ref.9

VAR_010905

Natural variant

291

1

T → 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 variant

312

1

Missing in ACHM2. Ref.9

VAR_047581

Natural variant

341

1

S → P in ACHM2. Ref.9 Ref.12

VAR_047582

Natural variant

369

1

T → S in ACHM2. Ref.9

VAR_047583

Natural variant

372

1

P → S in ACHM2. Ref.9

VAR_047584

Natural variant

380

1

F → S in ACHM2. Ref.9

VAR_047585

Natural variant

401

1

S → P in ACHM2. Ref.12

VAR_047586

Natural variant

406

1

M → T in ACHM2. Ref.9

VAR_047587

Natural variant

410

1

R → W in ACHM2. Ref.8 Ref.9 Ref.12

VAR_010910

Natural variant

427

1

R → C in ACHM2. Ref.9 Ref.12

VAR_047588

Natural variant

436

1

R → W in ACHM2. Ref.9 Ref.10 Ref.12

VAR_047589

Natural variant

439

1

R → 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 variant

469

1

A → 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

VAR_047591

Natural variant

471

1

N → 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 variant

485

1

D → V in ACHM2. Ref.9

VAR_047593

Natural variant

510

1

C → S in ACHM2. Ref.9

VAR_047594

Natural variant

513

1

G → E in ACHM2. Ref.9

VAR_047595

Natural variant

516

1

G → E in ACHM2. Ref.9

VAR_047596

Natural variant

522

1

I → T in ACHM2. Ref.9

VAR_047597

Natural variant

525

1

G → D in ACHM2. Ref.9

VAR_047598

Natural variant

527

1

L → M in LCA. Ref.14

VAR_066860

Natural variant

529

1

V → M in ACHM2. Ref.8 Ref.9 Ref.12

VAR_010907

Natural variant

547

1

F → 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 variant

548

1

G → R in ACHM2. Ref.10

VAR_047599

Natural variant

557

1

G → 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 variant

563

1

R → 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 variant

565

1

T → M in ACHM2. Ref.9 Ref.12

VAR_047601

Natural variant

569

1

R → H in ACHM2. Ref.9 Ref.10

VAR_047602

Natural variant

573

1

Y → C in ACHM2. Ref.9

VAR_047603

Natural variant

590

1

E → K in ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration. Ref.12 Ref.13

VAR_047604

Natural variant

593

1

E → K in ACHM2. Ref.9

VAR_047605

Secondary structure

1

.

.

.

694

Helix Strand Turn

Details...

Helix

626 – 668

43

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 4, 2001. Version 2. Checksum: AE00B4EE760D70A0	FASTA	694	78,838
	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
	Isoform 2 [UniParc]. Checksum: C6FB264BE7EB3D8D	FASTA	676	76,903
	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 RRKKTKKKDA IVVDPSSNLY YRWLTAIALP VFYNWYLLIC RACFDELQSE 190 200 210 220 230 240 YLMLWLVLDY SADVLYVLDV LVRARTGFLE QGLMVSDTNR LWQHYKTTTQ FKLDVLSLVP 250 260 270 280 290 300 TDLAYLKVGT NYPEVRFNRL LKFSRLFEFF DRTETRTNYP NMFRIGNLVL YILIIIHWNA 310 320 330 340 350 360 CIYFAISKFI GFGTDSWVYP NISIPEHGRL SRKYIYSLYW STLTLTTIGE TPPPVKDEEY 370 380 390 400 410 420 LFVVVDFLVG VLIFATIVGN VGSMISNMNA SRAEFQAKID SIKQYMQFRK VTKDLETRVI 430 440 450 460 470 480 RWFDYLWANK KTVDEKEVLK SLPDKLKAEI AINVHLDTLK KVRIFQDCEA GLLVELVLKL 490 500 510 520 530 540 RPTVFSPGDY ICKKGDIGKE MYIINEGKLA VVADDGVTQF VVLSDGSYFG EISILNIKGS 550 560 570 580 590 600 KSGNRRTANI RSIGYSDLFC LSKDDLMEAL TEYPEAKKAL EEKGRQILMK DNLIDEELAR 610 620 630 640 650 660 AGADPKDLEE KVEQLGSSLD TLQTRFARLL AEYNATQMKM KQRLSQLESQ VKGGGDKPLA 670 DGEVPGDATK TEDKQQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	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.

IPI

IPI00000812.
IPI00816511.

PIR

I78560.
S74179.

RefSeq

NP_001073347.1. NM_001079878.1.
NP_001289.1. NM_001298.2.

UniGene

Hs.234785.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SWY	X-ray	1.90	A/B/C	626-669	[»]

ProteinModelPortal

Q16281.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16281. 1 interaction.

STRING

9606.ENSP00000272602.

PTM databases

PhosphoSite

Q16281.

Polymorphism databases

DMDM

13959682.

Proteomic databases

PaxDb

Q16281.

PRIDE

Q16281.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000272602; ENSP00000272602; ENSG00000144191.
ENST00000393504; ENSP00000377140; ENSG00000144191.
ENST00000436404; ENSP00000410070; ENSG00000144191.

GeneID

1261.

KEGG

hsa:1261.

UCSC

uc002syt.3. human.

Organism-specific databases

CTD

1261.

GeneCards

GC02P098962.

HGNC

HGNC:2150. CNGA3.

MIM

216900. phenotype.
600053. gene.

neXtProt

NX_Q16281.

Orphanet

49382. Achromatopsia.
65. Leber congenital amaurosis.

PharmGKB

PA26660.

GenAtlas

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Phylogenomic databases

eggNOG

NOG300025.

HOGENOM

HOG000007898.

HOVERGEN

HBG000281.

KO

K04950.

PhylomeDB

Q16281.

Enzyme and pathway databases

Pathway_Interaction_DB

cone_pathway. Visual signal transduction: Cones.

Gene expression databases

ArrayExpress

Q16281.

Bgee

Q16281.

CleanEx

HS_CNGA3.

Genevestigator

Q16281.

GermOnline

ENSG00000144191. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.10. 1 hit.

InterPro

IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]

Pfam

PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]

SMART

SM00100. cNMP. 1 hit.
[Graphical view]

SUPFAM

SSF51206. cNMP_binding. 1 hit.

PROSITE

PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL1628463.

GenomeRNAi

1261.

NextBio

5101.

SOURCE

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Entry information

Entry name

CNGA3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.