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Cyclic nucleotide-gated cation channel alpha-3 (Cone photoreceptor cGMP-gated channel subunit alpha) (Cyclic nucleotide-gated channel alpha-3) (CNG channel alpha-3) (CNG-3) (CNG3)

 CNGA3_HUMAN             Reviewed;         694 AA.
Q16281; E9PF93; Q4VAP7; Q53RD2; Q6ZNA7; Q9UP64;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
04-MAY-2001, sequence version 2.
22-NOV-2017, entry version 170.
RecName: Full=Cyclic nucleotide-gated cation channel alpha-3;
AltName: Full=Cone photoreceptor cGMP-gated channel subunit alpha;
AltName: Full=Cyclic nucleotide-gated channel alpha-3;
Short=CNG channel alpha-3;
Short=CNG-3;
Short=CNG3;
Name=CNGA3; Synonyms=CNCG3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9517456; DOI=10.1111/j.1460-9568.1997.tb01680.x;
Wissinger B., Mueller F., Weyand I., Schuffenhauer S., Thanos S.,
Kaupp U.B., Zrenner E.;
"Cloning, chromosomal localization and functional expression of the
gene encoding the alpha-subunit of the cGMP-gated channel in human
cone photoreceptors.";
Eur. J. Neurosci. 9:2512-2521(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-580.
PubMed=7532814; DOI=10.1016/0028-3908(94)90027-2;
Distler M., Biel M., Flockerzi V., Hofmann F.;
"Expression of cyclic nucleotide-gated cation channels in non-sensory
tissues and cells.";
Neuropharmacology 33:1275-1282(1994).
[6]
FUNCTION, AND SUBUNIT.
PubMed=10888875; DOI=10.1038/77162;
Sundin O.H., Yang J.-M., Li Y., Zhu D., Hurd J.N., Mitchell T.N.,
Silva E.D., Maumenee I.H.;
"Genetic basis of total colourblindness among the Pingelapese
islanders.";
Nat. Genet. 25:289-293(2000).
[7]
SUBUNIT.
PubMed=15134637; DOI=10.1016/S0896-6273(04)00225-9;
Peng C., Rich E.D., Varnum M.D.;
"Subunit configuration of heteromeric cone cyclic nucleotide-gated
channels.";
Neuron 42:401-410(2004).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 626-669, AND SUBUNIT
STOICHIOMETRY.
PubMed=21878911; DOI=10.1038/ncomms1466;
Shuart N.G., Haitin Y., Camp S.S., Black K.D., Zagotta W.N.;
"Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic
nucleotide-gated ion channels.";
Nat. Commun. 2:457-457(2011).
[9]
VARIANTS ACHM2 LEU-163; GLN-283; TRP-283; ARG-291; TRP-410; MET-529;
LEU-547 AND ARG-557, AND VARIANT MET-153.
PubMed=9662398; DOI=10.1038/935;
Kohl S., Marx T., Giddings I., Jaegle H., Jacobson S.G.,
Apfelstedt-Sylla E., Zrenner E., Sharpe L.T., Wissinger B.;
"Total colourblindness is caused by mutations in the gene encoding the
alpha-subunit of the cone photoreceptor cGMP-gated cation channel.";
Nat. Genet. 19:257-259(1998).
[10]
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.
PubMed=11536077; DOI=10.1086/323613;
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.;
"CNGA3 mutations in hereditary cone photoreceptor disorders.";
Am. J. Hum. Genet. 69:722-737(2001).
[11]
VARIANTS ACHM2 TRP-223; TRP-436; LEU-547; ARG-548 AND HIS-569.
PubMed=14757870; DOI=10.1136/jmg.2003.011437;
Johnson S., Michaelides M., Aligianis I.A., Ainsworth J.R.,
Mollon J.D., Maher E.R., Moore A.T., Hunt D.M.;
"Achromatopsia caused by novel mutations in both CNGA3 and CNGB3.";
J. Med. Genet. 41:E20-E20(2004).
[12]
CHARACTERIZATION OF VARIANTS ACHM2 CYS-277; SER-471 AND HIS-563.
PubMed=15743887; DOI=10.1152/ajpcell.00490.2004;
Liu C., Varnum M.D.;
"Functional consequences of progressive cone dystrophy-associated
mutations in the human cone photoreceptor cyclic nucleotide-gated
channel CNGA3 subunit.";
Am. J. Physiol. 289:C187-C198(2005).
[13]
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, AND VARIANTS
LEU-48 AND MET-153.
PubMed=15712225; DOI=10.1002/humu.20142;
Nishiguchi K.M., Sandberg M.A., Gorji N., Berson E.L., Dryja T.P.;
"Cone cGMP-gated channel mutations and clinical findings in patients
with achromatopsia, macular degeneration, and other hereditary cone
diseases.";
Hum. Mutat. 25:248-258(2005).
[14]
VARIANTS ACHM2 LYS-228; CYS-277; GLN-283; TRP-439; THR-469; LEU-547
AND ARG-557, AND CHARACTERIZATION OF VARIANTS ACHM2 LYS-228; GLN-283;
ARG-291; TRP-439; THR-469; LEU-547; ARG-557 AND LYS-590.
PubMed=18521937; DOI=10.1002/humu.20790;
Achromatopsia clinical study group;
Reuter P., Koeppen K., Ladewig T., Kohl S., Baumann B., Wissinger B.;
"Mutations in CNGA3 impair trafficking or function of cone cyclic
nucleotide-gated channels, resulting in achromatopsia.";
Hum. Mutat. 29:1228-1236(2008).
[15]
VARIANT MET-527.
PubMed=21901789; DOI=10.1002/humu.21587;
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.;
"Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
mutations in patients with Leber congenital amaurosis.";
Hum. Mutat. 32:1450-1459(2011).
[16]
VARIANT CYS-335.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
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.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[17]
VARIANTS ASP-120; LYS-198; ILE-224; MET-247; ARG-258; SER-330;
PHE-334; HIS-533; ASN-570 AND HIS-646, AND VARIANTS ACHM2 CYS-171;
TRP-223; GLN-223; ASN-260; LYS-274; HIS-277; CYS-277; PRO-278;
TRP-283; SER-322; TRP-436; GLN-436; TRP-439; MET-529; 543-ASP--SER-545
DEL AND LYS-590.
PubMed=24903488; DOI=10.1001/jamaophthalmol.2014.1032;
Li S., Huang L., Xiao X., Jia X., Guo X., Zhang Q.;
"Identification of CNGA3 mutations in 46 Families: common cause of
achromatopsia and cone-rod dystrophies in Chinese patients.";
JAMA Ophthalmol. 132:1076-1083(2014).
[18]
VARIANTS ACHM2 ASP-323 AND HIS-569.
PubMed=26493561; DOI=10.1186/s12967-015-0694-7;
Li F.F., Huang X.F., Chen J., Yu X.D., Zheng M.Q., Lu F., Jin Z.B.,
Gan D.K.;
"Identification of novel mutations by targeted exome sequencing and
the genotype-phenotype assessment of patients with achromatopsia.";
J. Transl. Med. 13:334-334(2015).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:10888875}.
-!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
subunits. {ECO:0000269|PubMed:10888875,
ECO:0000269|PubMed:15134637, ECO:0000269|PubMed:21878911}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16281-1; Sequence=Displayed;
Name=2;
IsoId=Q16281-2; Sequence=VSP_042525;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q16281-3; Sequence=VSP_057075;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Prominently expressed in retina.
-!- DOMAIN: The C-terminal coiled-coil domain mediates
homotrimerization of CNGA subunits.
-!- 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.
{ECO:0000269|PubMed:11536077, ECO:0000269|PubMed:14757870,
ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:15743887,
ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:24903488,
ECO:0000269|PubMed:26493561, ECO:0000269|PubMed:9662398}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. CNGA3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Mutations of the CNGA3 gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/cnga3mut.htm";
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EMBL; AF065314; AAC17440.1; -; mRNA.
EMBL; AK131300; BAD18468.1; -; mRNA.
EMBL; AC092675; AAY24181.1; -; Genomic_DNA.
EMBL; BC096298; AAH96298.1; -; mRNA.
EMBL; BC096299; AAH96299.1; -; mRNA.
EMBL; BC096300; AAH96300.1; -; mRNA.
EMBL; S76069; AAD14208.1; -; Genomic_DNA.
CCDS; CCDS2034.1; -. [Q16281-1]
CCDS; CCDS42719.1; -. [Q16281-2]
PIR; I78560; I78560.
PIR; S74179; S74179.
RefSeq; NP_001073347.1; NM_001079878.1. [Q16281-2]
RefSeq; NP_001289.1; NM_001298.2. [Q16281-1]
UniGene; Hs.234785; -.
PDB; 3SWY; X-ray; 1.90 A; A/B/C=626-669.
PDBsum; 3SWY; -.
ProteinModelPortal; Q16281; -.
SMR; Q16281; -.
BioGrid; 107661; 27.
IntAct; Q16281; 1.
STRING; 9606.ENSP00000272602; -.
GuidetoPHARMACOLOGY; 396; -.
TCDB; 1.A.1.5.12; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q16281; -.
PhosphoSitePlus; Q16281; -.
BioMuta; CNGA3; -.
DMDM; 13959682; -.
PaxDb; Q16281; -.
PeptideAtlas; Q16281; -.
PRIDE; Q16281; -.
Ensembl; ENST00000272602; ENSP00000272602; ENSG00000144191. [Q16281-1]
Ensembl; ENST00000393504; ENSP00000377140; ENSG00000144191. [Q16281-1]
Ensembl; ENST00000409937; ENSP00000386761; ENSG00000144191. [Q16281-3]
Ensembl; ENST00000436404; ENSP00000410070; ENSG00000144191. [Q16281-2]
GeneID; 1261; -.
KEGG; hsa:1261; -.
UCSC; uc002syt.4; human. [Q16281-1]
CTD; 1261; -.
DisGeNET; 1261; -.
EuPathDB; HostDB:ENSG00000144191.11; -.
GeneCards; CNGA3; -.
GeneReviews; CNGA3; -.
HGNC; HGNC:2150; CNGA3.
MalaCards; CNGA3; -.
MIM; 216900; phenotype.
MIM; 600053; gene.
neXtProt; NX_Q16281; -.
OpenTargets; ENSG00000144191; -.
Orphanet; 49382; Achromatopsia.
Orphanet; 1872; Cone rod dystrophy.
PharmGKB; PA26660; -.
eggNOG; KOG0500; Eukaryota.
eggNOG; ENOG410YWWI; LUCA.
GeneTree; ENSGT00900000140801; -.
HOGENOM; HOG000007898; -.
HOVERGEN; HBG000281; -.
InParanoid; Q16281; -.
KO; K04950; -.
OMA; YLWANRK; -.
OrthoDB; EOG091G03EW; -.
PhylomeDB; Q16281; -.
TreeFam; TF319048; -.
GeneWiki; Cyclic_nucleotide-gated_channel_alpha_3; -.
GenomeRNAi; 1261; -.
PRO; PR:Q16281; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000144191; -.
CleanEx; HS_CNGA3; -.
Genevisible; Q16281; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
GO; GO:1902495; C:transmembrane transporter complex; IDA:UniProtKB.
GO; GO:0030553; F:cGMP binding; IMP:UniProtKB.
GO; GO:0005223; F:intracellular cGMP activated cation channel activity; IMP:UniProtKB.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:ProtInc.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
GO; GO:0006812; P:cation transport; IMP:UniProtKB.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR032406; CLZ_dom.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF16526; CLZ; 1.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS00889; CNMP_BINDING_2; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; cGMP; cGMP-binding; Coiled coil;
Complete proteome; Disease mutation; Ion channel; Ion transport;
Leber congenital amaurosis; Ligand-gated ion channel; Membrane;
Nucleotide-binding; Polymorphism; Reference proteome;
Sensory transduction; Transmembrane; Transmembrane helix; Transport;
Vision.
CHAIN 1 694 Cyclic nucleotide-gated cation channel
alpha-3.
/FTId=PRO_0000219317.
TOPO_DOM 1 166 Cytoplasmic. {ECO:0000255}.
TRANSMEM 167 187 Helical; Name=H1. {ECO:0000255}.
TOPO_DOM 188 199 Extracellular. {ECO:0000255}.
TRANSMEM 200 220 Helical; Name=H2. {ECO:0000255}.
TOPO_DOM 221 252 Cytoplasmic. {ECO:0000255}.
TRANSMEM 253 273 Helical; Name=H3. {ECO:0000255}.
TOPO_DOM 274 302 Extracellular. {ECO:0000255}.
TRANSMEM 303 323 Helical; Name=H4. {ECO:0000255}.
TOPO_DOM 324 378 Cytoplasmic. {ECO:0000255}.
TRANSMEM 379 399 Helical; Name=H5. {ECO:0000255}.
TOPO_DOM 400 481 Extracellular. {ECO:0000255}.
TRANSMEM 482 502 Helical; Name=H6. {ECO:0000255}.
TOPO_DOM 503 694 Cytoplasmic. {ECO:0000255}.
NP_BIND 482 605 cGMP.
COILED 626 669
BINDING 549 549 cGMP. {ECO:0000255}.
BINDING 564 564 cGMP. {ECO:0000255}.
VAR_SEQ 1 71 MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEE
TSSVLQPGIAMETRGLADSGQGSFTGQGIA -> METRGLA
DSGQGSFTGQGIARFGRIQKKSQPEKVVRAASRGRPLIGWT
QWCAEDGGDESEMALAGSPGCSSGPQG (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_057075.
VAR_SEQ 132 150 SAWPLAKCNTNTSNNTEEE -> R (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042525.
VARIANT 48 48 P -> L (in dbSNP:rs62156348).
{ECO:0000269|PubMed:15712225}.
/FTId=VAR_047565.
VARIANT 120 120 N -> D (in dbSNP:rs199859850).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071435.
VARIANT 153 153 T -> M (in dbSNP:rs34314205).
{ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010902.
VARIANT 162 162 D -> V (in ACHM2; dbSNP:rs747447519).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047566.
VARIANT 163 163 P -> L (in ACHM2; dbSNP:rs104893612).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010903.
VARIANT 171 171 W -> C (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs762773298).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071436.
VARIANT 181 181 Y -> C (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047567.
VARIANT 182 182 N -> Y (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047568.
VARIANT 186 186 L -> F (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047569.
VARIANT 191 191 C -> Y (in ACHM2; dbSNP:rs761554853).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047570.
VARIANT 194 194 E -> K (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047571.
VARIANT 198 198 E -> K (in dbSNP:rs2271041).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_021963.
VARIANT 223 223 R -> Q (in ACHM2; dbSNP:rs762668060).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071438.
VARIANT 223 223 R -> W (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs138958917).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:14757870,
ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047572.
VARIANT 224 224 T -> I (probable disease-associated
mutation found in patients with cone-rod
dystrophy).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071439.
VARIANT 224 224 T -> R (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047573.
VARIANT 228 228 E -> 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;
dbSNP:rs147415641).
{ECO:0000269|PubMed:18521937}.
/FTId=VAR_047574.
VARIANT 247 247 T -> M (in dbSNP:rs148616345).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071440.
VARIANT 249 249 F -> S (in ACHM2).
{ECO:0000269|PubMed:15712225}.
/FTId=VAR_047575.
VARIANT 258 258 P -> R (probable disease-associated
mutation found in patients with cone-rod
dystrophy).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071441.
VARIANT 260 260 D -> N (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs374258471).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047576.
VARIANT 263 263 Y -> D (in ACHM2).
{ECO:0000269|PubMed:15712225}.
/FTId=VAR_047577.
VARIANT 267 267 G -> D (in ACHM2; dbSNP:rs781673067).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047578.
VARIANT 274 274 R -> K (in ACHM2).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071442.
VARIANT 277 277 R -> C (in ACHM2; also found in patients
with cone-rod dystrophy; does not form
functional homomeric or heteromeric
channels; dbSNP:rs104893620).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:15743887,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047579.
VARIANT 277 277 R -> H (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs778114016).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047580.
VARIANT 278 278 L -> P (in ACHM2; dbSNP:rs763421555).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071443.
VARIANT 283 283 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; dbSNP:rs104893614).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010904.
VARIANT 283 283 R -> W (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs104893613).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:24903488,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010905.
VARIANT 291 291 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;
dbSNP:rs104893616).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010906.
VARIANT 312 312 Missing (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047581.
VARIANT 322 322 F -> S (in ACHM2).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071444.
VARIANT 323 323 A -> D (in ACHM2).
{ECO:0000269|PubMed:26493561}.
/FTId=VAR_075493.
VARIANT 330 330 F -> S (probable disease-associated
mutation found in patients with cone-rod
dystrophy).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071445.
VARIANT 334 334 S -> F (probable disease-associated
mutation found in patients with cone-rod
dystrophy).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071446.
VARIANT 335 335 W -> C. {ECO:0000269|PubMed:23033978}.
/FTId=VAR_069398.
VARIANT 341 341 S -> P (in ACHM2).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225}.
/FTId=VAR_047582.
VARIANT 369 369 T -> S (in ACHM2; dbSNP:rs766637612).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047583.
VARIANT 372 372 P -> S (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047584.
VARIANT 380 380 F -> S (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047585.
VARIANT 401 401 S -> P (in ACHM2).
{ECO:0000269|PubMed:15712225}.
/FTId=VAR_047586.
VARIANT 406 406 M -> T (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047587.
VARIANT 410 410 R -> W (in ACHM2; dbSNP:rs137852608).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010910.
VARIANT 427 427 R -> C (in ACHM2; dbSNP:rs141386891).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225}.
/FTId=VAR_047588.
VARIANT 436 436 R -> Q (in ACHM2; dbSNP:rs767083685).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071447.
VARIANT 436 436 R -> W (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs104893621).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:14757870,
ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047589.
VARIANT 439 439 R -> 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; dbSNP:rs749842881).
{ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047590.
VARIANT 469 469 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; dbSNP:rs117522010).
{ECO:0000269|PubMed:18521937}.
/FTId=VAR_047591.
VARIANT 471 471 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;
dbSNP:rs373954146).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15743887}.
/FTId=VAR_047592.
VARIANT 485 485 D -> V (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047593.
VARIANT 510 510 C -> S (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047594.
VARIANT 513 513 G -> E (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047595.
VARIANT 516 516 G -> E (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047596.
VARIANT 522 522 I -> T (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047597.
VARIANT 525 525 G -> D (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047598.
VARIANT 527 527 L -> M (found in a patient with Leber
congenital amaurosis; unknown
pathological significance).
{ECO:0000269|PubMed:21901789}.
/FTId=VAR_066860.
VARIANT 529 529 V -> M (in ACHM2; also found in patients
with cone-rod dystrophy;
dbSNP:rs104893619).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:24903488,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010907.
VARIANT 533 533 D -> H (probable disease-associated
mutation found in patients with cone-rod
dystrophy; dbSNP:rs775332304).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071448.
VARIANT 543 545 Missing (in ACHM2).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071449.
VARIANT 547 547 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; dbSNP:rs104893617).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:14757870,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010908.
VARIANT 548 548 G -> R (in ACHM2; dbSNP:rs781227859).
{ECO:0000269|PubMed:14757870}.
/FTId=VAR_047599.
VARIANT 557 557 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;
dbSNP:rs104893615).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:9662398}.
/FTId=VAR_010909.
VARIANT 563 563 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;
dbSNP:rs552069173).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15743887}.
/FTId=VAR_047600.
VARIANT 565 565 T -> M (in ACHM2; dbSNP:rs201747279).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:15712225}.
/FTId=VAR_047601.
VARIANT 569 569 R -> H (in ACHM2; dbSNP:rs201782746).
{ECO:0000269|PubMed:11536077,
ECO:0000269|PubMed:14757870,
ECO:0000269|PubMed:26493561}.
/FTId=VAR_047602.
VARIANT 570 570 S -> N (probable disease-associated
mutation found in patients with cone-rod
dystrophy).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071450.
VARIANT 573 573 Y -> C (in ACHM2).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047603.
VARIANT 590 590 E -> 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; dbSNP:rs763041373).
{ECO:0000269|PubMed:15712225,
ECO:0000269|PubMed:18521937,
ECO:0000269|PubMed:24903488}.
/FTId=VAR_047604.
VARIANT 593 593 E -> K (in ACHM2; dbSNP:rs774676415).
{ECO:0000269|PubMed:11536077}.
/FTId=VAR_047605.
VARIANT 646 646 R -> H (in dbSNP:rs141577844).
{ECO:0000269|PubMed:24903488}.
/FTId=VAR_071451.
HELIX 626 668 {ECO:0000244|PDB:3SWY}.
SEQUENCE 694 AA; 78838 MW; AE00B4EE760D70A0 CRC64;
MAKINTQYSH PSRTHLKVKT SDRDLNRAEN GLSRAHSSSE ETSSVLQPGI AMETRGLADS
GQGSFTGQGI ARLSRLIFLL RRWAARHVHH QDQGPDSFPD RFRGAELKEV SSQESNAQAN
VGSQEPADRG RSAWPLAKCN TNTSNNTEEE KKTKKKDAIV VDPSSNLYYR WLTAIALPVF
YNWYLLICRA CFDELQSEYL MLWLVLDYSA DVLYVLDVLV RARTGFLEQG LMVSDTNRLW
QHYKTTTQFK LDVLSLVPTD LAYLKVGTNY PEVRFNRLLK FSRLFEFFDR TETRTNYPNM
FRIGNLVLYI LIIIHWNACI YFAISKFIGF GTDSWVYPNI SIPEHGRLSR KYIYSLYWST
LTLTTIGETP PPVKDEEYLF VVVDFLVGVL IFATIVGNVG SMISNMNASR AEFQAKIDSI
KQYMQFRKVT KDLETRVIRW FDYLWANKKT VDEKEVLKSL PDKLKAEIAI NVHLDTLKKV
RIFQDCEAGL LVELVLKLRP TVFSPGDYIC KKGDIGKEMY IINEGKLAVV ADDGVTQFVV
LSDGSYFGEI SILNIKGSKS GNRRTANIRS IGYSDLFCLS KDDLMEALTE YPEAKKALEE
KGRQILMKDN LIDEELARAG ADPKDLEEKV EQLGSSLDTL QTRFARLLAE YNATQMKMKQ
RLSQLESQVK GGGDKPLADG EVPGDATKTE DKQQ


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