ID CNGA3_HUMAN Reviewed; 694 AA. AC Q16281; E9PF93; Q4VAP7; Q53RD2; Q6ZNA7; Q9UP64; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Cyclic nucleotide-gated cation channel alpha-3; DE AltName: Full=Cone photoreceptor cGMP-gated channel subunit alpha; DE AltName: Full=Cyclic nucleotide-gated channel alpha-3; DE Short=CNG channel alpha-3; DE Short=CNG-3; DE Short=CNG3; GN Name=CNGA3; Synonyms=CNCG3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9517456; DOI=10.1111/j.1460-9568.1997.tb01680.x; RA Wissinger B., Mueller F., Weyand I., Schuffenhauer S., Thanos S., RA Kaupp U.B., Zrenner E.; RT "Cloning, chromosomal localization and functional expression of the gene RT encoding the alpha-subunit of the cGMP-gated channel in human cone RT photoreceptors."; RL Eur. J. Neurosci. 9:2512-2521(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-580. RX PubMed=7532814; DOI=10.1016/0028-3908(94)90027-2; RA Distler M., Biel M., Flockerzi V., Hofmann F.; RT "Expression of cyclic nucleotide-gated cation channels in non-sensory RT tissues and cells."; RL Neuropharmacology 33:1275-1282(1994). RN [6] RP FUNCTION, AND SUBUNIT. RX PubMed=10888875; DOI=10.1038/77162; RA Sundin O.H., Yang J.-M., Li Y., Zhu D., Hurd J.N., Mitchell T.N., RA Silva E.D., Maumenee I.H.; RT "Genetic basis of total colourblindness among the Pingelapese islanders."; RL Nat. Genet. 25:289-293(2000). RN [7] RP SUBUNIT. RX PubMed=15134637; DOI=10.1016/s0896-6273(04)00225-9; RA Peng C., Rich E.D., Varnum M.D.; RT "Subunit configuration of heteromeric cone cyclic nucleotide-gated RT channels."; RL Neuron 42:401-410(2004). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 626-669, AND SUBUNIT RP STOICHIOMETRY. RX PubMed=21878911; DOI=10.1038/ncomms1466; RA Shuart N.G., Haitin Y., Camp S.S., Black K.D., Zagotta W.N.; RT "Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic RT nucleotide-gated ion channels."; RL Nat. Commun. 2:457-457(2011). RN [9] RP VARIANTS ACHM2 LEU-163; GLN-283; TRP-283; ARG-291; TRP-410; MET-529; RP LEU-547 AND ARG-557, AND VARIANT MET-153. RX PubMed=9662398; DOI=10.1038/935; RA Kohl S., Marx T., Giddings I., Jaegle H., Jacobson S.G., RA Apfelstedt-Sylla E., Zrenner E., Sharpe L.T., Wissinger B.; RT "Total colourblindness is caused by mutations in the gene encoding the RT alpha-subunit of the cone photoreceptor cGMP-gated cation channel."; RL Nat. Genet. 19:257-259(1998). RN [10] RP VARIANTS ACHM2 VAL-162; LEU-163; CYS-181; TYR-182; PHE-186; TYR-191; RP LYS-194; TRP-223; ARG-224; ASN-260; ASP-267; CYS-277; HIS-277; TRP-283; RP GLN-283; ARG-291; ILE-312 DEL; PRO-341; SER-369; SER-372; SER-380; THR-406; RP TRP-410; CYS-427; TRP-436; SER-471; VAL-485; SER-510; GLU-513; GLU-516; RP THR-522; ASP-525; MET-529; LEU-547; ARG-557; HIS-563; MET-565; HIS-569; RP CYS-573 AND LYS-593. RX PubMed=11536077; DOI=10.1086/323613; RA Wissinger B., Gamer D., Jaegle H., Giorda R., Marx T., Mayer S., RA Tippmann S., Broghammer M., Jurklies B., Rosenberg T., Jacobson S.G., RA Sener E.C., Tatlipinar S., Hoyng C.B., Castellan C., Bitoun P., RA Andreasson S., Rudolph G., Kellner U., Lorenz B., Wolff G., RA Verellen-Dumoulin C., Schwartz M., Cremers F.P.M., Apfelstedt-Sylla E., RA Zrenner E., Salati R., Sharpe L.T., Kohl S.; RT "CNGA3 mutations in hereditary cone photoreceptor disorders."; RL Am. J. Hum. Genet. 69:722-737(2001). RN [11] RP VARIANTS ACHM2 TRP-223; TRP-436; LEU-547; ARG-548 AND HIS-569. RX PubMed=14757870; DOI=10.1136/jmg.2003.011437; RA Johnson S., Michaelides M., Aligianis I.A., Ainsworth J.R., Mollon J.D., RA Maher E.R., Moore A.T., Hunt D.M.; RT "Achromatopsia caused by novel mutations in both CNGA3 and CNGB3."; RL J. Med. Genet. 41:E20-E20(2004). RN [12] RP CHARACTERIZATION OF VARIANTS ACHM2 CYS-277; SER-471 AND HIS-563. RX PubMed=15743887; DOI=10.1152/ajpcell.00490.2004; RA Liu C., Varnum M.D.; RT "Functional consequences of progressive cone dystrophy-associated mutations RT in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 RT subunit."; RL Am. J. Physiol. 289:C187-C198(2005). RN [13] RP VARIANTS ACHM2 TRP-223; SER-249; ASP-263; CYS-277; PRO-341; PRO-401; RP TRP-410; CYS-427; TRP-436; MET-529; MET-565 AND LYS-590, AND VARIANTS RP LEU-48 AND MET-153. RX PubMed=15712225; DOI=10.1002/humu.20142; RA Nishiguchi K.M., Sandberg M.A., Gorji N., Berson E.L., Dryja T.P.; RT "Cone cGMP-gated channel mutations and clinical findings in patients with RT achromatopsia, macular degeneration, and other hereditary cone diseases."; RL Hum. Mutat. 25:248-258(2005). RN [14] RP VARIANTS ACHM2 LYS-228; CYS-277; GLN-283; TRP-439; THR-469; LEU-547 AND RP ARG-557, AND CHARACTERIZATION OF VARIANTS ACHM2 LYS-228; GLN-283; ARG-291; RP TRP-439; THR-469; LEU-547; ARG-557 AND LYS-590. RX PubMed=18521937; DOI=10.1002/humu.20790; RG Achromatopsia clinical study group; RA Reuter P., Koeppen K., Ladewig T., Kohl S., Baumann B., Wissinger B.; RT "Mutations in CNGA3 impair trafficking or function of cone cyclic RT nucleotide-gated channels, resulting in achromatopsia."; RL Hum. Mutat. 29:1228-1236(2008). RN [15] RP VARIANT MET-527. RX PubMed=21901789; DOI=10.1002/humu.21587; RA Wang X., Wang H., Cao M., Li Z., Chen X., Patenia C., Gore A., Abboud E.B., RA Al-Rajhi A.A., Lewis A.R., Lupski J.R., Mardon G., Zhang K., Muzny D., RA Gibbs R.A., Chen R.; RT "Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A mutations RT in patients with Leber congenital amaurosis."; RL Hum. Mutat. 32:1450-1459(2011). RN [16] RP VARIANT CYS-335. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). RN [17] RP VARIANTS ASP-120; LYS-198; ILE-224; MET-247; ARG-258; SER-330; PHE-334; RP HIS-533; ASN-570 AND HIS-646, AND VARIANTS ACHM2 CYS-171; TRP-223; GLN-223; RP ASN-260; LYS-274; HIS-277; CYS-277; PRO-278; TRP-283; SER-322; TRP-436; RP GLN-436; TRP-439; MET-529; 543-ASP--SER-545 DEL AND LYS-590. RX PubMed=24903488; DOI=10.1001/jamaophthalmol.2014.1032; RA Li S., Huang L., Xiao X., Jia X., Guo X., Zhang Q.; RT "Identification of CNGA3 mutations in 46 Families: common cause of RT achromatopsia and cone-rod dystrophies in Chinese patients."; RL JAMA Ophthalmol. 132:1076-1083(2014). RN [18] RP VARIANTS ACHM2 ASP-323 AND HIS-569. RX PubMed=26493561; DOI=10.1186/s12967-015-0694-7; RA Li F.F., Huang X.F., Chen J., Yu X.D., Zheng M.Q., Lu F., Jin Z.B., RA Gan D.K.; RT "Identification of novel mutations by targeted exome sequencing and the RT genotype-phenotype assessment of patients with achromatopsia."; RL J. Transl. Med. 13:334-334(2015). CC -!- FUNCTION: Visual signal transduction is mediated by a G-protein coupled CC cascade using cGMP as second messenger. This protein can be activated CC by cyclic GMP which leads to an opening of the cation channel and CC thereby causing a depolarization of cone photoreceptors. Induced a CC flickering channel gating, weakened the outward rectification in the CC presence of extracellular calcium, increased sensitivity for L-cis CC diltiazem and enhanced the cAMP efficacy of the channel when CC coexpressed with CNGB3 (By similarity). Essential for the generation of CC light-evoked electrical responses in the red-, green- and blue CC sensitive cones. {ECO:0000250, ECO:0000269|PubMed:10888875}. CC -!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory CC subunits. {ECO:0000269|PubMed:10888875, ECO:0000269|PubMed:15134637, CC ECO:0000269|PubMed:21878911}. CC -!- INTERACTION: CC Q16281; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-1642108, EBI-1104552; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q16281-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16281-2; Sequence=VSP_042525; CC Name=3; CC IsoId=Q16281-3; Sequence=VSP_057075; CC -!- TISSUE SPECIFICITY: Prominently expressed in retina. CC -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of CC CNGA subunits. CC -!- DISEASE: Achromatopsia 2 (ACHM2) [MIM:216900]: An autosomal recessive, CC ocular stationary disorder due to the absence of functioning cone CC photoreceptors in the retina. It is characterized by total CC colorblindness, low visual acuity, photophobia and nystagmus. CC {ECO:0000269|PubMed:11536077, ECO:0000269|PubMed:14757870, CC ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:15743887, CC ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:24903488, CC ECO:0000269|PubMed:26493561, ECO:0000269|PubMed:9662398}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel CC (TC 1.A.1.5) family. CNGA3 subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the CNGA3 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/cnga3mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF065314; AAC17440.1; -; mRNA. DR EMBL; AK131300; BAD18468.1; -; mRNA. DR EMBL; AC092675; AAY24181.1; -; Genomic_DNA. DR EMBL; BC096298; AAH96298.1; -; mRNA. DR EMBL; BC096299; AAH96299.1; -; mRNA. DR EMBL; BC096300; AAH96300.1; -; mRNA. DR EMBL; S76069; AAD14208.1; -; Genomic_DNA. DR CCDS; CCDS2034.1; -. [Q16281-1] DR CCDS; CCDS42719.1; -. [Q16281-2] DR PIR; I78560; I78560. DR PIR; S74179; S74179. DR RefSeq; NP_001073347.1; NM_001079878.1. [Q16281-2] DR RefSeq; NP_001289.1; NM_001298.2. [Q16281-1] DR PDB; 3SWY; X-ray; 1.90 A; A/B/C=626-669. DR PDB; 7RHS; EM; 2.93 A; A/B/C=1-694. DR PDB; 8ETP; EM; 3.52 A; A/B/C=1-694. DR PDB; 8EU3; EM; 3.62 A; A/B/C=1-694. DR PDB; 8EUC; EM; 3.61 A; A/B/C=1-694. DR PDB; 8EV8; EM; 3.11 A; A/B/C=151-694. DR PDB; 8EV9; EM; 3.33 A; A/B/C=151-694. DR PDB; 8EVA; EM; 3.33 A; A/B/C=151-694. DR PDB; 8EVB; EM; 3.60 A; A/B/C=151-694. DR PDB; 8EVC; EM; 3.33 A; A/B/C=151-694. DR PDBsum; 3SWY; -. DR PDBsum; 7RHS; -. DR PDBsum; 8ETP; -. DR PDBsum; 8EU3; -. DR PDBsum; 8EUC; -. DR PDBsum; 8EV8; -. DR PDBsum; 8EV9; -. DR PDBsum; 8EVA; -. DR PDBsum; 8EVB; -. DR PDBsum; 8EVC; -. DR AlphaFoldDB; Q16281; -. DR EMDB; EMD-24468; -. DR EMDB; EMD-28595; -. DR EMDB; EMD-28603; -. DR EMDB; EMD-28611; -. DR EMDB; EMD-28622; -. DR EMDB; EMD-28623; -. DR EMDB; EMD-28624; -. DR EMDB; EMD-28625; -. DR EMDB; EMD-28626; -. DR SMR; Q16281; -. DR BioGRID; 107661; 34. DR IntAct; Q16281; 27. DR STRING; 9606.ENSP00000272602; -. DR GuidetoPHARMACOLOGY; 396; -. DR TCDB; 1.A.1.5.12; the voltage-gated ion channel (vic) superfamily. DR iPTMnet; Q16281; -. DR PhosphoSitePlus; Q16281; -. DR BioMuta; CNGA3; -. DR DMDM; 13959682; -. DR MassIVE; Q16281; -. DR PaxDb; 9606-ENSP00000377140; -. DR PeptideAtlas; Q16281; -. DR ProteomicsDB; 20054; -. DR ProteomicsDB; 60848; -. [Q16281-1] DR ProteomicsDB; 60849; -. [Q16281-2] DR Antibodypedia; 47515; 152 antibodies from 22 providers. DR DNASU; 1261; -. DR Ensembl; ENST00000272602.7; ENSP00000272602.2; ENSG00000144191.12. [Q16281-1] DR Ensembl; ENST00000436404.6; ENSP00000410070.2; ENSG00000144191.12. [Q16281-2] DR GeneID; 1261; -. DR KEGG; hsa:1261; -. DR MANE-Select; ENST00000272602.7; ENSP00000272602.2; NM_001298.3; NP_001289.1. DR UCSC; uc002syt.4; human. [Q16281-1] DR AGR; HGNC:2150; -. DR CTD; 1261; -. DR DisGeNET; 1261; -. DR GeneCards; CNGA3; -. DR GeneReviews; CNGA3; -. DR HGNC; HGNC:2150; CNGA3. DR HPA; ENSG00000144191; Tissue enhanced (choroid plexus, intestine, pituitary gland, retina). DR MalaCards; CNGA3; -. DR MIM; 216900; phenotype. DR MIM; 600053; gene. DR neXtProt; NX_Q16281; -. DR OpenTargets; ENSG00000144191; -. DR Orphanet; 49382; Achromatopsia. DR Orphanet; 1872; Cone rod dystrophy. DR PharmGKB; PA26660; -. DR VEuPathDB; HostDB:ENSG00000144191; -. DR eggNOG; KOG0500; Eukaryota. DR GeneTree; ENSGT00940000158737; -. DR HOGENOM; CLU_005746_12_0_1; -. DR InParanoid; Q16281; -. DR OMA; LTHFPAM; -. DR OrthoDB; 74296at2759; -. DR PhylomeDB; Q16281; -. DR TreeFam; TF319048; -. DR PathwayCommons; Q16281; -. DR SignaLink; Q16281; -. DR BioGRID-ORCS; 1261; 16 hits in 1146 CRISPR screens. DR GeneWiki; Cyclic_nucleotide-gated_channel_alpha_3; -. DR GenomeRNAi; 1261; -. DR Pharos; Q16281; Tchem. DR PRO; PR:Q16281; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q16281; Protein. DR Bgee; ENSG00000144191; Expressed in ventricular zone and 85 other cell types or tissues. DR GO; GO:0043194; C:axon initial segment; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl. DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:1902495; C:transmembrane transporter complex; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl. DR GO; GO:0030553; F:cGMP binding; IMP:UniProtKB. DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central. DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IMP:UniProtKB. DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; TAS:ProtInc. DR GO; GO:0017022; F:myosin binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central. DR GO; GO:0098659; P:inorganic cation import across plasma membrane; IEA:Ensembl. DR GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central. DR GO; GO:0006812; P:monoatomic cation transport; IMP:UniProtKB. DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl. DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd00038; CAP_ED; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.5.300; -; 1. DR Gene3D; 1.10.287.630; Helix hairpin bin; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR InterPro; IPR032406; CLZ_dom. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR45638:SF6; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL ALPHA-3; 1. DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1. DR Pfam; PF16526; CLZ; 1. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF00520; Ion_trans; 1. DR SMART; SM00100; cNMP; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR Genevisible; Q16281; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; cGMP; cGMP-binding; Coiled coil; KW Disease variant; Ion channel; Ion transport; Leber congenital amaurosis; KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome; KW Sensory transduction; Transmembrane; Transmembrane helix; Transport; KW Vision. FT CHAIN 1..694 FT /note="Cyclic nucleotide-gated cation channel alpha-3" FT /id="PRO_0000219317" FT TOPO_DOM 1..166 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 167..187 FT /note="Helical; Name=H1" FT /evidence="ECO:0000255" FT TOPO_DOM 188..199 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 200..220 FT /note="Helical; Name=H2" FT /evidence="ECO:0000255" FT TOPO_DOM 221..252 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 253..273 FT /note="Helical; Name=H3" FT /evidence="ECO:0000255" FT TOPO_DOM 274..302 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical; Name=H4" FT /evidence="ECO:0000255" FT TOPO_DOM 324..378 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 379..399 FT /note="Helical; Name=H5" FT /evidence="ECO:0000255" FT TOPO_DOM 400..481 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 482..502 FT /note="Helical; Name=H6" FT /evidence="ECO:0000255" FT TOPO_DOM 503..694 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 109..152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 662..694 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 626..669 FT COMPBIAS 109..125 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 482..605 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT BINDING 549 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000255" FT BINDING 564 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000255" FT VAR_SEQ 1..71 FT /note="MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAM FT ETRGLADSGQGSFTGQGIA -> METRGLADSGQGSFTGQGIARFGRIQKKSQPEKVVR FT AASRGRPLIGWTQWCAEDGGDESEMALAGSPGCSSGPQG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057075" FT VAR_SEQ 132..150 FT /note="SAWPLAKCNTNTSNNTEEE -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042525" FT VARIANT 48 FT /note="P -> L (in dbSNP:rs62156348)" FT /evidence="ECO:0000269|PubMed:15712225" FT /id="VAR_047565" FT VARIANT 120 FT /note="N -> D (in dbSNP:rs199859850)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071435" FT VARIANT 153 FT /note="T -> M (in dbSNP:rs34314205)" FT /evidence="ECO:0000269|PubMed:15712225, FT ECO:0000269|PubMed:9662398" FT /id="VAR_010902" FT VARIANT 162 FT /note="D -> V (in ACHM2; dbSNP:rs747447519)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047566" FT VARIANT 163 FT /note="P -> L (in ACHM2; dbSNP:rs104893612)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:9662398" FT /id="VAR_010903" FT VARIANT 171 FT /note="W -> C (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs762773298)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071436" FT VARIANT 181 FT /note="Y -> C (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047567" FT VARIANT 182 FT /note="N -> Y (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047568" FT VARIANT 186 FT /note="L -> F (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047569" FT VARIANT 191 FT /note="C -> Y (in ACHM2; dbSNP:rs761554853)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047570" FT VARIANT 194 FT /note="E -> K (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047571" FT VARIANT 198 FT /note="E -> K (in dbSNP:rs2271041)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_021963" FT VARIANT 223 FT /note="R -> Q (in ACHM2; dbSNP:rs762668060)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071438" FT VARIANT 223 FT /note="R -> W (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs138958917)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:15712225, FT ECO:0000269|PubMed:24903488" FT /id="VAR_047572" FT VARIANT 224 FT /note="T -> I (found in patients with cone-rod dystrophy; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071439" FT VARIANT 224 FT /note="T -> R (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047573" FT VARIANT 228 FT /note="E -> K (in ACHM2; uncertain significance; the FT dose-response relationship for cGMP-activation is not FT significantly different from that of wild-type CNGA3; the FT dose-response relationship of the mutant CNGA3 + CNGB3 is FT similar to that of the wild-type protein; the channel FT density into the cell membrane is considerably improved by FT decreasing the cultivation temperature; dbSNP:rs147415641)" FT /evidence="ECO:0000269|PubMed:18521937" FT /id="VAR_047574" FT VARIANT 247 FT /note="T -> M (in dbSNP:rs148616345)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071440" FT VARIANT 249 FT /note="F -> S (in ACHM2)" FT /evidence="ECO:0000269|PubMed:15712225" FT /id="VAR_047575" FT VARIANT 258 FT /note="P -> R (found in patients with cone-rod dystrophy; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071441" FT VARIANT 260 FT /note="D -> N (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs374258471)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:24903488" FT /id="VAR_047576" FT VARIANT 263 FT /note="Y -> D (in ACHM2; dbSNP:rs943314733)" FT /evidence="ECO:0000269|PubMed:15712225" FT /id="VAR_047577" FT VARIANT 267 FT /note="G -> D (in ACHM2; dbSNP:rs781673067)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047578" FT VARIANT 274 FT /note="R -> K (in ACHM2)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071442" FT VARIANT 277 FT /note="R -> C (in ACHM2; also found in patients with FT cone-rod dystrophy; does not form functional homomeric or FT heteromeric channels; dbSNP:rs104893620)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:15743887, FT ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:24903488" FT /id="VAR_047579" FT VARIANT 277 FT /note="R -> H (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs778114016)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:24903488" FT /id="VAR_047580" FT VARIANT 278 FT /note="L -> P (in ACHM2; dbSNP:rs763421555)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071443" FT VARIANT 283 FT /note="R -> Q (in ACHM2; does not reveal any detectable FT calcium influx upon agonist application at 37 degrees FT Celsius; the channel function could be restored by FT incubating the transfected cells at 27 degrees Celsius; the FT dose-response relationship for cGMP-activation is not FT significantly different from that of wild-type CNGA3; the FT dose-response relationship of the mutant CNGA3 + CNGB3 is FT similar to that of the wild-type protein; a substantial FT reduction of macroscopic cGMP maximum current to only FT one-third of the mean value for wild-type CNGA3 + CNGB3 is FT observed for the mutant CNGA3 + CNGB3; the channel density FT into the cell membrane is considerably improved by FT decreasing the cultivation temperature; dbSNP:rs104893614)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:9662398" FT /id="VAR_010904" FT VARIANT 283 FT /note="R -> W (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs104893613)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:24903488, ECO:0000269|PubMed:9662398" FT /id="VAR_010905" FT VARIANT 291 FT /note="T -> R (in ACHM2; does not reveal any detectable FT calcium influx upon agonist application at 37 degrees FT Celsius; the channel function could be restored by FT incubating the transfected cells at 27 degrees Celsius; the FT K(1/2) value is shifted toward a higher cGMP concentration FT by a factor of 1.8; no positive influence of the CNGB3 FT subunit in the cGMP sensitivity is observed; a substantial FT reduction of macroscopic cGMP maximum current to only FT one-third of the mean value for wild-type CNGA3 + CNGB3 is FT observed for the mutant CNGA3 + CNGB3; the channel density FT into the cell membrane is considerably improved by FT decreasing the cultivation temperature; dbSNP:rs104893616)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:9662398" FT /id="VAR_010906" FT VARIANT 312 FT /note="Missing (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047581" FT VARIANT 322 FT /note="F -> S (in ACHM2)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071444" FT VARIANT 323 FT /note="A -> D (in ACHM2)" FT /evidence="ECO:0000269|PubMed:26493561" FT /id="VAR_075493" FT VARIANT 330 FT /note="F -> S (found in patients with cone-rod dystrophy; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071445" FT VARIANT 334 FT /note="S -> F (found in patients with cone-rod dystrophy; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071446" FT VARIANT 335 FT /note="W -> C" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_069398" FT VARIANT 341 FT /note="S -> P (in ACHM2; dbSNP:rs1227761587)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225" FT /id="VAR_047582" FT VARIANT 369 FT /note="T -> S (in ACHM2; dbSNP:rs766637612)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047583" FT VARIANT 372 FT /note="P -> S (in ACHM2; dbSNP:rs1464167194)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047584" FT VARIANT 380 FT /note="F -> S (in ACHM2; dbSNP:rs1692911763)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047585" FT VARIANT 401 FT /note="S -> P (in ACHM2; dbSNP:rs916035276)" FT /evidence="ECO:0000269|PubMed:15712225" FT /id="VAR_047586" FT VARIANT 406 FT /note="M -> T (in ACHM2; dbSNP:rs1553450734)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047587" FT VARIANT 410 FT /note="R -> W (in ACHM2; dbSNP:rs137852608)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:9662398" FT /id="VAR_010910" FT VARIANT 427 FT /note="R -> C (in ACHM2; dbSNP:rs141386891)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225" FT /id="VAR_047588" FT VARIANT 436 FT /note="R -> Q (in ACHM2; dbSNP:rs767083685)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071447" FT VARIANT 436 FT /note="R -> W (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs104893621)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:15712225, FT ECO:0000269|PubMed:24903488" FT /id="VAR_047589" FT VARIANT 439 FT /note="R -> W (in ACHM2; also found in patients with FT cone-rod dystrophy; does not reveal any detectable calcium FT influx upon agonist application at 37 degrees Celsius; FT dbSNP:rs749842881)" FT /evidence="ECO:0000269|PubMed:18521937, FT ECO:0000269|PubMed:24903488" FT /id="VAR_047590" FT VARIANT 469 FT /note="A -> T (in ACHM2; the dose-response relationship for FT cGMP-activation is shifted toward a lower cGMP FT concentration; the left shift in the dose-response FT relationship of the mutant CNGA3 is less distinctive than FT in homomeric channels with this mutation indicating a FT partial rescue effect of the CNGB3 subunit; is in large FT part located in the cell membrane at 37 and 27 degrees FT Celsius; dbSNP:rs117522010)" FT /evidence="ECO:0000269|PubMed:18521937" FT /id="VAR_047591" FT VARIANT 471 FT /note="N -> S (in ACHM2; mutant CNGA3 alone or together FT with the CNGB3 subunit exhibit an increase in apparent FT affinity for cGMP and an increase in the relative agonist FT efficacy of cAMP compared with cGMP; cell surface FT expression levels is unchanged; dbSNP:rs373954146)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15743887" FT /id="VAR_047592" FT VARIANT 485 FT /note="D -> V (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047593" FT VARIANT 510 FT /note="C -> S (in ACHM2; dbSNP:rs908111816)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047594" FT VARIANT 513 FT /note="G -> E (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047595" FT VARIANT 516 FT /note="G -> E (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047596" FT VARIANT 522 FT /note="I -> T (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047597" FT VARIANT 525 FT /note="G -> D (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047598" FT VARIANT 527 FT /note="L -> M (found in a patient with Leber congenital FT amaurosis; uncertain significance)" FT /evidence="ECO:0000269|PubMed:21901789" FT /id="VAR_066860" FT VARIANT 529 FT /note="V -> M (in ACHM2; also found in patients with FT cone-rod dystrophy; dbSNP:rs104893619)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225, ECO:0000269|PubMed:24903488, FT ECO:0000269|PubMed:9662398" FT /id="VAR_010907" FT VARIANT 533 FT /note="D -> H (found in patients with cone-rod dystrophy; FT likely pathogenic; dbSNP:rs775332304)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071448" FT VARIANT 543..545 FT /note="Missing (in ACHM2)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071449" FT VARIANT 547 FT /note="F -> L (in ACHM2; does not reveal any detectable FT calcium influx upon agonist application at 37 degrees FT Celsius; the channel function could be restored by FT incubating the transfected cells at 27 degrees Celsius; the FT dose-response relationship for cGMP-activation is shifted FT toward a lower cGMP concentration; a substantial reduction FT of macroscopic cGMP maximum current to only one-third of FT the mean value for wild-type CNGA3 + CNGB3 is observed for FT the mutant CNGA3 + CNGB3; is in large part located in the FT cell membrane at 37 and 27 degrees Celsius; FT dbSNP:rs104893617)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:18521937, FT ECO:0000269|PubMed:9662398" FT /id="VAR_010908" FT VARIANT 548 FT /note="G -> R (in ACHM2; dbSNP:rs781227859)" FT /evidence="ECO:0000269|PubMed:14757870" FT /id="VAR_047599" FT VARIANT 557 FT /note="G -> R (in ACHM2; the K(1/2) value is shifted toward FT a higher cGMP concentration by a factor of 3.0; no positive FT influence of the CNGB3 subunit in the cGMP sensitivity is FT observed; average cGMP maximum current is decreased to half FT of the mean wild-type value for the mutant CNGA3 + CNGB3; FT dbSNP:rs104893615)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:9662398" FT /id="VAR_010909" FT VARIANT 563 FT /note="R -> H (in ACHM2; mutant CNGA3 alone or together FT with the CNGB3 subunit exhibit an increase in apparent FT affinity for cGMP and an increase in the relative agonist FT efficacy of cAMP compared with cGMP; cell surface FT expression levels is significantly reduced; FT dbSNP:rs552069173)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15743887" FT /id="VAR_047600" FT VARIANT 565 FT /note="T -> M (in ACHM2; dbSNP:rs201747279)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:15712225" FT /id="VAR_047601" FT VARIANT 569 FT /note="R -> H (in ACHM2; dbSNP:rs201782746)" FT /evidence="ECO:0000269|PubMed:11536077, FT ECO:0000269|PubMed:14757870, ECO:0000269|PubMed:26493561" FT /id="VAR_047602" FT VARIANT 570 FT /note="S -> N (found in patients with cone-rod dystrophy; FT likely pathogenic)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071450" FT VARIANT 573 FT /note="Y -> C (in ACHM2)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047603" FT VARIANT 590 FT /note="E -> K (in ACHM2; also found in patients with FT cone-rod dystrophy; the dose-response relationship for FT cGMP-activation is shifted toward a lower cGMP FT concentration; dbSNP:rs763041373)" FT /evidence="ECO:0000269|PubMed:15712225, FT ECO:0000269|PubMed:18521937, ECO:0000269|PubMed:24903488" FT /id="VAR_047604" FT VARIANT 593 FT /note="E -> K (in ACHM2; dbSNP:rs774676415)" FT /evidence="ECO:0000269|PubMed:11536077" FT /id="VAR_047605" FT VARIANT 646 FT /note="R -> H (in dbSNP:rs141577844)" FT /evidence="ECO:0000269|PubMed:24903488" FT /id="VAR_071451" FT HELIX 167..192 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 200..221 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 236..244 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 247..255 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 271..279 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 281..294 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 298..328 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:7RHS" FT TURN 343..346 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 348..363 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 375..406 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 408..426 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 431..446 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 453..456 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 458..460 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 462..470 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 480..485 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 488..496 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 499..503 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 518..524 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 527..530 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 538..541 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 549..553 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 566..572 FT /evidence="ECO:0007829|PDB:7RHS" FT STRAND 574..580 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 581..587 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 592..609 FT /evidence="ECO:0007829|PDB:7RHS" FT HELIX 626..668 FT /evidence="ECO:0007829|PDB:3SWY" SQ 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 //