CNGA1_HUMAN
ID CNGA1_HUMAN Reviewed; 686 AA.
AC P29973; A8K7K6; J3KPZ2; Q16279; Q16485; Q4W5E3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=cGMP-gated cation channel alpha-1;
DE AltName: Full=Cyclic nucleotide-gated cation channel 1;
DE AltName: Full=Cyclic nucleotide-gated channel alpha-1;
DE Short=CNG channel alpha-1;
DE Short=CNG-1;
DE Short=CNG1;
DE AltName: Full=Cyclic nucleotide-gated channel, photoreceptor;
DE AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha;
GN Name=CNGA1; Synonyms=CNCG, CNCG1;
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].
RC TISSUE=Retina;
RX PubMed=1372902; DOI=10.1016/s0021-9258(18)42689-0;
RA Pittler S.J., Lee A.K., Altherr M.R., Howard T.A., Seldin M.F.,
RA Hurwitz R.L., Wasmuth J.J., Baehr W.;
RT "Primary structure and chromosomal localization of human and mouse rod
RT photoreceptor cGMP-gated cation channel.";
RL J. Biol. Chem. 267:6257-6262(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-114.
RC TISSUE=Retina;
RX PubMed=1379636; DOI=10.1523/jneurosci.12-08-03248.1992;
RA Dhallan R.S., Macke J.P., Eddy R.L., Shows T.B., Reed R.R., Yau K.-W.,
RA Nathans J.;
RT "Human rod photoreceptor cGMP-gated channel: amino acid sequence, gene
RT structure, and functional expression.";
RL J. Neurosci. 12:3248-3256(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-573.
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 [7]
RP VARIANT RP49 PHE-316, AND VARIANTS GLN-28 AND ASN-114.
RX PubMed=7479749; DOI=10.1073/pnas.92.22.10177;
RA Dryja T.P., Finn J.T., Peng Y.-W., McGee T.L., Berson E.L., Yau K.-W.;
RT "Mutations in the gene encoding the alpha subunit of the rod cGMP-gated
RT channel in autosomal recessive retinitis pigmentosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10177-10181(1995).
RN [8]
RP INVOLVEMENT IN RP49.
RX PubMed=15570217;
RA Zhang Q., Zulfiqar F., Riazuddin S.A., Xiao X., Ahmad Z., Riazuddin S.,
RA Hejtmancik J.F.;
RT "Autosomal recessive retinitis pigmentosa in a Pakistani family mapped to
RT CNGA1 with identification of a novel mutation.";
RL Mol. Vis. 10:884-889(2004).
CC -!- FUNCTION: Subunit of the rod cyclic GMP-gated cation channel, which is
CC involved in the final stage of the phototransduction pathway. When
CC light hits rod photoreceptors, cGMP concentrations decrease causing
CC rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization
CC of the membrane potential. {ECO:0000250|UniProtKB:Q00194}.
CC -!- SUBUNIT: Forms a heterotetramer with CNGB1 in a 3:1 ratio. May also
CC form cyclic nucleotide-activated homotetrameric channels, that are
CC efficiently activated by saturating cGMP, but poorly activated by
CC saturating cAMP compared to the heterotetramer with CNGB1.
CC {ECO:0000250|UniProtKB:Q00194}.
CC -!- INTERACTION:
CC P29973; Q5ICW4: GRB14; Xeno; NbExp=4; IntAct=EBI-8417095, EBI-7639273;
CC P29973; Q9JLM9: Grb14; Xeno; NbExp=2; IntAct=EBI-8417095, EBI-8347358;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00194};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00194}.
CC -!- TISSUE SPECIFICITY: Rod cells in the retina.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of
CC CNGA subunits. {ECO:0000250}.
CC -!- DISEASE: Retinitis pigmentosa 49 (RP49) [MIM:613756]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:15570217,
CC ECO:0000269|PubMed:7479749}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52010.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF84710.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mutations of the CNGA1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/cnga1mut.htm";
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DR EMBL; M84741; AAA52010.1; ALT_INIT; mRNA.
DR EMBL; S42457; AAB22778.1; -; mRNA.
DR EMBL; AK292021; BAF84710.1; ALT_INIT; mRNA.
DR EMBL; AC096749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107068; AAY40919.1; -; Genomic_DNA.
DR EMBL; CH471069; EAW93048.1; -; Genomic_DNA.
DR EMBL; S76062; AAD14206.1; -; Genomic_DNA.
DR CCDS; CCDS43226.1; -.
DR CCDS; CCDS47050.1; -.
DR PIR; A42161; A42161.
DR RefSeq; NP_000078.2; NM_000087.3.
DR RefSeq; NP_001136036.1; NM_001142564.1.
DR RefSeq; XP_016863201.1; XM_017007712.1.
DR PDB; 7LFT; EM; 2.60 A; A/B/C/D=140-686.
DR PDB; 7LFW; EM; 2.90 A; A/B/C/D=140-686.
DR PDB; 7LFX; EM; 3.10 A; A/B/C/D=140-686.
DR PDB; 7LFY; EM; 3.60 A; A/B/C/D=140-686.
DR PDB; 7LG1; EM; 2.70 A; A/B/C/D=140-686.
DR PDB; 7RH9; EM; 2.61 A; A/C/D=140-686.
DR PDB; 7RHG; EM; 2.88 A; A/C/D=140-686.
DR PDB; 7RHH; EM; 3.31 A; A/C/D=140-686.
DR PDB; 7RHI; EM; 3.31 A; A/C/D=140-686.
DR PDB; 7RHJ; EM; 2.88 A; A/C/D=140-686.
DR PDB; 7RHK; EM; 3.27 A; A/C/D=140-686.
DR PDB; 7RHL; EM; 3.03 A; A/C/D=140-686.
DR PDBsum; 7LFT; -.
DR PDBsum; 7LFW; -.
DR PDBsum; 7LFX; -.
DR PDBsum; 7LFY; -.
DR PDBsum; 7LG1; -.
DR PDBsum; 7RH9; -.
DR PDBsum; 7RHG; -.
DR PDBsum; 7RHH; -.
DR PDBsum; 7RHI; -.
DR PDBsum; 7RHJ; -.
DR PDBsum; 7RHK; -.
DR PDBsum; 7RHL; -.
DR AlphaFoldDB; P29973; -.
DR BioGRID; 107659; 39.
DR IntAct; P29973; 2.
DR MINT; P29973; -.
DR STRING; 9606.ENSP00000384264; -.
DR DrugBank; DB04209; Dequalinium.
DR DrugCentral; P29973; -.
DR GuidetoPHARMACOLOGY; 394; -.
DR TCDB; 1.A.1.5.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P29973; 1 site.
DR iPTMnet; P29973; -.
DR PhosphoSitePlus; P29973; -.
DR BioMuta; CNGA1; -.
DR DMDM; 239938910; -.
DR jPOST; P29973; -.
DR MassIVE; P29973; -.
DR PaxDb; P29973; -.
DR PeptideAtlas; P29973; -.
DR PRIDE; P29973; -.
DR Antibodypedia; 23791; 101 antibodies from 24 providers.
DR DNASU; 1259; -.
DR Ensembl; ENST00000402813.9; ENSP00000384264.5; ENSG00000198515.16.
DR Ensembl; ENST00000420489.7; ENSP00000389881.3; ENSG00000198515.16.
DR Ensembl; ENST00000514170.7; ENSP00000426862.3; ENSG00000198515.16.
DR GeneID; 1259; -.
DR KEGG; hsa:1259; -.
DR MANE-Select; ENST00000514170.7; ENSP00000426862.3; NM_001379270.1; NP_001366199.1.
DR UCSC; uc003gxt.5; human.
DR CTD; 1259; -.
DR DisGeNET; 1259; -.
DR GeneCards; CNGA1; -.
DR GeneReviews; CNGA1; -.
DR HGNC; HGNC:2148; CNGA1.
DR HPA; ENSG00000198515; Tissue enriched (retina).
DR MalaCards; CNGA1; -.
DR MIM; 123825; gene.
DR MIM; 613756; phenotype.
DR neXtProt; NX_P29973; -.
DR OpenTargets; ENSG00000198515; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA26658; -.
DR VEuPathDB; HostDB:ENSG00000198515; -.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000156074; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR InParanoid; P29973; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; P29973; -.
DR TreeFam; TF319048; -.
DR PathwayCommons; P29973; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SignaLink; P29973; -.
DR BioGRID-ORCS; 1259; 26 hits in 1064 CRISPR screens.
DR ChiTaRS; CNGA1; human.
DR GeneWiki; Cyclic_nucleotide-gated_channel_alpha_1; -.
DR GenomeRNAi; 1259; -.
DR Pharos; P29973; Tchem.
DR PRO; PR:P29973; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P29973; protein.
DR Bgee; ENSG00000198515; Expressed in lower esophagus mucosa and 119 other tissues.
DR ExpressionAtlas; P29973; baseline and differential.
DR Genevisible; P29973; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR032945; CNGA1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF9; PTHR45638:SF9; 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; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; cGMP; cGMP-binding; Coiled coil;
KW Disease variant; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Retinitis pigmentosa; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..686
FT /note="cGMP-gated cation channel alpha-1"
FT /id="PRO_0000219308"
FT TOPO_DOM 1..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 161..181
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 182..194
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 195..213
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 214..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 236..255
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 256..262
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 263..284
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 285..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 296..322
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 323..365
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 366..397
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 398..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 31..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..356
FT /note="P-helix"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 357..365
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 398..480
FT /note="C-linker"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 481..608
FT /note="Cyclic nucleotide-binding domain (CNBD)"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COILED 619..662
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COMPBIAS 94..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..605
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 542
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 557
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT VARIANT 28
FT /note="R -> Q (in dbSNP:rs76537883)"
FT /evidence="ECO:0000269|PubMed:7479749"
FT /id="VAR_009295"
FT VARIANT 114
FT /note="D -> N (in dbSNP:rs28642966)"
FT /evidence="ECO:0000269|PubMed:1379636,
FT ECO:0000269|PubMed:7479749"
FT /id="VAR_009296"
FT VARIANT 118
FT /note="N -> D (in dbSNP:rs28642966)"
FT /id="VAR_047385"
FT VARIANT 316
FT /note="S -> F (in RP49; dbSNP:rs62625014)"
FT /evidence="ECO:0000269|PubMed:7479749"
FT /id="VAR_009297"
FT CONFLICT 1
FT /note="M -> MKLSM (in Ref. 3; BAF84710 and 1; AAA52010)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> V (in Ref. 3; BAF84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="S -> Y (in Ref. 1; AAA52010)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> I (in Ref. 1; AAA52010)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="EE -> HH (in Ref. 1; AAA52010)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="I -> V (in Ref. 3; BAF84710)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="Y -> T (in Ref. 1; AAA52010)"
FT /evidence="ECO:0000305"
FT CONFLICT 677..678
FT /note="GA -> WS (in Ref. 1; AAA52010)"
FT /evidence="ECO:0000305"
FT HELIX 159..184
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 193..215
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 291..321
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:7LFT"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 368..399
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 401..419
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 424..439
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:7RHH"
FT HELIX 455..472
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:7LG1"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:7LG1"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:7LFT"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:7LFT"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 585..600
FT /evidence="ECO:0007829|PDB:7LFT"
FT HELIX 622..658
FT /evidence="ECO:0007829|PDB:7RHL"
SQ SEQUENCE 686 AA; 79126 MW; E5200D216FC97AF6 CRC64;
MKNNIINTQQ SFVTMPNVIV PDIEKEIRRM ENGACSSFSE DDDSASTSEE SENENPHARG
SFSYKSLRKG GPSQREQYLP GAIALFNVNN SSNKDQEPEE KKKKKKEKKS KSDDKNENKN
DPEKKKKKKD KEKKKKEEKS KDKKEEEKKE VVVIDPSGNT YYNWLFCITL PVMYNWTMVI
ARACFDELQS DYLEYWLILD YVSDIVYLID MFVRTRTGYL EQGLLVKEEL KLINKYKSNL
QFKLDVLSLI PTDLLYFKLG WNYPEIRLNR LLRFSRMFEF FQRTETRTNY PNIFRISNLV
MYIVIIIHWN ACVFYSISKA IGFGNDTWVY PDINDPEFGR LARKYVYSLY WSTLTLTTIG
ETPPPVRDSE YVFVVVDFLI GVLIFATIVG NIGSMISNMN AARAEFQARI DAIKQYMHFR
NVSKDMEKRV IKWFDYLWTN KKTVDEKEVL KYLPDKLRAE IAINVHLDTL KKVRIFADCE
AGLLVELVLK LQPQVYSPGD YICKKGDIGR EMYIIKEGKL AVVADDGVTQ FVVLSDGSYF
GEISILNIKG SKAGNRRTAN IKSIGYSDLF CLSKDDLMEA LTEYPDAKTM LEEKGKQILM
KDGLLDLNIA NAGSDPKDLE EKVTRMEGSV DLLQTRFARI LAEYESMQQK LKQRLTKVEK
FLKPLIDTEF SSIEGPGAES GPIDST
