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cGMP-gated cation channel alpha-1 (Cyclic nucleotide-gated cation channel 1) (Cyclic nucleotide-gated channel alpha-1) (CNG channel alpha-1) (CNG-1) (CNG1) (Cyclic nucleotide-gated channel, photoreceptor) (Rod photoreceptor cGMP-gated channel subunit alpha)

 CNGA1_BOVIN             Reviewed;         690 AA.
Q00194;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=cGMP-gated cation channel alpha-1;
AltName: Full=Cyclic nucleotide-gated cation channel 1;
AltName: Full=Cyclic nucleotide-gated channel alpha-1;
Short=CNG channel alpha-1;
Short=CNG-1;
Short=CNG1;
AltName: Full=Cyclic nucleotide-gated channel, photoreceptor;
AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha;
Name=CNGA1; Synonyms=CNCG, CNCG1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Retinal rod cell;
PubMed=2481236; DOI=10.1038/342762a0;
Kaupp U.B., Niidome T., Tanabe T., Terada S., Boenigk W., Stuehmer W.,
Cook N.J., Kangawa K., Matsuo H., Hirose T., Miyata T., Numa S.;
"Primary structure and functional expression from complementary DNA of
the rod photoreceptor cyclic GMP-gated channel.";
Nature 342:762-766(1989).
[2]
3D-STRUCTURE MODELING OF 485-610.
PubMed=1316156; DOI=10.1021/bi00134a015;
Kumar V.D., Weber I.T.;
"Molecular model of the cyclic GMP-binding domain of the cyclic GMP-
gated ion channel.";
Biochemistry 31:4643-4649(1992).
[3]
TOPOLOGY.
PubMed=7543681; DOI=10.1073/pnas.92.16.7425;
Henn D.K., Baumann A., Kaupp U.B.;
"Probing the transmembrane topology of cyclic nucleotide-gated ion
channels with a gene fusion approach.";
Proc. Natl. Acad. Sci. U.S.A. 92:7425-7429(1995).
[4]
TOPOLOGY.
PubMed=1370452;
Wohlfart P., Haase W., Molday R.S., Cook N.J.;
"Antibodies against synthetic peptides used to determine the topology
and site of glycosylation of the cGMP-gated channel from bovine rod
photoreceptors.";
J. Biol. Chem. 267:644-648(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 621-690, COILED-COIL DOMAIN,
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).
-!- FUNCTION: Visual signal transduction is mediated by a G-protein
coupled cascade using cGMP as second messenger. This protein can
be activated by cGMP which leads to an opening of the cation
channel and thereby causing a depolarization of rod
photoreceptors.
-!- SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory
subunits. {ECO:0000269|PubMed:21878911}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Rod cells in the retina.
-!- DOMAIN: The C-terminal coiled-coil domain mediates
homotrimerization of CNGA subunits.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X51604; CAA35947.1; -; mRNA.
PIR; S07103; S07103.
RefSeq; NP_776703.1; NM_174278.2.
UniGene; Bt.53; -.
PDB; 3SWF; X-ray; 2.14 A; A/B/C=621-690.
PDBsum; 3SWF; -.
ProteinModelPortal; Q00194; -.
SMR; Q00194; -.
IntAct; Q00194; 1.
MINT; MINT-6825023; -.
STRING; 9913.ENSBTAP00000002853; -.
BindingDB; Q00194; -.
ChEMBL; CHEMBL4907; -.
iPTMnet; Q00194; -.
PaxDb; Q00194; -.
PRIDE; Q00194; -.
Ensembl; ENSBTAT00000002853; ENSBTAP00000002853; ENSBTAG00000002205.
GeneID; 281700; -.
KEGG; bta:281700; -.
CTD; 1259; -.
eggNOG; KOG0500; Eukaryota.
eggNOG; ENOG410YWWI; LUCA.
GeneTree; ENSGT00900000140801; -.
HOGENOM; HOG000007898; -.
HOVERGEN; HBG000281; -.
InParanoid; Q00194; -.
KO; K04948; -.
OMA; CMYFAIS; -.
OrthoDB; EOG091G03EW; -.
TreeFam; TF319048; -.
Reactome; R-BTA-2485179; Activation of the phototransduction cascade.
Reactome; R-BTA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
EvolutionaryTrace; Q00194; -.
PRO; PR:Q00194; -.
Proteomes; UP000009136; Chromosome 6.
Bgee; ENSBTAG00000002205; -.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
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: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:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR032406; CLZ_dom.
InterPro; IPR032945; CNGA1.
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.
PANTHER; PTHR10217:SF387; PTHR10217:SF387; 1.
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; cGMP; cGMP-binding; Coiled coil; Complete proteome;
Direct protein sequencing; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Nucleotide-binding;
Reference proteome; Sensory transduction; Transmembrane;
Transmembrane helix; Transport; Vision.
CHAIN 1 690 cGMP-gated cation channel alpha-1.
/FTId=PRO_0000219306.
TOPO_DOM 1 162 Cytoplasmic. {ECO:0000305}.
TRANSMEM 163 183 Helical; Name=H1. {ECO:0000305}.
TOPO_DOM 184 196 Extracellular. {ECO:0000305}.
TRANSMEM 197 215 Helical; Name=H2. {ECO:0000305}.
TOPO_DOM 216 239 Cytoplasmic. {ECO:0000305}.
TRANSMEM 240 259 Helical; Name=H3. {ECO:0000305}.
TOPO_DOM 260 297 Extracellular. {ECO:0000305}.
TRANSMEM 298 320 Helical; Name=H4. {ECO:0000305}.
TOPO_DOM 321 372 Cytoplasmic. {ECO:0000305}.
TRANSMEM 373 392 Helical; Name=H5. {ECO:0000305}.
TOPO_DOM 393 476 Extracellular. {ECO:0000305}.
TRANSMEM 477 497 Helical; Name=H6. {ECO:0000305}.
TOPO_DOM 498 690 Cytoplasmic. {ECO:0000305}.
NP_BIND 485 607 cGMP. {ECO:0000255}.
COILED 621 664 {ECO:0000269|PubMed:21878911}.
BINDING 544 544 cGMP. {ECO:0000255}.
BINDING 559 559 cGMP. {ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
HELIX 621 672 {ECO:0000244|PDB:3SWF}.
SEQUENCE 690 AA; 79602 MW; A01CFB6567424455 CRC64;
MKKVIINTWH SFVNIPNVVG PDVEKEITRM ENGACSSFSG DDDDSASMFE ESETENPHAR
DSFRSNTHGS GQPSQREQYL PGAIALFNVN NSSNKEQEPK EKKKKKKEKK SKPDDKNENK
KDPEKKKKKE KDKDKKKKEE KGKDKKEEEK KEVVVIDPSG NTYYNWLFCI TLPVMYNWTM
IIARACFDEL QSDYLEYWLA FDYLSDVVYL LDMFVRTRTG YLEQGLLVKE ERKLIDKYKS
TFQFKLDVLS VIPTDLLYIK FGWNYPEIRL NRLLRISRMF EFFQRTETRT NYPNIFRISN
LVMYIIIIIH WNACVYFSIS KAIGFGNDTW VYPDVNDPDF GRLARKYVYS LYWSTLTLTT
IGETPPPVRD SEYFFVVADF LIGVLIFATI VGNIGSMISN MNAARAEFQA RIDAIKQYMH
FRNVSKDMEK RVIKWFDYLW TNKKTVDERE VLKYLPDKLR AEIAINVHLD TLKKVRIFAD
CEAGLLVELV LKLQPQVYSP GDYICKKGDI GREMYIIKEG KLAVVADDGI TQFVVLSDGS
YFGEISILNI KGSKAGNRRT ANIKSIGYSD LFCLSKDDLM EALTEYPDAK GMLEEKGKQI
LMKDGLLDIN IANAGSDPKD LEEKVTRMES SVDLLQTRFA RILAEYESMQ QKLKQRLTKV
EKFLKPLIDT EFSAIEGSGT ESGPTDSTQD


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