CNGA1_BOVIN
ID CNGA1_BOVIN Reviewed; 690 AA.
AC Q00194;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 162.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 240-245; 261-269; 279-284;
RP 406-411; 417-422; 435-443; 454-460; 513-518; 591-596; 628-637; 639-652 AND
RP 663-677, AND FUNCTION.
RC TISSUE=Retinal rod cell;
RX PubMed=2481236; DOI=10.1038/342762a0;
RA Kaupp U.B., Niidome T., Tanabe T., Terada S., Boenigk W., Stuehmer W.,
RA Cook N.J., Kangawa K., Matsuo H., Hirose T., Miyata T., Numa S.;
RT "Primary structure and functional expression from complementary DNA of the
RT rod photoreceptor cyclic GMP-gated channel.";
RL Nature 342:762-766(1989).
RN [2]
RP 3D-STRUCTURE MODELING OF 485-610.
RX PubMed=1316156; DOI=10.1021/bi00134a015;
RA Kumar V.D., Weber I.T.;
RT "Molecular model of the cyclic GMP-binding domain of the cyclic GMP-gated
RT ion channel.";
RL Biochemistry 31:4643-4649(1992).
RN [3]
RP TOPOLOGY.
RX PubMed=7543681; DOI=10.1073/pnas.92.16.7425;
RA Henn D.K., Baumann A., Kaupp U.B.;
RT "Probing the transmembrane topology of cyclic nucleotide-gated ion channels
RT with a gene fusion approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7425-7429(1995).
RN [4]
RP TOPOLOGY, GLYCOSYLATION AT ASN-327, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1370452; DOI=10.1016/s0021-9258(18)48542-0;
RA Wohlfart P., Haase W., Molday R.S., Cook N.J.;
RT "Antibodies against synthetic peptides used to determine the topology and
RT site of glycosylation of the cGMP-gated channel from bovine rod
RT photoreceptors.";
RL J. Biol. Chem. 267:644-648(1992).
RN [5]
RP TOPOLOGY, MUTAGENESIS OF PRO-293, AND SUBCELLULAR LOCATION.
RX PubMed=25963832; DOI=10.1038/ncomms8093;
RA Maity S., Mazzolini M., Arcangeletti M., Valbuena A., Fabris P.,
RA Lazzarino M., Torre V.;
RT "Conformational rearrangements in the transmembrane domain of CNGA1
RT channels revealed by single-molecule force spectroscopy.";
RL Nat. Commun. 6:7093-7093(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 621-690, COILED-COIL DOMAIN,
RP HOMOTETRAMERIZATION, AND HETEROTETRAMERIZATION WITH CNGB1.
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).
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:0000269|PubMed:2481236}.
CC -!- SUBUNIT: Forms a heterotetramer with CNGB1 in a 3:1 ratio
CC (PubMed:21878911). May also form cyclic nucleotide-activated
CC homotetrameric channels, that are efficiently activated by saturating
CC cGMP, but poorly activated by saturating cAMP compared to the
CC heterotetramer with CNGB1 (PubMed:21878911).
CC {ECO:0000269|PubMed:21878911}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1370452};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1370452,
CC ECO:0000269|PubMed:25963832}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, in rod cells (at protein
CC level). {ECO:0000269|PubMed:1370452}.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of
CC CNGA subunits.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
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DR EMBL; X51604; CAA35947.1; -; mRNA.
DR PIR; S07103; S07103.
DR RefSeq; NP_776703.1; NM_174278.2.
DR PDB; 3SWF; X-ray; 2.14 A; A/B/C=621-690.
DR PDB; 7O4H; EM; 3.40 A; A/B/C=1-690.
DR PDBsum; 3SWF; -.
DR PDBsum; 7O4H; -.
DR AlphaFoldDB; Q00194; -.
DR SMR; Q00194; -.
DR IntAct; Q00194; 1.
DR MINT; Q00194; -.
DR STRING; 9913.ENSBTAP00000002853; -.
DR BindingDB; Q00194; -.
DR ChEMBL; CHEMBL4907; -.
DR DrugCentral; Q00194; -.
DR iPTMnet; Q00194; -.
DR PaxDb; Q00194; -.
DR PRIDE; Q00194; -.
DR Ensembl; ENSBTAT00000002853; ENSBTAP00000002853; ENSBTAG00000002205.
DR GeneID; 281700; -.
DR KEGG; bta:281700; -.
DR CTD; 1259; -.
DR VEuPathDB; HostDB:ENSBTAG00000002205; -.
DR VGNC; VGNC:27497; CNGA1.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000156074; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR InParanoid; Q00194; -.
DR OMA; FQFKLDF; -.
DR OrthoDB; 1073751at2759; -.
DR TreeFam; TF319048; -.
DR EvolutionaryTrace; Q00194; -.
DR PRO; PR:Q00194; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000002205; Expressed in retina and 22 other tissues.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IDA:UniProtKB.
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:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IMP:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Direct protein sequencing; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1..690
FT /note="cGMP-gated cation channel alpha-1"
FT /id="PRO_0000219306"
FT TOPO_DOM 1..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 163..183
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 184..196
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 197..215
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 216..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 238..257
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 258..264
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 265..286
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 287..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 298..324
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 325..367
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TRANSMEM 368..399
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000305|PubMed:25963832"
FT TOPO_DOM 400..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25963832"
FT REGION 33..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..358
FT /note="P-helix"
FT /evidence="ECO:0000305|PubMed:25963832"
FT REGION 359..367
FT /note="Selectivity filter"
FT /evidence="ECO:0000305|PubMed:25963832"
FT REGION 400..482
FT /note="C-linker"
FT /evidence="ECO:0000305|PubMed:25963832"
FT REGION 483..610
FT /note="Cyclic nucleotide-binding domain (CNBD)"
FT /evidence="ECO:0000305|PubMed:25963832"
FT COILED 621..664
FT /evidence="ECO:0000269|PubMed:21878911"
FT COMPBIAS 111..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..607
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 544
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 559
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1370452"
FT MUTAGEN 293
FT /note="P->A: Affects ionic permeation."
FT /evidence="ECO:0000269|PubMed:25963832"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 293..322
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 374..401
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 420..423
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 426..440
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:7O4H"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:7O4H"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 577..582
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 587..603
FT /evidence="ECO:0007829|PDB:7O4H"
FT HELIX 621..672
FT /evidence="ECO:0007829|PDB:3SWF"
SQ 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
