CNGA1_CANLF
ID CNGA1_CANLF Reviewed; 691 AA.
AC Q28279;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Beagle X Briard;
RX PubMed=9427553; DOI=10.1016/s0378-1119(97)00461-7;
RA Veske A., Nilsson S.E.G., Gal A.;
RT "Characterization of canine rod photoreceptor cGMP-gated cation channel
RT alpha-subunit gene and exclusion of its involvement in the hereditary
RT retinal dystrophy of Swedish Briards.";
RL Gene 202:115-119(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9268598; DOI=10.1006/exer.1997.0342;
RA Zhang Q., Pearce-Kelling S., Acland G.M., Aguirre G.D., Ray K.;
RT "Canine rod photoreceptor cGMP-gated channel protein alpha-subunit: studies
RT on the expression of the gene and characterization of the cDNA.";
RL Exp. Eye Res. 65:301-309(1997).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q00194};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00194}.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of
CC CNGA subunits. {ECO:0000250}.
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; X99914; CAA68186.1; -; Genomic_DNA.
DR EMBL; U83905; AAB61707.1; -; mRNA.
DR PIR; JC6509; JC6509.
DR RefSeq; NP_001003222.1; NM_001003222.1.
DR RefSeq; XP_005628028.1; XM_005627971.1.
DR AlphaFoldDB; Q28279; -.
DR SMR; Q28279; -.
DR STRING; 9612.ENSCAFP00000035274; -.
DR PaxDb; Q28279; -.
DR GeneID; 403891; -.
DR KEGG; cfa:403891; -.
DR CTD; 1259; -.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q28279; -.
DR OrthoDB; 1073751at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Cell membrane; cGMP; cGMP-binding; Coiled coil; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..691
FT /note="cGMP-gated cation channel alpha-1"
FT /id="PRO_0000219307"
FT TOPO_DOM 1..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 164..184
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 185..197
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 198..216
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 217..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 239..258
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 259..265
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 266..287
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 288..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 299..325
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 326..368
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 369..400
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 401..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 31..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..359
FT /note="P-helix"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 360..368
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 401..483
FT /note="C-linker"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 484..611
FT /note="Cyclic nucleotide-binding domain (CNBD)"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COILED 622..665
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..608
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 545
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 560
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
SQ SEQUENCE 691 AA; 80251 MW; 0775CAA42F065275 CRC64;
MKKNIINTWY SFVNIPNVIV PDIEKEIRRM ENGARSSFSD DDGDDDSASM FEESENETPH
ARDSCRNNSQ RRDPSQREQY LPGAIALFNV NNSSNKEQEP KEKKKKKKEK KSKSGDKNEN
KKDSEKKKKK EKEKEKKNKE EKGKDKKEEE KKEVMVIDPA GNMYYNWLFC ITLPVMYNWT
MVIARACFDE LQSDYLEYWI IFDYLSDIVY LLDMFVRTRT GYLEQGLLVR EEAKLIEKYK
SNLQFKLDFL SVIPTDLLYF KLGWNYPEIR LNRLLRISRM FEFFQRTETR TNYPNIFRIS
NLVMYIVIII HWNACVYFSI SKAIGFGNDT WVYPDVNDPE FGRLARKYVY SLYWSTLTLT
TIGETPPPVR DSEYVFVVVD FLIGVLIFAT IVGNIGSMIS NMNAARAEFQ ARIDAIKQYM
HFRNVSKDME KRVIKWFDYL WTNKKTVDEK EVLKYLPDKL RAEIAINVHL DTLKKVRIFA
DCEAGLLVEL VLKLQPQVYS PGDYICKKGD IGREMYIIKE GKLAVVADDG ITQFVVLSDG
SYFGEISILN IKGSKAGNRR TANIKSIGYS DLFCLSKDDL MEALTEYPDA KTMLEEKGKQ
ILMKDGLLDI NIANAGSDPK DLEEKVTRME GSVDLLQTRF ARILAEYESM QQKLKQRLTK
VERFLKPIID TEFSALEGTG DESRPLDSTQ D
