CNGA1_MOUSE
ID CNGA1_MOUSE Reviewed; 684 AA.
AC P29974; B9EJ09; Q60776;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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].
RC TISSUE=Kidney;
RX PubMed=7540868; DOI=10.1016/0005-2736(95)00068-e;
RA Karlson K.H., Ciampolillo-Bates F., McCoy D.E., Kizer N.L., Stanton B.A.;
RT "Cloning of a cGMP-gated cation channel from mouse kidney inner medullary
RT collecting duct.";
RL Biochim. Biophys. Acta 1236:197-200(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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 -!- TISSUE SPECIFICITY: Rod cells in the retina and inner medulla of
CC kidney.
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; M84742; AAA37425.1; -; mRNA.
DR EMBL; U19717; AAA85702.1; -; mRNA.
DR EMBL; U19715; AAA85700.1; -; mRNA.
DR EMBL; U19716; AAA85701.1; -; mRNA.
DR EMBL; BC141261; AAI41262.1; -; mRNA.
DR CCDS; CCDS19333.1; -.
DR RefSeq; NP_031749.2; NM_007723.2.
DR AlphaFoldDB; P29974; -.
DR SMR; P29974; -.
DR BioGRID; 198783; 17.
DR IntAct; P29974; 1.
DR STRING; 10090.ENSMUSP00000084464; -.
DR GlyGen; P29974; 1 site.
DR iPTMnet; P29974; -.
DR PhosphoSitePlus; P29974; -.
DR MaxQB; P29974; -.
DR PaxDb; P29974; -.
DR PRIDE; P29974; -.
DR ProteomicsDB; 283399; -.
DR ABCD; P29974; 1 sequenced antibody.
DR Antibodypedia; 23791; 101 antibodies from 24 providers.
DR DNASU; 12788; -.
DR Ensembl; ENSMUST00000087213; ENSMUSP00000084464; ENSMUSG00000067220.
DR Ensembl; ENSMUST00000169997; ENSMUSP00000132329; ENSMUSG00000067220.
DR Ensembl; ENSMUST00000201463; ENSMUSP00000143881; ENSMUSG00000067220.
DR GeneID; 12788; -.
DR KEGG; mmu:12788; -.
DR UCSC; uc008xrr.1; mouse.
DR CTD; 1259; -.
DR MGI; MGI:88436; Cnga1.
DR VEuPathDB; HostDB:ENSMUSG00000067220; -.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000156074; -.
DR InParanoid; P29974; -.
DR OMA; FQFKLDF; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; P29974; -.
DR TreeFam; TF319048; -.
DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 12788; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cnga1; mouse.
DR PRO; PR:P29974; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P29974; protein.
DR Bgee; ENSMUSG00000067220; Expressed in retinal neural layer and 47 other tissues.
DR ExpressionAtlas; P29974; baseline and differential.
DR Genevisible; P29974; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0030553; F:cGMP binding; ISO:MGI.
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; ISO:MGI.
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:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
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..684
FT /note="cGMP-gated cation channel alpha-1"
FT /id="PRO_0000219309"
FT TOPO_DOM 1..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 157..177
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 178..190
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 191..209
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 210..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 232..251
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 252..258
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 259..280
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 281..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 292..318
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 319..361
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 362..393
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 394..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 34..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..352
FT /note="P-helix"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 353..361
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 394..476
FT /note="C-linker"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 477..604
FT /note="Cyclic nucleotide-binding domain (CNBD)"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COILED 615..658
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COMPBIAS 51..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..601
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 538
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 553
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT CONFLICT 113..114
FT /note="NK -> I (in Ref. 1; AAA37425)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> N (in Ref. 1; AAA37425)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="A -> V (in Ref. 1; AAA37425)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="R -> C (in Ref. 1; AAA37425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 79460 MW; 13EC2A405B6B8CBF CRC64;
MKTNIINTWH SFVNIPNVIV PAIEKEIRRM ENGACSSFSD DDNGSLSEES ENEDSFFRSN
SYKRRGPSQR EQHLPGTMAL FNVNNSSNKD QEPKEKKKKK KEKKSKADDK NENKKDPEKK
KKKEKEKEKK KKEEKTKEKK EEEKKEVVVI DPSGNTYYNW LFCITLPVMY NWTMIIARAC
FDELQSDYLE YWLIFDYVSD VVYLADMFVR TRTGYLEQGL LVKDRMKLIE KYKANLQFKL
DVLSVIPTDL LYIKFGWNYP EIRLNRLLRI SRMFEFFQRT ETRTNYPNIF RISNLVMYIV
IIIHWNACVY YSISKAIGFG NDTWVYPDVN DPEFGRLARK YVYSLYWSTL TLTTIGETPP
PVLDSEYIFV VVDFLIGVLI FATIVGNIGS MISNMNAARA EFQSRVDAIK QYMNFRNVSK
DMEKRVIKWF DYLWTNKKTV DEREVLRYLP DKLRAEIAIN VHLDTLKKVR IFADCEAGLL
VELVLKLQPQ VYSPGDYICK KGDIGREMYI IKEGKLAVVA DDGITQFVVL SDGSYFGEIS
ILNIKGSKAG NRRTANIKSI GYSDLFCLSK DDLMEALTEY PDAKTMLEEK GRQILMKDGL
LDINIANMGS DPKDLEEKVT RMEGSVDLLQ TRFARILAEY ESMQQKLKQR LTKVEKFLKP
LIETEFSALE EPGGESELTE SLQD
