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   24-JAN-2024, entry version 186.
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
CC       (TC 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   GlyCosmos; P29974; 1 site, No reported glycans.
DR   GlyGen; P29974; 1 site.
DR   iPTMnet; P29974; -.
DR   PhosphoSitePlus; P29974; -.
DR   MaxQB; P29974; -.
DR   PaxDb; 10090-ENSMUSP00000084464; -.
DR   ProteomicsDB; 283399; -.
DR   ABCD; P29974; 1 sequenced antibody.
DR   Antibodypedia; 23791; 113 antibodies from 24 providers.
DR   DNASU; 12788; -.
DR   Ensembl; ENSMUST00000087213.12; ENSMUSP00000084464.6; ENSMUSG00000067220.13.
DR   Ensembl; ENSMUST00000169997.6; ENSMUSP00000132329.2; ENSMUSG00000067220.13.
DR   Ensembl; ENSMUST00000201463.4; ENSMUSP00000143881.2; ENSMUSG00000067220.13.
DR   GeneID; 12788; -.
DR   KEGG; mmu:12788; -.
DR   UCSC; uc008xrr.1; mouse.
DR   AGR; MGI:88436; -.
DR   CTD; 1259; -.
DR   MGI; MGI:88436; Cnga1.
DR   VEuPathDB; HostDB:ENSMUSG00000067220; -.
DR   eggNOG; KOG0500; Eukaryota.
DR   GeneTree; ENSGT00940000156074; -.
DR   InParanoid; P29974; -.
DR   OMA; IYYNWLF; -.
DR   OrthoDB; 74296at2759; -.
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 76 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 48 other cell types or tissues.
DR   ExpressionAtlas; P29974; baseline and differential.
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:0051899; P:membrane depolarization; ISO:MGI.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central.
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; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR032406; CLZ_dom.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   PANTHER; PTHR45638:SF9; CYCLIC NUCLEOTIDE-GATED CHANNEL ROD PHOTORECEPTOR SUBUNIT ALPHA; 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; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   Genevisible; P29974; MM.
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
//