CNGA1_RAT
ID CNGA1_RAT Reviewed; 683 AA.
AC Q62927; O08659;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sprague-Dawley;
RA Barnstable C.J., Wei J.Y.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9142860; DOI=10.1152/ajpcell.1997.272.4.c1335;
RA Ding C., Potter E.D., Qiu W., Coon S.L., Levine M.A., Guggino S.E.;
RT "Cloning and widespread distribution of the rat rod-type cyclic nucleotide-
RT gated cation channel.";
RL Am. J. Physiol. 272:C1335-C1344(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 521-683.
RC STRAIN=Sprague-Dawley;
RX PubMed=9045728; DOI=10.1523/jneurosci.17-06-01993.1997;
RA Bradley J., Zhang Y., Bakin R., Lester H.A., Ronnett G.V., Zinn K.;
RT "Functional expression of the heteromeric 'olfactory' cyclic nucleotide-
RT gated channel in the hippocampus: a potential effector of synaptic
RT plasticity in brain neurons.";
RL J. Neurosci. 17:1993-2005(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 -!- TISSUE SPECIFICITY: Rod cells in the retina.
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; U48803; AAA92110.1; -; Genomic_DNA.
DR EMBL; U93851; AAC53139.1; -; mRNA.
DR EMBL; U76220; AAC17594.1; -; mRNA.
DR RefSeq; NP_445949.1; NM_053497.1.
DR AlphaFoldDB; Q62927; -.
DR SMR; Q62927; -.
DR IntAct; Q62927; 1.
DR MINT; Q62927; -.
DR STRING; 10116.ENSRNOP00000006469; -.
DR GuidetoPHARMACOLOGY; 394; -.
DR GlyGen; Q62927; 1 site.
DR PhosphoSitePlus; Q62927; -.
DR PaxDb; Q62927; -.
DR PRIDE; Q62927; -.
DR ABCD; Q62927; 1 sequenced antibody.
DR GeneID; 85259; -.
DR KEGG; rno:85259; -.
DR UCSC; RGD:621815; rat.
DR CTD; 1259; -.
DR RGD; 621815; Cnga1.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q62927; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q62927; -.
DR Reactome; R-RNO-2485179; Activation of the phototransduction cascade.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:Q62927; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0030553; F:cGMP binding; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; TAS:RGD.
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; IDA:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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..683
FT /note="cGMP-gated cation channel alpha-1"
FT /id="PRO_0000219310"
FT TOPO_DOM 1..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 156..176
FT /note="Helical; Name=S1"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 177..189
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 190..208
FT /note="Helical; Name=S2"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 209..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 231..250
FT /note="Helical; Name=S3"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 251..257
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 258..279
FT /note="Helical; Name=S4"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 280..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 291..317
FT /note="Helical; Name=S5"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 318..360
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TRANSMEM 361..392
FT /note="Helical; Name=S6"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT TOPO_DOM 393..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 34..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..351
FT /note="P-helix"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 352..360
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 393..475
FT /note="C-linker"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT REGION 476..603
FT /note="Cyclic nucleotide-binding domain (CNBD)"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT COILED 614..657
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..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..600
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 537
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 552
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00194"
FT CONFLICT 3..4
FT /note="TN -> KV (in Ref. 2; AAC53139)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> G (in Ref. 2; AAC53139)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="E -> K (in Ref. 2; AAC53139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 79228 MW; 62D49F64F8D917C5 CRC64;
MKTNIINTWH SFVNIPNVVV PAIEKEIRRM ENGACSSFSD NDNGSLSEES ENEDSLFRSN
SYRRRGPSQR EHYLPGTMAL FNVNNSSNKD QDPKEKKKKK KEKKSKADDK KESKKDPEKK
KKKEKEKEKK KEEKPKEKKE EEKKEVVVID PSGNMYYNWL FCITLPVMYN WTMIIARACF
DELQSDYLEY WLIFDYVSDV VYLADMFVRT RTGYLEQGLL VKDELKLIEK YKANLQFKLD
VLSVIPTDLL YFKFGWNYPE IRLNRLLRIS RMFEFFQRTE TRTNYPNIFR ISNLVMYIVI
IIHWNACVYY SISKAIGFGN DTWVYPDVND PEFGRLARKY VYSLYWSTLT LTTIGETPPP
VLDSEYVFVV VDFLIGVLIF ATIVGNIGSM ISNMNAARAE FQSRVDAIKQ YMNFRNVSKD
MEKRVIKWFD YLWTNKKTVD EREVLRYLPD KLRAEIAINV HLDTLKKVRI FADCEAGLLV
ELVLKLQPQV YSPGDYICKK GDIGREMYII KEGKLAVVAD DGITQFVVLS DGSYFGEISI
LNIKGSKAGN RRTANIKSIG YSDLFCLSKD DLMEALTEYP DAKTMLEEKG RQILMKDGLL
DINIANLGSD PKDLEEKVTR MEGSVDLLQT RFARILAEYE SMQQKLKQRL TKVEKFLKPL
IETEFSALEE PGGESEPTES LQG
