ID G9BLT0_9CHIR Unreviewed; 428 AA.
AC G9BLT0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=cGMP-gated cation channel alpha-1 {ECO:0000256|ARBA:ARBA00021373};
DE AltName: Full=Cyclic nucleotide-gated cation channel 1 {ECO:0000256|ARBA:ARBA00031628};
DE AltName: Full=Cyclic nucleotide-gated channel alpha-1 {ECO:0000256|ARBA:ARBA00033061};
DE AltName: Full=Cyclic nucleotide-gated channel, photoreceptor {ECO:0000256|ARBA:ARBA00032867};
DE AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha {ECO:0000256|ARBA:ARBA00030411};
DE Flags: Fragment;
GN Name=CNGA1 {ECO:0000313|EMBL:AET43286.1};
OS Rhinolophus marshalli (Marshall's horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=476588 {ECO:0000313|EMBL:AET43286.1};
RN [1] {ECO:0000313|EMBL:AET43286.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y.-P., Shen Y.-Y.;
RT "Adaptive evolution of a phototransduction gene CNGA1 in bats.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002301}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000256|ARBA:ARBA00010530}.
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DR EMBL; HQ610173; AET43286.1; -; mRNA.
DR AlphaFoldDB; G9BLT0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
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; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
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; 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.
PE 2: Evidence at transcript level;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT TRANSMEM 13..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 293..399
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AET43286.1"
FT NON_TER 428
FT /evidence="ECO:0000313|EMBL:AET43286.1"
SQ SEQUENCE 428 AA; 49542 MW; 776D0AEC380F6C7A CRC64;
ACFDELQADY LEYWLFLDYL SDVVYLLDMF IRTRTGYLEQ GLLVKEELKL IEKYKSNLQF
KLDVLSVVPT DLLYFKLGWN YPEIRLNRLL RISRIFEFFQ RTETRTNYPN IFRISNLVMY
IVIIIHWNAC VYYSISKAIG FGNDTWVYPD VNDPEFGRLA RKYVYSLYWS TLTLTTIGET
PPPVRDSEYV FVVVDFLIGV LIFATIVGNI GSMISNMNAA RAEFQARIDA IKQYMHFRNV
SKDMEKRVIK WFDYLWTNKK TVDEREVLKY LPDKLRAEIA ISVHLDTLKK VRIFADCEAG
LLVELVLKLQ PQVYSPGDYI CKKGDIGREM YIIKEGKLAV VADDGITQFV VLSDGSYFGE
ISILNIKGSK AGNRRTANIK SIGYSDLFCL SKDDLMEALT EYPDAKCILE EKGKQILMKD
GLLDINIA
//
