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Database: UniProt
Entry: G9BLS5_EONSP
LinkDB: G9BLS5_EONSP
Original site: G9BLS5_EONSP 
ID   G9BLS5_EONSP            Unreviewed;       501 AA.
AC   G9BLS5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
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:AET43281.1};
OS   Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Macroglossinae; Eonycteris.
OX   NCBI_TaxID=58065 {ECO:0000313|EMBL:AET43281.1};
RN   [1] {ECO:0000313|EMBL:AET43281.1}
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; HQ610168; AET43281.1; -; mRNA.
DR   AlphaFoldDB; G9BLS5; -.
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        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          364..470
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AET43281.1"
FT   NON_TER         501
FT                   /evidence="ECO:0000313|EMBL:AET43281.1"
SQ   SEQUENCE   501 AA;  58356 MW;  8BBAEF21EF4378EA CRC64;
     DDKNENKKDP EKKKKKEKDK EKKKKEEKDK DKKEEEKKEV MVIDPSGNTY YNWLFCITLP
     VMYNWTMIIA RACFEELQSD YLAYWLIFDY LSDIVYLLDM FVRTRTGYLE QGLLVKEKLK
     LIEKYKSNLQ FKLDVLSVVP TDLLFFKLGW NYPEIRLNRL LRISRMFEFF QRTETRTNYP
     NIFRISNLVM YIVIIIHWNA CVYYSISKVI GFGNDTWVYP DVNDPEFGRL ARKYVYSLYW
     STLTLTTIGE TPPPVRDSEY VFVVVDFLIG VLIFATIVGN IGSMISNMNA ARAEFQARID
     AIKQYMNFRN VSKDMEKRVI KWFDYLWTNK KTVDEREVLK YLPDKLRAEI AISVHLDTLK
     KVRIFADCEA GLLVELVLKL QPQVYSPGDY ICKKGDIGRE MYIIKEGKLA VVADDGITQF
     VVLSDGSYFG EISILNIKGS KAGNRRTANI KSIGYSDLFC LSKDDLMEAL TEYPDAKGML
     EEKGKQILMK DGLLDINIAN A
//
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