ID M3Y1L9_MUSPF Unreviewed; 658 AA.
AC M3Y1L9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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};
GN Name=CNGA1 {ECO:0000313|Ensembl:ENSMPUP00000005220.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005220.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000005220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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; AEYP01062457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3Y1L9; -.
DR STRING; 9669.ENSMPUP00000005220; -.
DR Ensembl; ENSMPUT00000005308.1; ENSMPUP00000005220.1; ENSMPUG00000005258.1.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000156074; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR InParanoid; M3Y1L9; -.
DR OMA; MITNINA; -.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
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; 1.20.5.170; -; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..551
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 75952 MW; 8AF84FE68EEA43AD CRC64;
SSFSDDDEDD DDDSASMFEE SENENPHARG SHKHNSHRGG PSQREQYLPG ALALFNVNNS
SNKEPEPKEK KKKKKEKKGK SDDKNENKND SEKKKKKAKE KEKKKKEEKD KDKKEEEKKE
VMVIDPSGTT YYNWLFCISL PVMYNWTMVI ARACFEELQS DYLAYWVILD YISDIIYLLD
MFVRIRTGYL EQGLLVKEET KLIKKYKSTL QFKLDFLSVI PTDLLYFKLG WNYPEIRLNR
LLRISRMFEF FQRTETRTNF PNIFRISNLV MYIVIIIHWN ACVYFSISKA VGFGNDTWVY
PDVNDPEFGR LARKYVYSLY WSTLTLTTIG ETPPPVRDSE YVFVVVDFLI GVLIFATIVG
NIGSMISNMN AARAEFQARI DAIKQYMHFR NVSKDMEKRV IKWFDYLWSN KKTVDEKEVL
KYLPDKLRAE IAINVHLDTL KKVRIFADCE AGLLVELVLK LQPQVYSPGD YICKKGDIGR
EMYIIKEGRL AVVADDGVTQ FVVLSDGSYF GEISILNIKG SKAGNRRTAN IKSIGYSDLF
CLSKDDLMEA LTEYPDAKTM LEEKGKQILM KDGLLDINIA NAGSDPKDLE EKVTRMEGSV
DLLQTRFARI LAEYESMQQK LKQRLTKVER FLKPLIDTEF SALEGSGVES GLLDSTQD
//
