ID A0A340WQD5_LIPVE Unreviewed; 689 AA.
AC A0A340WQD5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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|RefSeq:XP_007451031.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007451031.1};
RN [1] {ECO:0000313|RefSeq:XP_007451031.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_007451031.1; XM_007450969.1.
DR AlphaFoldDB; A0A340WQD5; -.
DR STRING; 118797.A0A340WQD5; -.
DR GeneID; 103078535; -.
DR KEGG; lve:103078535; -.
DR CTD; 1259; -.
DR InParanoid; A0A340WQD5; -.
DR OrthoDB; 74296at2759; -.
DR Proteomes; UP000265300; Unplaced.
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; 1.20.5.170; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 300..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 476..582
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 34..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 79514 MW; 798F0EFE42E20347 CRC64;
MKKIIINTRR SFVNIPNVIV PDIEKEIRRM ENGACSSFSD DDDSASLFEE SESENTRARD
SFTSSRHGRG QPSQREQYLP GAIALFNVNN SSNKEQEPKE KKKKKKEKKS KPDDKNKNKK
DPEKEKKKEK DKDKKKKEEK GKDKKEEEKK EVMVIDPSGS TYYNWLFCIT LPVMYNWTMI
IARACFDELQ SDYLEYWLIL DYLSDIVYLL DMFVRTRTGY LEQGLLVKEE LKLIEKYKSD
FQFKLDVVSV IPTDLLYFNL GWNYPEIRLN RLLRISRMFE FFQRTETRTN YPNIFRISNL
VMYIVIIIHW NACVYFSISK AVGFGNDTWV YPDVNDPEFG RLARKYVYSL YWSTLTLTTI
GETPPPVRDS EYIFVVADFL IGVLIFATIV GNIGSMISNM NAARAEFQAR IDAIKQYMHF
RNVSKDMEKR VIKWFDYLWT NKKTVDEKEV LKYLPDKLRA EIAINVHLDT LKKVRIFADC
EAGLLVELVL KLQPQVYSPG DYICKKGDIG REMYIIKEGK LAVVADDGIT QFVVLSDGSY
FGEISILNIK GSKAGNRRTA NIKSIGYSDL FCLSKDDLME ALTEYPDAKC MLEEKGKQIL
MKDGLLDINI ANAGSDPKDL EEKVTRMEGS VDLLQTKFAR ILAEYESMQQ KLKQRLTKVE
QFLKPLIDTE FSAIEGSGAE SGPTGSTQD
//
