ID Q9N0H4_PIG Unreviewed; 686 AA.
AC Q9N0H4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 119.
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=CNG-1 {ECO:0000313|EMBL:AAD05039.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAD05039.1};
RN [1] {ECO:0000313|EMBL:AAD05039.1}
RP NUCLEOTIDE SEQUENCE.
RA Ratcliffe C.F., Brammar W.J., Conley E.C.;
RT "Cloning of cDNAs Encoding cGMP-Gated Cation Channels from Intact Coronary
RT Arteries and Human Vascular Endothelial Cells.";
RL Submitted (JAN-1997) 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; U85404; AAD05039.1; -; mRNA.
DR RefSeq; NP_999342.1; NM_214177.1.
DR AlphaFoldDB; Q9N0H4; -.
DR Genevisible; Q9N0H4; SS.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; 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 2: Evidence at transcript level;
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 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..581
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 31..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 79125 MW; DB86A7C16CE79D3F CRC64;
MKNNIINTQQ SFVTMPNVIV PDIEKEIRRM ENGACSSFSE DDDSASTSEE SENENPHARG
SFSYKSLRKG GPSQREQYLP GAIALFNVNN SSNKDQEPEE KKKKKKEKKS KSDNKNENKN
DPEKKKKKKD KEKKKKEEKS KDKKEEEKKE VVVIDPSGNT YYNWLFCITL PVMYNWTMVI
ARACFDELQS DYLEYWLILD YVSDIVYLID MFVRTRTGYL EQGLLVKEEL KLINKYKSNL
QFKLDVLSLI PTDLLYFKLG WNYPEIRLNR LLRFSRMFEF FQRTETRTNY PNIFRISNLV
MYIVIIIHWN ACVFYSISKA IGFGNDTWVY PDINDPEFGR LARKYVYSLY WSTLTLTTIG
ETPPPVRDSE YVFVVVDFLI GVLIFATIVG NIGSMISNMN AARAEFQARI DAIKQYMHFR
NVSKDMEKRV IKWFDYLWTN KKTVDEKEVL KYLPDKLRAE IAINVHLDTL KKVRIFADCE
AGLLVELVLK LQPQVYSPGD YICKKGDIGR EMYIIKEGKL AVVADDGVTQ FVVLSDGSYF
GEISILNIKG SKAGNRRTAN IKSIGYSDLF CLSKDDLMEA LTEYPDAKTM LEEKGKQILM
KDGLLDLNIA NAGSDPKDLE EKVTRMEGSV DLLQTRFARI LAEYESMQQK LKQRLTKVEK
FLKPLIDTEF SSIEGPGAES GPIDST
//