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Database: UniProt
Entry: Q9N0H4_PIG
LinkDB: Q9N0H4_PIG
Original site: Q9N0H4_PIG 
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
//
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