CNG1_CHICK
ID CNG1_CHICK Reviewed; 735 AA.
AC Q90805;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cyclic nucleotide-gated channel cone photoreceptor subunit alpha;
DE AltName: Full=CNG channel 1;
DE Short=CNG-1;
DE Short=CNG1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7684234; DOI=10.1016/0896-6273(93)90202-3;
RA Boenigk W., Altenhofen W., Mueller F., Dose A., Illing M., Molday R.S.,
RA Kaupp U.B.;
RT "Rod and cone photoreceptor cells express distinct genes for cGMP-gated
RT channels.";
RL Neuron 10:865-877(1993).
CC -!- FUNCTION: Visual signal transduction is mediated by a G-protein coupled
CC cascade using cGMP as second messenger. This protein can be activated
CC by cyclic GMP which leads to an opening of the cation channel and
CC thereby causing a depolarization of cone photoreceptors.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. {ECO:0000305}.
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DR EMBL; X89598; CAA61757.1; -; mRNA.
DR PIR; I50630; I50630.
DR RefSeq; NP_990552.1; NM_205221.1.
DR AlphaFoldDB; Q90805; -.
DR SMR; Q90805; -.
DR STRING; 9031.ENSGALP00000041391; -.
DR PaxDb; Q90805; -.
DR PRIDE; Q90805; -.
DR GeneID; 396144; -.
DR KEGG; gga:396144; -.
DR CTD; 1261; -.
DR VEuPathDB; HostDB:geneid_396144; -.
DR eggNOG; KOG0500; Eukaryota.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q90805; -.
DR PRO; PR:Q90805; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
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; 2.60.120.10; -; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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; SSF51206; 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 cAMP; cAMP-binding; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1..735
FT /note="Cyclic nucleotide-gated channel cone photoreceptor
FT subunit alpha"
FT /id="PRO_0000219324"
FT TOPO_DOM 1..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..230
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..262
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..367
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..439
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 142..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 532..654
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 606
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 735 AA; 85032 MW; A67ADFDD942CEFCE CRC64;
MAKINTQHSY PGMHGLSVRT TDEDIERIEN GFIRTHSLCE DTSSELQRVI SMEGRHLSGS
QTSPFTGRGA MARLSRFVVS LRSWATRHLH HEDQRPDSFL ERIRGPELVE VSSRQSNIRS
FLGIREQPGG VNGPWPLARF NVNFSNNTNE DKKEEKKEVK EEKKEEKKEE KKEEKKDDKK
DDKKDDKKDD KKKEEQKKEV FVIDPSSNMY YNWLTIIAAP VFYNWCMLIC RACFDELQID
HIKLWLFLDY CSDIIYVFDM FVRFRTGFLE QGLLVKDEKK LRDHYTQTVQ FKLDVLSLLP
TDLAYLKLGL NYPELRFNRL LRIARLFEFF DRTETRTNYP NMFRIGNLVL YILIIIHWNA
CIYFAISKVI GFGTDSWVYP NVSIPEYGRL SRKYIYSLYW STLTLTTIGE TPPPVKDEEY
LFVVIDFLVG VLIFATIVGN VGSMISNMNA SRAEFQAKVD SIKQYMHFRK VTKDLEARVI
KWFDYLWTNK KTVDEKEVLK NLPDKLKAEI AINVHLDTLK KVRIFQDCEA GLLIELVLKL
KPTVFSPGDY ICKKGDIGRE MYIIKEGKLA VVADDGITQF VVLSDGSYFG EISILNIKGS
KSGNRRTANI RSIGYSDLFC LSKDDLMEAL TEYPEAKKAL EEKGRQILMK DNLIDEEAAK
AGADPKDLEE KIDRLETALD TLQTRFARLL AEYSSSQQKV KQRLARVETR VKKYGSGSLS
VGEPEPEKPE EQKKD
