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cGMP-gated cation channel alpha-1 (Cyclic nucleotide-gated cation channel 1) (Cyclic nucleotide-gated channel alpha-1) (CNG channel alpha-1) (CNG-1) (CNG1) (Cyclic nucleotide-gated channel, photoreceptor) (Rod photoreceptor cGMP-gated channel subunit alpha)

 CNGA1_CANLF             Reviewed;         691 AA.
Q28279;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=cGMP-gated cation channel alpha-1;
AltName: Full=Cyclic nucleotide-gated cation channel 1;
AltName: Full=Cyclic nucleotide-gated channel alpha-1;
Short=CNG channel alpha-1;
Short=CNG-1;
Short=CNG1;
AltName: Full=Cyclic nucleotide-gated channel, photoreceptor;
AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha;
Name=CNGA1; Synonyms=CNCG, CNCG1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Beagle X Briard;
PubMed=9427553; DOI=10.1016/S0378-1119(97)00461-7;
Veske A., Nilsson S.E.G., Gal A.;
"Characterization of canine rod photoreceptor cGMP-gated cation
channel alpha-subunit gene and exclusion of its involvement in the
hereditary retinal dystrophy of Swedish Briards.";
Gene 202:115-119(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9268598; DOI=10.1006/exer.1997.0342;
Zhang Q., Pearce-Kelling S., Acland G.M., Aguirre G.D., Ray K.;
"Canine rod photoreceptor cGMP-gated channel protein alpha-subunit:
studies on the expression of the gene and characterization of the
cDNA.";
Exp. Eye Res. 65:301-309(1997).
-!- FUNCTION: Visual signal transduction is mediated by a G-protein
coupled cascade using cGMP as second messenger. This protein can
be activated by cGMP which leads to an opening of the cation
channel and thereby causing a depolarization of rod
photoreceptors.
-!- SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory
subunits. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- DOMAIN: The C-terminal coiled-coil domain mediates
homotrimerization of CNGA subunits. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. CNGA1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X99914; CAA68186.1; -; Genomic_DNA.
EMBL; U83905; AAB61707.1; -; mRNA.
PIR; JC6509; JC6509.
RefSeq; NP_001003222.1; NM_001003222.1.
RefSeq; XP_005628028.1; XM_005627971.1.
UniGene; Cfa.3753; -.
ProteinModelPortal; Q28279; -.
SMR; Q28279; -.
STRING; 9615.ENSCAFP00000035274; -.
PaxDb; Q28279; -.
GeneID; 403891; -.
KEGG; cfa:403891; -.
CTD; 1259; -.
eggNOG; KOG0500; Eukaryota.
eggNOG; ENOG410YWWI; LUCA.
HOGENOM; HOG000007898; -.
HOVERGEN; HBG000281; -.
InParanoid; Q28279; -.
KO; K04948; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IEA:InterPro.
GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR032406; CLZ_dom.
InterPro; IPR032945; CNGA1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
PANTHER; PTHR10217:SF387; PTHR10217:SF387; 1.
Pfam; PF16526; CLZ; 1.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS00889; CNMP_BINDING_2; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
2: Evidence at transcript level;
cGMP; cGMP-binding; Coiled coil; Complete proteome; Glycoprotein;
Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
Nucleotide-binding; Reference proteome; Sensory transduction;
Transmembrane; Transmembrane helix; Transport; Vision.
CHAIN 1 691 cGMP-gated cation channel alpha-1.
/FTId=PRO_0000219307.
TOPO_DOM 1 163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 164 184 Helical; Name=H1. {ECO:0000255}.
TOPO_DOM 185 197 Extracellular. {ECO:0000255}.
TRANSMEM 198 216 Helical; Name=H2. {ECO:0000255}.
TOPO_DOM 217 240 Cytoplasmic. {ECO:0000255}.
TRANSMEM 241 260 Helical; Name=H3. {ECO:0000255}.
TOPO_DOM 261 298 Extracellular. {ECO:0000255}.
TRANSMEM 299 321 Helical; Name=H4. {ECO:0000255}.
TOPO_DOM 322 373 Cytoplasmic. {ECO:0000255}.
TRANSMEM 374 393 Helical; Name=H5. {ECO:0000255}.
TOPO_DOM 394 477 Extracellular. {ECO:0000255}.
TRANSMEM 478 498 Helical; Name=H6. {ECO:0000255}.
TOPO_DOM 499 691 Cytoplasmic. {ECO:0000255}.
NP_BIND 486 608 cGMP. {ECO:0000255}.
COILED 622 665 {ECO:0000250}.
BINDING 545 545 cGMP. {ECO:0000255}.
BINDING 560 560 cGMP. {ECO:0000255}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 691 AA; 80251 MW; 0775CAA42F065275 CRC64;
MKKNIINTWY SFVNIPNVIV PDIEKEIRRM ENGARSSFSD DDGDDDSASM FEESENETPH
ARDSCRNNSQ RRDPSQREQY LPGAIALFNV NNSSNKEQEP KEKKKKKKEK KSKSGDKNEN
KKDSEKKKKK EKEKEKKNKE EKGKDKKEEE KKEVMVIDPA GNMYYNWLFC ITLPVMYNWT
MVIARACFDE LQSDYLEYWI IFDYLSDIVY LLDMFVRTRT GYLEQGLLVR EEAKLIEKYK
SNLQFKLDFL SVIPTDLLYF KLGWNYPEIR LNRLLRISRM FEFFQRTETR TNYPNIFRIS
NLVMYIVIII HWNACVYFSI SKAIGFGNDT WVYPDVNDPE FGRLARKYVY SLYWSTLTLT
TIGETPPPVR DSEYVFVVVD FLIGVLIFAT IVGNIGSMIS NMNAARAEFQ ARIDAIKQYM
HFRNVSKDME KRVIKWFDYL WTNKKTVDEK EVLKYLPDKL RAEIAINVHL DTLKKVRIFA
DCEAGLLVEL VLKLQPQVYS PGDYICKKGD IGREMYIIKE GKLAVVADDG ITQFVVLSDG
SYFGEISILN IKGSKAGNRR TANIKSIGYS DLFCLSKDDL MEALTEYPDA KTMLEEKGKQ
ILMKDGLLDI NIANAGSDPK DLEEKVTRME GSVDLLQTRF ARILAEYESM QQKLKQRLTK
VERFLKPIID TEFSALEGTG DESRPLDSTQ D


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