Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cGMP-gated cation channel alpha-1

Gene

Cnga1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei537 – 5371cGMPSequence analysis
Binding sitei552 – 5521cGMPSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi478 – 600123cGMPSequence analysisAdd
BLAST

GO - Molecular functioni

  • cGMP binding Source: RGD
  • intracellular cGMP activated cation channel activity Source: RGD
  • intracellular cyclic nucleotide activated cation channel activity Source: RGD

GO - Biological processi

  • membrane depolarization Source: RGD
  • regulation of cytosolic calcium ion concentration Source: RGD
  • response to stimulus Source: UniProtKB-KW
  • spermatogenesis Source: RGD
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport, Vision

Keywords - Ligandi

cGMP, cGMP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-gated cation channel alpha-1
Alternative name(s):
Cyclic nucleotide-gated cation channel 1
Cyclic nucleotide-gated channel alpha-1
Short name:
CNG channel alpha-1
Short name:
CNG-1
Short name:
CNG1
Cyclic nucleotide-gated channel, photoreceptor
Rod photoreceptor cGMP-gated channel subunit alpha
Gene namesi
Name:Cnga1
Synonyms:Cncg, Cncg1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621815. Cnga1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 155155CytoplasmicSequence analysisAdd
BLAST
Transmembranei156 – 17621Helical; Name=H1Sequence analysisAdd
BLAST
Topological domaini177 – 18913ExtracellularSequence analysisAdd
BLAST
Transmembranei190 – 20819Helical; Name=H2Sequence analysisAdd
BLAST
Topological domaini209 – 23224CytoplasmicSequence analysisAdd
BLAST
Transmembranei233 – 25220Helical; Name=H3Sequence analysisAdd
BLAST
Topological domaini253 – 29038ExtracellularSequence analysisAdd
BLAST
Transmembranei291 – 31323Helical; Name=H4Sequence analysisAdd
BLAST
Topological domaini314 – 36552CytoplasmicSequence analysisAdd
BLAST
Transmembranei366 – 38520Helical; Name=H5Sequence analysisAdd
BLAST
Topological domaini386 – 46984ExtracellularSequence analysisAdd
BLAST
Transmembranei470 – 49021Helical; Name=H6Sequence analysisAdd
BLAST
Topological domaini491 – 683193CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • intracellular cyclic nucleotide activated cation channel complex Source: RGD
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

GuidetoPHARMACOLOGYi394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683cGMP-gated cation channel alpha-1PRO_0000219310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ62927.
PRIDEiQ62927.

PTM databases

PhosphoSiteiQ62927.

Expressioni

Tissue specificityi

Rod cells in the retina.

Interactioni

Subunit structurei

Tetramer formed of three CNGA1 and one CNGB1 modulatory subunits.By similarity

Protein-protein interaction databases

IntActiQ62927. 1 interaction.
MINTiMINT-8057701.
STRINGi10116.ENSRNOP00000006469.

Structurei

3D structure databases

ProteinModelPortaliQ62927.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili614 – 65744By similarityAdd
BLAST

Domaini

The C-terminal coiled-coil domain mediates homotrimerization of CNGA subunits.By similarity

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0500. Eukaryota.
ENOG410YWWI. LUCA.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiQ62927.
KOiK04948.
PhylomeDBiQ62927.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR032945. CNGA1.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PANTHERiPTHR10217:SF387. PTHR10217:SF387. 1 hit.
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62927-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTNIINTWH SFVNIPNVVV PAIEKEIRRM ENGACSSFSD NDNGSLSEES
60 70 80 90 100
ENEDSLFRSN SYRRRGPSQR EHYLPGTMAL FNVNNSSNKD QDPKEKKKKK
110 120 130 140 150
KEKKSKADDK KESKKDPEKK KKKEKEKEKK KEEKPKEKKE EEKKEVVVID
160 170 180 190 200
PSGNMYYNWL FCITLPVMYN WTMIIARACF DELQSDYLEY WLIFDYVSDV
210 220 230 240 250
VYLADMFVRT RTGYLEQGLL VKDELKLIEK YKANLQFKLD VLSVIPTDLL
260 270 280 290 300
YFKFGWNYPE IRLNRLLRIS RMFEFFQRTE TRTNYPNIFR ISNLVMYIVI
310 320 330 340 350
IIHWNACVYY SISKAIGFGN DTWVYPDVND PEFGRLARKY VYSLYWSTLT
360 370 380 390 400
LTTIGETPPP VLDSEYVFVV VDFLIGVLIF ATIVGNIGSM ISNMNAARAE
410 420 430 440 450
FQSRVDAIKQ YMNFRNVSKD MEKRVIKWFD YLWTNKKTVD EREVLRYLPD
460 470 480 490 500
KLRAEIAINV HLDTLKKVRI FADCEAGLLV ELVLKLQPQV YSPGDYICKK
510 520 530 540 550
GDIGREMYII KEGKLAVVAD DGITQFVVLS DGSYFGEISI LNIKGSKAGN
560 570 580 590 600
RRTANIKSIG YSDLFCLSKD DLMEALTEYP DAKTMLEEKG RQILMKDGLL
610 620 630 640 650
DINIANLGSD PKDLEEKVTR MEGSVDLLQT RFARILAEYE SMQQKLKQRL
660 670 680
TKVEKFLKPL IETEFSALEE PGGESEPTES LQG
Length:683
Mass (Da):79,228
Last modified:November 1, 1997 - v1
Checksum:i62D49F64F8D917C5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42TN → KV in AAC53139 (PubMed:9142860).Curated
Sequence conflicti141 – 1411E → G in AAC53139 (PubMed:9142860).Curated
Sequence conflicti224 – 2241E → K in AAC53139 (PubMed:9142860).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48803 Genomic DNA. Translation: AAA92110.1.
U93851 mRNA. Translation: AAC53139.1.
U76220 mRNA. Translation: AAC17594.1.
RefSeqiNP_445949.1. NM_053497.1.
UniGeneiRn.54534.

Genome annotation databases

GeneIDi85259.
KEGGirno:85259.
UCSCiRGD:621815. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48803 Genomic DNA. Translation: AAA92110.1.
U93851 mRNA. Translation: AAC53139.1.
U76220 mRNA. Translation: AAC17594.1.
RefSeqiNP_445949.1. NM_053497.1.
UniGeneiRn.54534.

3D structure databases

ProteinModelPortaliQ62927.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62927. 1 interaction.
MINTiMINT-8057701.
STRINGi10116.ENSRNOP00000006469.

Chemistry

GuidetoPHARMACOLOGYi394.

PTM databases

PhosphoSiteiQ62927.

Proteomic databases

PaxDbiQ62927.
PRIDEiQ62927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85259.
KEGGirno:85259.
UCSCiRGD:621815. rat.

Organism-specific databases

CTDi1259.
RGDi621815. Cnga1.

Phylogenomic databases

eggNOGiKOG0500. Eukaryota.
ENOG410YWWI. LUCA.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiQ62927.
KOiK04948.
PhylomeDBiQ62927.

Miscellaneous databases

PROiQ62927.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR032945. CNGA1.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PANTHERiPTHR10217:SF387. PTHR10217:SF387. 1 hit.
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Barnstable C.J., Wei J.Y.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-Dawley.
  2. "Cloning and widespread distribution of the rat rod-type cyclic nucleotide-gated cation channel."
    Ding C., Potter E.D., Qiu W., Coon S.L., Levine M.A., Guggino S.E.
    Am. J. Physiol. 272:C1335-C1344(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Functional expression of the heteromeric 'olfactory' cyclic nucleotide-gated channel in the hippocampus: a potential effector of synaptic plasticity in brain neurons."
    Bradley J., Zhang Y., Bakin R., Lester H.A., Ronnett G.V., Zinn K.
    J. Neurosci. 17:1993-2005(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 521-683.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiCNGA1_RAT
AccessioniPrimary (citable) accession number: Q62927
Secondary accession number(s): O08659
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.