Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P29974 (CNGA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cnga1
Synonyms:Cncg, Cncg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Rod cells in the retina and inner medulla of kidney.

Domain

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

Sequence similarities

Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA1 subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Ontologies

Keywords
   Biological processIon transport
Sensory transduction
Transport
Vision
   Cellular componentMembrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandcGMP
cGMP-binding
Nucleotide-binding
   Molecular functionIon channel
Ligand-gated ion channel
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphototransduction, visible light

Inferred from Biological aspect of Ancestor. Source: RefGenome

potassium ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of membrane potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 15634774. Source: MGI

photoreceptor outer segment

Inferred from direct assay PubMed 15634774PubMed 20592197. Source: MGI

photoreceptor outer segment membrane

Inferred from direct assay PubMed 18654668. Source: BHF-UCL

   Molecular_functioncGMP binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cAMP activated cation channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular cGMP activated cation channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

voltage-gated potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684cGMP-gated cation channel alpha-1
PRO_0000219309

Regions

Topological domain1 – 156156Cytoplasmic Potential
Transmembrane157 – 17721Helical; Name=H1; Potential
Topological domain178 – 19013Extracellular Potential
Transmembrane191 – 20919Helical; Name=H2; Potential
Topological domain210 – 23324Cytoplasmic Potential
Transmembrane234 – 25320Helical; Name=H3; Potential
Topological domain254 – 29138Extracellular Potential
Transmembrane292 – 31423Helical; Name=H4; Potential
Topological domain315 – 36652Cytoplasmic Potential
Transmembrane367 – 38620Helical; Name=H5; Potential
Topological domain387 – 47084Extracellular Potential
Transmembrane471 – 49121Helical; Name=H6; Potential
Topological domain492 – 684193Cytoplasmic Potential
Nucleotide binding479 – 601123cGMP Potential
Coiled coil615 – 65844 By similarity

Sites

Binding site5381cGMP Potential
Binding site5531cGMP Potential

Amino acid modifications

Glycosylation4171N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict113 – 1142NK → I in AAA37425. Ref.1
Sequence conflict2001D → N in AAA37425. Ref.1
Sequence conflict5761A → V in AAA37425. Ref.1
Sequence conflict6351R → C in AAA37425. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29974 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 13EC2A405B6B8CBF

FASTA68479,460
        10         20         30         40         50         60 
MKTNIINTWH SFVNIPNVIV PAIEKEIRRM ENGACSSFSD DDNGSLSEES ENEDSFFRSN 

        70         80         90        100        110        120 
SYKRRGPSQR EQHLPGTMAL FNVNNSSNKD QEPKEKKKKK KEKKSKADDK NENKKDPEKK 

       130        140        150        160        170        180 
KKKEKEKEKK KKEEKTKEKK EEEKKEVVVI DPSGNTYYNW LFCITLPVMY NWTMIIARAC 

       190        200        210        220        230        240 
FDELQSDYLE YWLIFDYVSD VVYLADMFVR TRTGYLEQGL LVKDRMKLIE KYKANLQFKL 

       250        260        270        280        290        300 
DVLSVIPTDL LYIKFGWNYP EIRLNRLLRI SRMFEFFQRT ETRTNYPNIF RISNLVMYIV 

       310        320        330        340        350        360 
IIIHWNACVY YSISKAIGFG NDTWVYPDVN DPEFGRLARK YVYSLYWSTL TLTTIGETPP 

       370        380        390        400        410        420 
PVLDSEYIFV VVDFLIGVLI FATIVGNIGS MISNMNAARA EFQSRVDAIK QYMNFRNVSK 

       430        440        450        460        470        480 
DMEKRVIKWF DYLWTNKKTV DEREVLRYLP DKLRAEIAIN VHLDTLKKVR IFADCEAGLL 

       490        500        510        520        530        540 
VELVLKLQPQ VYSPGDYICK KGDIGREMYI IKEGKLAVVA DDGITQFVVL SDGSYFGEIS 

       550        560        570        580        590        600 
ILNIKGSKAG NRRTANIKSI GYSDLFCLSK DDLMEALTEY PDAKTMLEEK GRQILMKDGL 

       610        620        630        640        650        660 
LDINIANMGS DPKDLEEKVT RMEGSVDLLQ TRFARILAEY ESMQQKLKQR LTKVEKFLKP 

       670        680 
LIETEFSALE EPGGESELTE SLQD 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel."
Pittler S.J., Lee A.K., Altherr M.R., Howard T.A., Seldin M.F., Hurwitz R.L., Wasmuth J.J., Baehr W.
J. Biol. Chem. 267:6257-6262(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Cloning of a cGMP-gated cation channel from mouse kidney inner medullary collecting duct."
Karlson K.H., Ciampolillo-Bates F., McCoy D.E., Kizer N.L., Stanton B.A.
Biochim. Biophys. Acta 1236:197-200(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84742 mRNA. Translation: AAA37425.1.
U19717 mRNA. Translation: AAA85702.1.
U19715 mRNA. Translation: AAA85700.1.
U19716 mRNA. Translation: AAA85701.1.
BC141261 mRNA. Translation: AAI41262.1.
CCDSCCDS19333.1.
RefSeqNP_031749.2. NM_007723.2.
UniGeneMm.436652.

3D structure databases

ProteinModelPortalP29974.
SMRP29974. Positions 340-588, 615-664.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP29974.

Proteomic databases

PRIDEP29974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087213; ENSMUSP00000084464; ENSMUSG00000067220.
ENSMUST00000135701; ENSMUSP00000119886; ENSMUSG00000067220.
ENSMUST00000169997; ENSMUSP00000132329; ENSMUSG00000067220.
GeneID12788.
KEGGmmu:12788.
UCSCuc008xrr.1. mouse.

Organism-specific databases

CTD1259.
MGIMGI:88436. Cnga1.

Phylogenomic databases

eggNOGNOG300025.
GeneTreeENSGT00550000074376.
HOGENOMHOG000007898.
HOVERGENHBG000281.
InParanoidP29974.
KOK04948.
OMAWTMVIAR.
OrthoDBEOG771268.
PhylomeDBP29974.
TreeFamTF319048.

Gene expression databases

BgeeP29974.
CleanExMM_CNGA1.
GenevestigatorP29974.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
PROSITEPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282186.
PROP29974.
SOURCESearch...

Entry information

Entry nameCNGA1_MOUSE
AccessionPrimary (citable) accession number: P29974
Secondary accession number(s): B9EJ09, Q60776
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot