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Q16280 (CNGA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Cyclic nucleotide-gated olfactory channel
Alternative name(s):
Cyclic nucleotide-gated cation channel 2
Cyclic nucleotide-gated channel alpha-2
Short name=CNG channel alpha-2
Short name=CNG-2
Short name=CNG2
Gene names
Name:CNGA2
Synonyms:CNCA, CNCA1, CNCG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.

Subunit structure

Heterotetramer composed of two subunits of CNGA2, one of CNGA4 and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG) channel of olfactory sensory neurons By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

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

Sequence similarities

Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGA2 subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Cyclic nucleotide-gated olfactory channel
PRO_0000219312

Regions

Topological domain1 – 138138Cytoplasmic Potential
Transmembrane139 – 15921Helical; Name=H1; Potential
Topological domain160 – 17112Extracellular Potential
Transmembrane172 – 19221Helical; Name=H2; Potential
Topological domain193 – 22432Cytoplasmic Potential
Transmembrane225 – 24521Helical; Name=H3; Potential
Topological domain246 – 27429Extracellular Potential
Transmembrane275 – 29521Helical; Name=H4; Potential
Topological domain296 – 35055Cytoplasmic Potential
Transmembrane351 – 37121Helical; Name=H5; Potential
Topological domain372 – 45382Extracellular Potential
Transmembrane454 – 47421Helical; Name=H6; Potential
Topological domain475 – 662188Cytoplasmic Potential
Nucleotide binding454 – 577124cAMP By similarity
Coiled coil597 – 64044 By similarity

Sites

Binding site5211cAMP By similarity
Binding site5361cAMP By similarity

Amino acid modifications

Glycosylation3791N-linked (GlcNAc...) Potential

Natural variations

Natural variant971R → H in a breast cancer sample; somatic mutation. Ref.3
VAR_036603
Natural variant1181D → H.
Corresponds to variant rs6627455 [ dbSNP | Ensembl ].
VAR_048748
Natural variant1391W → L.
Corresponds to variant rs35350051 [ dbSNP | Ensembl ].
VAR_061107
Natural variant3991R → Q in a breast cancer sample; somatic mutation. Ref.3
VAR_036604
Natural variant6631E → K.
Corresponds to variant rs714147 [ dbSNP | Ensembl ].
VAR_048749

Sequences

Sequence LengthMass (Da)Tools
Q16280 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: E8FB934468429CE5

FASTA66476,048
        10         20         30         40         50         60 
MTEKTNGVKS SPANNHNHHA PPAIKANGKD DHRTSSRPHS AADDDTSSEL QRLADVDAPQ 

        70         80         90        100        110        120 
QGRSGFRRIV RLVGIIREWA NKNFREEEPR PDSFLERFRG PELQTVTTQE GDGKGDKDGE 

       130        140        150        160        170        180 
DKGTKKKFEL FVLDPAGDWY YCWLFVIAMP VLYNWCLLVA RACFSDLQKG YYLVWLVLDY 

       190        200        210        220        230        240 
VSDVVYIADL FIRLRTGFLE QGLLVKDTKK LRDNYIHTLQ FKLDVASIIP TDLIYFAVDI 

       250        260        270        280        290        300 
HSPEVRFNRL LHFARMFEFF DRTETRTNYP NIFRISNLVL YILVIIHWNA CIYYAISKSI 

       310        320        330        340        350        360 
GFGVDTWVYP NITDPEYGYL AREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG 

       370        380        390        400        410        420 
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKGMEAKVI RWFDYLWTNK 

       430        440        450        460        470        480 
KTVDEREILK NLPAKLRAEI AINVHLSTLK KVRIFHDCEA GLLVELVLKL RPQVFSPGDY 

       490        500        510        520        530        540 
ICRKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI 

       550        560        570        580        590        600 
RSLGYSDLFC LSKDDLMEAV TEYPDAKKVL EERGREILMK EGLLDENEVA TSMEVDVQEK 

       610        620        630        640        650        660 
LGQLETNMET LYTRFGRLLA EYTGAQQKLK QRITVLETKM KQNNEDDYLS DGMNSPELAA 


ADEP 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells."
Distler M., Biel M., Flockerzi V., Hofmann F.
Neuropharmacology 33:1275-1282(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-552.
[3]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-97 AND GLN-399.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC126302 mRNA. Translation: AAI26303.1.
BC126304 mRNA. Translation: AAI26305.1.
S76067 Genomic DNA. Translation: AAD14207.1.
PIRI78559.
RefSeqNP_005131.1. NM_005140.1.
UniGeneHs.447360.

3D structure databases

ProteinModelPortalQ16280.
SMRQ16280. Positions 59-85, 277-373, 381-571, 597-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000328478.

Chemistry

ChEMBLCHEMBL1628471.

PTM databases

PhosphoSiteQ16280.

Polymorphism databases

DMDM119370323.

Proteomic databases

PaxDbQ16280.
PRIDEQ16280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329903; ENSP00000328478; ENSG00000183862.
GeneID1260.
KEGGhsa:1260.
UCSCuc004fey.1. human.

Organism-specific databases

CTD1260.
GeneCardsGC0XP150904.
HGNCHGNC:2149. CNGA2.
HPAHPA015065.
MIM300338. gene.
neXtProtNX_Q16280.
PharmGKBPA26659.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300025.
HOGENOMHOG000007898.
HOVERGENHBG000281.
InParanoidQ16280.
KOK04949.
OMAHYMHFRK.
OrthoDBEOG771268.
PhylomeDBQ16280.
TreeFamTF319048.

Gene expression databases

CleanExHS_CNGA2.
GenevestigatorQ16280.

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

GeneWikiCyclic_nucleotide-gated_channel_alpha_2.
GenomeRNAi1260.
NextBio5097.
PROQ16280.
SOURCESearch...

Entry information

Entry nameCNGA2_HUMAN
AccessionPrimary (citable) accession number: Q16280
Secondary accession number(s): A0AVD0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM