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Q62398 (CNGA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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:
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:Cncg2, Cncg4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Ontologies

Keywords
   Biological processIon transport
Olfaction
Sensory transduction
Transport
   Cellular componentMembrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandCalmodulin-binding
cAMP
cAMP-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

sensory perception of smell

Inferred from mutant phenotype PubMed 10798394PubMed 21516098. Source: MGI

   Cellular_componentintegral component of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functioncAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cGMP 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

ion channel activity

Inferred from mutant phenotype PubMed 10798394. Source: MGI

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 – 664664Cyclic nucleotide-gated olfactory channel
PRO_0000219313

Regions

Topological domain1 – 142142Cytoplasmic Potential
Transmembrane143 – 16321Helical; Name=H1; Potential
Topological domain164 – 17512Extracellular Potential
Transmembrane176 – 19419Helical; Name=H2; Potential
Topological domain195 – 21824Cytoplasmic Potential
Transmembrane219 – 23820Helical; Name=H3; Potential
Topological domain239 – 27638Extracellular Potential
Transmembrane277 – 29923Helical; Name=H4; Potential
Topological domain300 – 35152Cytoplasmic Potential
Transmembrane352 – 37120Helical; Name=H5; Potential
Topological domain372 – 45584Extracellular Potential
Transmembrane456 – 47621Helical; Name=H6; Potential
Topological domain477 – 664188Cytoplasmic Potential
Nucleotide binding464 – 586123cAMP By similarity
Coiled coil599 – 64244 By similarity

Sites

Binding site5231cAMP Potential
Binding site5381cAMP Potential

Amino acid modifications

Glycosylation3811N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1101T → P in AAC52712. Ref.1
Sequence conflict3551V → F in AAC52712. Ref.1
Sequence conflict540 – 5412AN → GT in AAC52712. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62398 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 34F8DF3B372C0D9C

FASTA66476,193
        10         20         30         40         50         60 
MMTEKSNGVK SSPANNHNHH PPPSIKANGK DDHRAGSRPQ SVAADDDTSS ELQRLAEMDT 

        70         80         90        100        110        120 
PRRGRGGFRR IVRLVGIIRD WANKNFREEE PRPDSFLERF RGPELQTVTT HQGDGKGDKD 

       130        140        150        160        170        180 
GEGKGTKKKF ELFVLDPAGD WYYRWLFVIA MPVLYNWCLL VARACFSDLQ RNYFVVWLVL 

       190        200        210        220        230        240 
DYFSDTVYIA DLIIRLRTGF LEQGLLVKDP KKLRDNYIHT LQFKLDVASI IPTDLIYFAV 

       250        260        270        280        290        300 
GIHSPEVRFN RLLHFARMFE FFDRTETRTS YPNIFRISNL VLYILVIIHW NACIYYAISK 

       310        320        330        340        350        360 
SIGFGVDTWV YPNITDPEYG YLAREYIYCL YWSTLTLTTI GETPPPVKDE EYLFVIFDFL 

       370        380        390        400        410        420 
IGVLIFATIV GNVGSMISNM NATRAEFQAK IDAVKHYMQF RKVSKDMEAK VIKWFDYLWT 

       430        440        450        460        470        480 
NKKTVDEREV LKNLPAKLRA EIAINVHLST LKKVRIFQDC EAGLLVELVL KLRPQVFSPG 

       490        500        510        520        530        540 
DYICRKGDIG KEMYIIKEGK LAVVADDGVT QYALLSAGSC FGEISILNIK GSKMGNRRTA 

       550        560        570        580        590        600 
NIRSLGYSDL FCLSKDDLME AVTEYPDAKK VLEERGREIL MKEGLLDENE VAASMEVDVQ 

       610        620        630        640        650        660 
EKLEQLETNM ETLYTRFARL LAEYTGAQQK LKQRITVLET KMKQNHEDDY LSDGINTPEP 


AVAE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of an olfactory cyclic nucleotide-gated channel expressed in mouse heart."
Ruiz M.L., London B., Nadal-Ginard B.
J. Mol. Cell. Cardiol. 28:1453-1461(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Heart.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Olfactory epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49391 Genomic DNA. Translation: AAC52712.1.
AK132574 mRNA. Translation: BAE21237.1.
CH466624 Genomic DNA. Translation: EDL26564.1.
BC048775 mRNA. Translation: AAH48775.1.
CCDSCCDS30184.1.
RefSeqNP_031750.2. NM_007724.2.
XP_006527824.1. XM_006527761.1.
XP_006527825.1. XM_006527762.1.
UniGeneMm.5097.

3D structure databases

ProteinModelPortalQ62398.
SMRQ62398. Positions 60-87, 325-573, 599-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000006020.

Protein family/group databases

TCDB1.A.1.5.4. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ62398.

Proteomic databases

PRIDEQ62398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006020; ENSMUSP00000006020; ENSMUSG00000005864.
GeneID12789.
KEGGmmu:12789.
UCSCuc009tkk.1. mouse.

Organism-specific databases

CTD1260.
MGIMGI:108040. Cnga2.

Phylogenomic databases

eggNOGNOG300025.
GeneTreeENSGT00550000074376.
HOGENOMHOG000007898.
HOVERGENHBG000281.
InParanoidQ80XH6.
KOK04949.
OMAYLSDGMN.
OrthoDBEOG771268.
TreeFamTF319048.

Gene expression databases

BgeeQ62398.
CleanExMM_CNGA2.
GenevestigatorQ62398.

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.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01463. EAGCHANLFMLY.
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

NextBio282190.
PROQ62398.
SOURCESearch...

Entry information

Entry nameCNGA2_MOUSE
AccessionPrimary (citable) accession number: Q62398
Secondary accession number(s): Q80XH6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 119 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