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Protein

Cyclic nucleotide-gated olfactory channel

Gene

Cnga2

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

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei523cAMPSequence analysis1
Binding sitei538cAMPSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi464 – 586cAMPBy similarityAdd BLAST123

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • cGMP binding Source: RGD
  • intracellular cAMP activated cation channel activity Source: RGD
  • intracellular cGMP activated cation channel activity Source: RGD
  • voltage-gated potassium channel activity Source: GO_Central

GO - Biological processi

  • membrane depolarization Source: RGD
  • protein heterotetramerization Source: RGD
  • protein homotetramerization Source: RGD
  • response to stimulus Source: UniProtKB-KW
  • sensory perception of smell Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel

Keywords - Biological processi

Ion transport, Olfaction, Sensory transduction, Transport

Keywords - Ligandi

Calmodulin-binding, cAMP, cAMP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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
Cyclic nucleotide-gated olfactory channel subunit OCNC1
Gene namesi
Name:Cnga2
Synonyms:Cncg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2367. Cnga2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 142CytoplasmicSequence analysisAdd BLAST142
Transmembranei143 – 162Helical; Name=H1Sequence analysisAdd BLAST20
Topological domaini163 – 175ExtracellularSequence analysisAdd BLAST13
Transmembranei176 – 194Helical; Name=H2Sequence analysisAdd BLAST19
Topological domaini195 – 218CytoplasmicSequence analysisAdd BLAST24
Transmembranei219 – 238Helical; Name=H3Sequence analysisAdd BLAST20
Topological domaini239 – 276ExtracellularSequence analysisAdd BLAST38
Transmembranei277 – 299Helical; Name=H4Sequence analysisAdd BLAST23
Topological domaini300 – 351CytoplasmicSequence analysisAdd BLAST52
Transmembranei352 – 371Helical; Name=H5Sequence analysisAdd BLAST20
Topological domaini372 – 455ExtracellularSequence analysisAdd BLAST84
Transmembranei456 – 476Helical; Name=H6Sequence analysisAdd BLAST21
Topological domaini477 – 664CytoplasmicSequence analysisAdd BLAST188

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • intracellular cyclic nucleotide activated cation channel complex Source: RGD
  • perikaryon Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi395.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002193151 – 664Cyclic nucleotide-gated olfactory channelAdd BLAST664

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ00195.
PRIDEiQ00195.

Expressioni

Tissue specificityi

Olfactory neurons.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

DIPiDIP-61291N.
STRINGi10116.ENSRNOP00000016415.

Structurei

Secondary structure

1664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi62 – 64Combined sources3
Helixi66 – 82Combined sources17
Turni83 – 85Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M0JNMR-B60-87[»]
2M0KNMR-B60-87[»]
ProteinModelPortaliQ00195.
SMRiQ00195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili599 – 642By similarityAdd BLAST44

Domaini

The C-terminal coiled-coil domain mediates trimerization 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.
InParanoidiQ00195.
KOiK04949.
PhylomeDBiQ00195.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR018490. 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]
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
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.

Q00195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTEKSNGVK SSPANNHNHH PPPSIKANGK DDHRAGSRPQ SVAADDDTSP
60 70 80 90 100
ELQRLAEMDT PRRGRGGFQR IVRLVGVIRD WANKNFREEE PRPDSFLERF
110 120 130 140 150
RGPELQTVTT HQGDDKGGKD GEGKGTKKKF ELFVLDPAGD WYYRWLFVIA
160 170 180 190 200
MPVLYNWCLL VARACFSDLQ RNYFVVWLVL DYFSDTVYIA DLIIRLRTGF
210 220 230 240 250
LEQGLLVKDP KKLRDNYIHT LQFKLDVASI IPTDLIYFAV GIHSPEVRFN
260 270 280 290 300
RLLHFARMFE FFDRTETRTS YPNIFRISNL VLYILVIIHW NACIYYVISK
310 320 330 340 350
SIGFGVDTWV YPNITDPEYG YLAREYIYCL YWSTLTLTTI GETPPPVKDE
360 370 380 390 400
EYLFVIFDFL IGVLIFATIV GNVGSMISNM NATRAEFQAK IDAVKHYMQF
410 420 430 440 450
RKVSKDMEAK VIKWFDYLWT NKKTVDEREV LKNLPAKLRA EIAINVHLST
460 470 480 490 500
LKKVRIFQDC EAGLLVELVL KLRPQVFSPG DYICRKGDIG KEMYIIKEGK
510 520 530 540 550
LAVVADDGVT QYALLSAGSC FGEISILNIK GSKMGNRRTA NIRSLGYSDL
560 570 580 590 600
FCLSKDDLME AVTEYPDAKK VLEERGREIL MKEGLLDENE VAASMEVDVQ
610 620 630 640 650
EKLEQLETNM DTLYTRFARL LAEYTGAQQK LKQRITVLET KMKQNHEDDY
660
LSDGINTPEP TAAE
Length:664
Mass (Da):76,177
Last modified:December 1, 1992 - v1
Checksum:i720806950EC27F3C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti212K → R.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55519 mRNA. Translation: CAA39135.1.
AF126808 mRNA. Translation: AAD41473.1.
PIRiS11517.
RefSeqiNP_037060.1. NM_012928.1.
XP_017455916.1. XM_017600427.1.
UniGeneiRn.10384.

Genome annotation databases

GeneIDi108348053.
25411.
KEGGirno:25411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55519 mRNA. Translation: CAA39135.1.
AF126808 mRNA. Translation: AAD41473.1.
PIRiS11517.
RefSeqiNP_037060.1. NM_012928.1.
XP_017455916.1. XM_017600427.1.
UniGeneiRn.10384.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M0JNMR-B60-87[»]
2M0KNMR-B60-87[»]
ProteinModelPortaliQ00195.
SMRiQ00195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61291N.
STRINGi10116.ENSRNOP00000016415.

Chemistry databases

GuidetoPHARMACOLOGYi395.

Proteomic databases

PaxDbiQ00195.
PRIDEiQ00195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi108348053.
25411.
KEGGirno:25411.

Organism-specific databases

CTDi1260.
RGDi2367. Cnga2.

Phylogenomic databases

eggNOGiKOG0500. Eukaryota.
ENOG410YWWI. LUCA.
HOGENOMiHOG000007898.
HOVERGENiHBG000281.
InParanoidiQ00195.
KOiK04949.
PhylomeDBiQ00195.

Miscellaneous databases

PROiQ00195.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR032406. CLZ_dom.
IPR018490. 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]
PfamiPF16526. CLZ. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
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...

Entry informationi

Entry nameiCNGA2_RAT
AccessioniPrimary (citable) accession number: Q00195
Secondary accession number(s): Q549G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.