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Q9JJZ9 (CNGB3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 76. 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 cation channel beta-3
Alternative name(s):
Cone photoreceptor cGMP-gated channel subunit beta
Cyclic nucleotide-gated cation channel modulatory subunit
Cyclic nucleotide-gated channel beta-3
Short name=CNG channel beta-3
Cyclic nucleotide-gated channel subunit CNG6
Gene names
Name:Cngb3
Synonyms:Cng6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones By similarity. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGA3. Ref.1

Subunit structure

Heterooligomeric complex with CNGA3. Ref.1

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Small subset of retinal photorecptor cells and testis. Ref.1

Sequence similarities

Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGB3 subfamily. [View classification]

Contains 1 cyclic nucleotide-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694Cyclic nucleotide-gated cation channel beta-3
PRO_0000219321

Regions

Topological domain1 – 209209Cytoplasmic Potential
Transmembrane210 – 23021Helical; Name=H1; Potential
Topological domain231 – 24212Extracellular Potential
Transmembrane243 – 26321Helical; Name=H2; Potential
Topological domain264 – 29431Cytoplasmic Potential
Transmembrane295 – 31521Helical; Name=H3; Potential
Topological domain316 – 35136Extracellular Potential
Transmembrane352 – 37221Helical; Name=H4; Potential
Topological domain373 – 40937Cytoplasmic Potential
Transmembrane410 – 43021Helical; Name=H5; Potential
Topological domain431 – 568138Extracellular Potential
Transmembrane569 – 58921Helical; Name=H6; Potential
Topological domain590 – 694105Cytoplasmic Potential
Nucleotide binding524 – 668145cGMP By similarity

Sites

Binding site5841cGMP By similarity
Binding site5961cGMP By similarity

Amino acid modifications

Glycosylation5071N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9JJZ9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0B9F9CF3B180DA82

FASTA69479,722
        10         20         30         40         50         60 
MLKSLTVKFN KVNPMEGRME KKLCPNLSSL SQPTIAQGDN QSEKEPLRSR TPITFEKSHS 

        70         80         90        100        110        120 
KEDNSTGENS LRDFTPNPDP ECRAELTRTM AEMEKTRTGK ERPVSFKTKV LETSIINEYT 

       130        140        150        160        170        180 
DAHLHNLVER MRERTALYKK TLTEEENFPE VEASSQTAMS TNISPKQENN SKLKEHQDTF 

       190        200        210        220        230        240 
SFKPQRVPVK EHLRRMILPR SIDSYTDRVY LLWLLLVTIA YNWNCWLLPV RLVFPCQTPD 

       250        260        270        280        290        300 
NKNYWIITDI VCDIIYLCDI LLIQPRLQFV RGGEIIVDSN ELKRNYRSST KFRMDVASLL 

       310        320        330        340        350        360 
PFEVLYIFFG VNPIFRANRI LKYTSFFEFN HHLESIMDKA YVYRVIRTTG YLLFLLHINA 

       370        380        390        400        410        420 
CVYYWASDYE GIGSTKWVYN GEGNKYLRCF YWAVRTLITI GGLPEPQTSF EIVFQFLNFF 

       430        440        450        460        470        480 
SGVFVFSSLI GQMRDVIGAA TANQNYFQAC MDHIIAYMNK YSIPQSVQYR VRTWLEYTWN 

       490        500        510        520        530        540 
SQRILDESNL LENLPTAMQL SIALDINFSI IDKVELFKGC DTQMIYDLLL RLKSTIYLPG 

       550        560        570        580        590        600 
DFVCKKGEIG KEMYIIKHGE VQVLGGPDGA QVLVTLKAGS VFGEISLLAK GGGNRRTADV 

       610        620        630        640        650        660 
VAHGFANLLT LDKKTLQEIL LHYPTSKKLL MKKAKILLSQ KGKTTQAIPA RPGPAFLFPP 

       670        680        690 
KEETPRMLKV LLGNTGKVDL GRLLKGKRKT TTQK 

« Hide

References

[1]"Molecular cloning and functional characterization of a new modulatory cyclic nucleotide-gated channel subunit from mouse retina."
Gerstner A., Zong X., Hofmann F., Biel M.
J. Neurosci. 20:1324-1332(2000) [PubMed: 10662822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243572 mRNA. Translation: CAB71152.1.
IPIIPI00875084.
RefSeqNP_038955.1. NM_013927.2.
UniGeneMm.445778.

3D structure databases

ProteinModelPortalQ9JJZ9.
SMRQ9JJZ9. Positions 347-437, 441-643.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JJZ9.

PTM databases

PhosphoSiteQ9JJZ9.

Proteomic databases

PRIDEQ9JJZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102999; ENSMUSP00000100064; ENSMUSG00000056494.
GeneID30952.
KEGGmmu:30952.

Organism-specific databases

CTD54714.
MGIMGI:1353562. Cngb3.

Phylogenomic databases

GeneTreeENSGT00550000074376.
HOGENOMHBG445757.
HOVERGENHBG051038.
InParanoidQ9JJZ9.
OrthoDBEOG4FJ887.

Gene expression databases

ArrayExpressQ9JJZ9.
BgeeQ9JJZ9.
CleanExMM_CNGB3.
GenevestigatorQ9JJZ9.

Family and domain databases

InterProIPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KOK04953.
PfamPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF51206. cNMP_binding. 1 hit.
PROSITEPS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 1 hit.
PS50042. CNMP_BINDING_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307424.
SOURCESearch...

Entry information

Entry nameCNGB3_MOUSE
AccessionPrimary (citable) accession number: Q9JJZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2000
Last modified: December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families