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Cyclic nucleotide-gated cation channel beta-3 (Cone photoreceptor cGMP-gated channel subunit beta) (Cyclic nucleotide-gated cation channel modulatory subunit) (Cyclic nucleotide-gated channel beta-3) (CNG channel beta-3) (Cyclic nucleotide-gated channel subunit CNG6)

 CNGB3_MOUSE             Reviewed;         694 AA.
Q9JJZ9;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-DEC-2018, entry version 128.
RecName: Full=Cyclic nucleotide-gated cation channel beta-3;
AltName: Full=Cone photoreceptor cGMP-gated channel subunit beta;
AltName: Full=Cyclic nucleotide-gated cation channel modulatory subunit;
AltName: Full=Cyclic nucleotide-gated channel beta-3;
Short=CNG channel beta-3;
AltName: Full=Cyclic nucleotide-gated channel subunit CNG6;
Name=Cngb3; Synonyms=Cng6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=10662822;
Gerstner A., Zong X., Hofmann F., Biel M.;
"Molecular cloning and functional characterization of a new modulatory
cyclic nucleotide-gated channel subunit from mouse retina.";
J. Neurosci. 20:1324-1332(2000).
-!- 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. {ECO:0000250,
ECO:0000269|PubMed:10662822}.
-!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
subunits. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Small subset of retinal photorecptor cells and
testis. {ECO:0000269|PubMed:10662822}.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. CNGB3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ243572; CAB71152.1; -; mRNA.
CCDS; CCDS17990.1; -.
RefSeq; NP_038955.1; NM_013927.2.
UniGene; Mm.445778; -.
ProteinModelPortal; Q9JJZ9; -.
SMR; Q9JJZ9; -.
STRING; 10090.ENSMUSP00000100064; -.
GuidetoPHARMACOLOGY; 399; -.
iPTMnet; Q9JJZ9; -.
PhosphoSitePlus; Q9JJZ9; -.
PaxDb; Q9JJZ9; -.
PeptideAtlas; Q9JJZ9; -.
PRIDE; Q9JJZ9; -.
Ensembl; ENSMUST00000102999; ENSMUSP00000100064; ENSMUSG00000056494.
GeneID; 30952; -.
KEGG; mmu:30952; -.
UCSC; uc008sbx.1; mouse.
CTD; 54714; -.
MGI; MGI:1353562; Cngb3.
eggNOG; KOG0499; Eukaryota.
eggNOG; ENOG410ZJ5U; LUCA.
GeneTree; ENSGT00940000154824; -.
HOGENOM; HOG000231425; -.
HOVERGEN; HBG051038; -.
InParanoid; Q9JJZ9; -.
KO; K04953; -.
OMA; CDIIYLC; -.
OrthoDB; EOG091G03EW; -.
PhylomeDB; Q9JJZ9; -.
TreeFam; TF318250; -.
PRO; PR:Q9JJZ9; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000056494; Expressed in 20 organ(s), highest expression level in pineal body.
CleanEx; MM_CNGB3; -.
Genevisible; Q9JJZ9; MM.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IC:MGI.
GO; GO:1902495; C:transmembrane transporter complex; ISO:MGI.
GO; GO:0030553; F:cGMP binding; ISO:MGI.
GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IPI:MGI.
GO; GO:0006812; P:cation transport; ISO:MGI.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR032943; CNG6.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
PANTHER; PTHR10217:SF385; PTHR10217:SF385; 1.
Pfam; PF00027; cNMP_binding; 1.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS00889; CNMP_BINDING_2; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
1: Evidence at protein level;
cGMP; cGMP-binding; Complete proteome; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
Reference proteome; Sensory transduction; Transmembrane;
Transmembrane helix; Transport; Vision.
CHAIN 1 694 Cyclic nucleotide-gated cation channel
beta-3.
/FTId=PRO_0000219321.
TOPO_DOM 1 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical; Name=H1. {ECO:0000255}.
TOPO_DOM 231 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 263 Helical; Name=H2. {ECO:0000255}.
TOPO_DOM 264 294 Cytoplasmic. {ECO:0000255}.
TRANSMEM 295 315 Helical; Name=H3. {ECO:0000255}.
TOPO_DOM 316 351 Extracellular. {ECO:0000255}.
TRANSMEM 352 372 Helical; Name=H4. {ECO:0000255}.
TOPO_DOM 373 409 Cytoplasmic. {ECO:0000255}.
TRANSMEM 410 430 Helical; Name=H5. {ECO:0000255}.
TOPO_DOM 431 568 Extracellular. {ECO:0000255}.
TRANSMEM 569 589 Helical; Name=H6. {ECO:0000255}.
TOPO_DOM 590 694 Cytoplasmic. {ECO:0000255}.
NP_BIND 524 668 cGMP. {ECO:0000250}.
BINDING 584 584 cGMP. {ECO:0000250}.
BINDING 596 596 cGMP. {ECO:0000250}.
CARBOHYD 507 507 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 694 AA; 79722 MW; 0B9F9CF3B180DA82 CRC64;
MLKSLTVKFN KVNPMEGRME KKLCPNLSSL SQPTIAQGDN QSEKEPLRSR TPITFEKSHS
KEDNSTGENS LRDFTPNPDP ECRAELTRTM AEMEKTRTGK ERPVSFKTKV LETSIINEYT
DAHLHNLVER MRERTALYKK TLTEEENFPE VEASSQTAMS TNISPKQENN SKLKEHQDTF
SFKPQRVPVK EHLRRMILPR SIDSYTDRVY LLWLLLVTIA YNWNCWLLPV RLVFPCQTPD
NKNYWIITDI VCDIIYLCDI LLIQPRLQFV RGGEIIVDSN ELKRNYRSST KFRMDVASLL
PFEVLYIFFG VNPIFRANRI LKYTSFFEFN HHLESIMDKA YVYRVIRTTG YLLFLLHINA
CVYYWASDYE GIGSTKWVYN GEGNKYLRCF YWAVRTLITI GGLPEPQTSF EIVFQFLNFF
SGVFVFSSLI GQMRDVIGAA TANQNYFQAC MDHIIAYMNK YSIPQSVQYR VRTWLEYTWN
SQRILDESNL LENLPTAMQL SIALDINFSI IDKVELFKGC DTQMIYDLLL RLKSTIYLPG
DFVCKKGEIG KEMYIIKHGE VQVLGGPDGA QVLVTLKAGS VFGEISLLAK GGGNRRTADV
VAHGFANLLT LDKKTLQEIL LHYPTSKKLL MKKAKILLSQ KGKTTQAIPA RPGPAFLFPP
KEETPRMLKV LLGNTGKVDL GRLLKGKRKT TTQK


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