CNGB3_MOUSE
ID CNGB3_MOUSE Reviewed; 694 AA.
AC Q9JJZ9;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cyclic nucleotide-gated cation channel beta-3;
DE AltName: Full=Cone photoreceptor cGMP-gated channel subunit beta;
DE AltName: Full=Cyclic nucleotide-gated cation channel modulatory subunit;
DE AltName: Full=Cyclic nucleotide-gated channel beta-3;
DE Short=CNG channel beta-3;
DE AltName: Full=Cyclic nucleotide-gated channel subunit CNG6;
GN Name=Cngb3; Synonyms=Cng6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=10662822; DOI=10.1523/jneurosci.20-04-01324.2000;
RA Gerstner A., Zong X., Hofmann F., Biel M.;
RT "Molecular cloning and functional characterization of a new modulatory
RT cyclic nucleotide-gated channel subunit from mouse retina.";
RL J. Neurosci. 20:1324-1332(2000).
CC -!- FUNCTION: Visual signal transduction is mediated by a G-protein coupled
CC cascade using cGMP as second messenger. This protein can be activated
CC by cGMP which leads to an opening of the cation channel and thereby
CC causing a depolarization of rod photoreceptors. Essential for the
CC generation of light-evoked electrical responses in the red-, green- and
CC blue sensitive cones (By similarity). Induced a flickering channel
CC gating, weakened the outward rectification in the presence of
CC extracellular calcium, increased sensitivity for L-cis diltiazem and
CC enhanced the cAMP efficacy of the channel when coexpressed with CNGA3.
CC {ECO:0000250, ECO:0000269|PubMed:10662822}.
CC -!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Small subset of retinal photoreceptor cells and
CC testis. {ECO:0000269|PubMed:10662822}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGB3 subfamily. {ECO:0000305}.
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DR EMBL; AJ243572; CAB71152.1; -; mRNA.
DR CCDS; CCDS17990.1; -.
DR RefSeq; NP_038955.1; NM_013927.2.
DR AlphaFoldDB; Q9JJZ9; -.
DR SMR; Q9JJZ9; -.
DR STRING; 10090.ENSMUSP00000100064; -.
DR GuidetoPHARMACOLOGY; 399; -.
DR GlyGen; Q9JJZ9; 1 site.
DR iPTMnet; Q9JJZ9; -.
DR PhosphoSitePlus; Q9JJZ9; -.
DR PaxDb; Q9JJZ9; -.
DR PeptideAtlas; Q9JJZ9; -.
DR PRIDE; Q9JJZ9; -.
DR ProteomicsDB; 285508; -.
DR Antibodypedia; 59091; 122 antibodies from 24 providers.
DR DNASU; 30952; -.
DR Ensembl; ENSMUST00000102999; ENSMUSP00000100064; ENSMUSG00000056494.
DR GeneID; 30952; -.
DR KEGG; mmu:30952; -.
DR UCSC; uc008sbx.1; mouse.
DR CTD; 54714; -.
DR MGI; MGI:1353562; Cngb3.
DR VEuPathDB; HostDB:ENSMUSG00000056494; -.
DR eggNOG; KOG0499; Eukaryota.
DR GeneTree; ENSGT00940000154824; -.
DR HOGENOM; CLU_005746_11_1_1; -.
DR InParanoid; Q9JJZ9; -.
DR OMA; RTWFEYT; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q9JJZ9; -.
DR TreeFam; TF318250; -.
DR BioGRID-ORCS; 30952; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9JJZ9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJZ9; protein.
DR Bgee; ENSMUSG00000056494; Expressed in pineal body and 16 other tissues.
DR Genevisible; Q9JJZ9; MM.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; ISO:MGI.
DR GO; GO:0030553; F:cGMP binding; ISO:MGI.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032943; CNG6.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF8; PTHR45638:SF8; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW cGMP; cGMP-binding; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1..694
FT /note="Cyclic nucleotide-gated cation channel beta-3"
FT /id="PRO_0000219321"
FT TOPO_DOM 1..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..351
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..694
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 24..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 524..668
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
