CNGB3_CANLF
ID CNGB3_CANLF Reviewed; 782 AA.
AC Q8MJD7; Q1G1Y4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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;
GN Name=CNGB3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CD ASN-262.
RX PubMed=12140185; DOI=10.1093/hmg/11.16.1823;
RA Sidjanin D.J., Lowe J.K., McElwee J.L., Milne B.S., Phippen T.M.,
RA Sargan D.R., Aguirre G.D., Acland G.M., Ostrander E.A.;
RT "Canine CNGB3 mutations establish cone degeneration as orthologous to the
RT human achromatopsia locus ACHM3.";
RL Hum. Mol. Genet. 11:1823-1833(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Alaskan malamute;
RX PubMed=16879359; DOI=10.1111/j.1365-2052.2006.01484.x;
RA Seddon J.M., Hampson E.C.G.M., Smith R.I.E., Hughes I.P.;
RT "Genetic heterogeneity of day blindness in Alaskan Malamutes.";
RL Anim. Genet. 37:407-410(2006).
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. Induced a flickering
CC channel 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 Essential for the generation of light-evoked electrical responses in
CC the red-, green- and blue sensitive cones (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DISEASE: Note=Defects in CNGB3 are a cause of cone degeneration (cd).
CC Cd is characterized by day-blindness and absence of retinal cone
CC function. This autosomal recessive disorder occurs naturally in the
CC Alaskan Malamute and German Shorthaired Pointer breeds.
CC {ECO:0000269|PubMed:12140185, ECO:0000269|PubMed:16879359}.
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; AF490511; AAM89224.1; -; mRNA.
DR EMBL; DQ497639; ABF58779.1; -; Genomic_DNA.
DR RefSeq; NP_001003030.1; NM_001003030.1.
DR AlphaFoldDB; Q8MJD7; -.
DR SMR; Q8MJD7; -.
DR STRING; 9615.ENSCAFP00000013075; -.
DR PaxDb; Q8MJD7; -.
DR Ensembl; ENSCAFT00030046500; ENSCAFP00030040639; ENSCAFG00030025193.
DR Ensembl; ENSCAFT00040041525; ENSCAFP00040036223; ENSCAFG00040022330.
DR GeneID; 403554; -.
DR KEGG; cfa:403554; -.
DR CTD; 54714; -.
DR eggNOG; KOG0499; Eukaryota.
DR InParanoid; Q8MJD7; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
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; IBA:GO_Central.
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: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; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF8; PTHR45638:SF8; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 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; Disease variant; 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..782
FT /note="Cyclic nucleotide-gated cation channel beta-3"
FT /id="PRO_0000219319"
FT TOPO_DOM 1..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..412
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..572
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527..671
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT VARIANT 262
FT /note="D -> N (in cd; in a German Shorthaired Pointer)"
FT /evidence="ECO:0000269|PubMed:12140185"
SQ SEQUENCE 782 AA; 89424 MW; 7139EF3B86268A79 CRC64;
MFKSLTIKSN KVKPREENDE NKQDPDPSNQ PQQSTRQGEN KSENKSLQTK MTPVTFEESH
AKMQDKISEK NSLRDLTTNP NHQHPTESKG AMSEQKEMET GKEGLVSPKS KPLGVPVINE
YADAQLHNLV RRMRQRTMLY KKKLAEGDIS SPEASPQTAK PTAVPSTQES NAKLKEEHYY
HILCFKFQKM PLTEYLKRFR LPGSIDSYTD RLYLLWLLLV TIAYNWNCWL IPLRLVFPYQ
TPDNTHYWFI TDITCDIIYL CDMLLIQPRL QFIKGGDIMV DSNELKRHYR SSTKFQLDVA
SVMPFDVFYL FFGFNPVFRM NRILKYTSFF EFNHHLESIM DKAYIYRVIR TTGYLLYTLH
INACIYYWAS DYEGIGSTKW VYNGEGNKYL RCYYWAVRTL ITIGGLPEPQ TSFEIVFQLL
NFFSGVFVFS SLIGQMQDVI GAATANQNNF RISMDHTISY MNTYSIPKNV QNRVRTWYEY
TWDSQRMLDE SDLLCTLPVT MQLALTVDVN LSIISKVELF KGCDTQMIYD MLLRLKSTVY
LPGDFVCKKG EIGKEMYIIK QGEVQVLGGS DGAQVLVTLK AGAVFGEISL LAGRGGNRRT
ANVIAHGFAN LLTLDKKTLQ EILVHYPDSE KLLMKKASVL LKKKAPATET TPPRKGLAFL
FPPKQETPKI FKALLGGTGK AGLTRLLKLK REQTIQKTSE NSEEGGGKRR EYEDKEREPS
EKILDSSECR ANCIIAEEMP QSIRRAALPR GTTRQSLIIS MAPSAEAGEE VLTIEVKEKA
KQ
