CNGA4_RAT
ID CNGA4_RAT Reviewed; 575 AA.
AC Q64359; Q6Q2I4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cyclic nucleotide-gated cation channel alpha-4;
DE AltName: Full=Cyclic nucleotide-gated channel alpha-4;
DE Short=CNG channel alpha-4;
DE Short=CNG-4;
DE Short=CNG4;
DE AltName: Full=Cyclic nucleotide-gated olfactory channel subunit OCNC2;
GN Name=Cnga4; Synonyms=Cgn2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7522325; DOI=10.1073/pnas.91.19.8890;
RA Bradley J., Li J., Davidson N., Lester H.A., Zinn K.;
RT "Heteromeric olfactory cyclic nucleotide-gated channels: a subunit that
RT confers increased sensitivity to cAMP.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8890-8894(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Olfactory neuroepithelium;
RX PubMed=7522482; DOI=10.1016/0896-6273(94)90029-9;
RA Liman E.R., Buck L.B.;
RT "A second subunit of the olfactory cyclic nucleotide-gated channel confers
RT high sensitivity to cAMP.";
RL Neuron 13:611-621(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-191.
RC STRAIN=Sprague-Dawley;
RA Lozach A., Castel H.L.N., Garrel G., Vaudry H., Counis R.;
RT "Characterization and functional expression of cyclic nucleotide-gated
RT channels in rat pituitary gonadotrophs.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-35.
RC STRAIN=Sprague-Dawley;
RA Bradley J., Zhang Y., Bakin R., Lester H.A., Ronnett G., Zinn K.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=15195096; DOI=10.1038/nn1266;
RA Bradley J., Boenigk W., Yau K.-W., Frings S.;
RT "Calmodulin permanently associates with rat olfactory CNG channels under
RT native conditions.";
RL Nat. Neurosci. 7:705-710(2004).
RN [6]
RP SUBUNITS.
RX PubMed=15134638; DOI=10.1016/s0896-6273(04)00253-3;
RA Zheng J., Zagotta W.N.;
RT "Stoichiometry and assembly of olfactory cyclic nucleotide-gated
RT channels.";
RL Neuron 42:411-421(2004).
CC -!- FUNCTION: Second messenger, cAMP, causes the opening of cation-
CC selective cyclic nucleotide-gated (CNG) channels and depolarization of
CC the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory
CC subunit of this channel which is known to play a central role in the
CC transduction of odorant signals and subsequent adaptation. By
CC accelerating the calcium-mediated negative feedback in olfactory
CC signaling it allows rapid adaptation to odor stimulation and extends
CC its range of odor detection (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Calcium-calmodulin exerts its inhibitory effect in
CC cAMP sensitivity by binding to IQ-like motif of CNGA4 and preferably
CC binds to the channel in the closed state. Inhibition by PIP3 of the CNG
CC channel probably occurs via CGNA2 binding.
CC {ECO:0000269|PubMed:15195096}.
CC -!- SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of CNGA4
CC and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG)
CC channel of olfactory sensory neurons. {ECO:0000269|PubMed:15134638}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Olfactory neurons.
CC -!- DOMAIN: The C-terminal coiled-coil domain mediates trimerization of
CC CNGA subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA4 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12623; AAA21464.1; -; mRNA.
DR EMBL; U12425; AAA64748.1; -; mRNA.
DR EMBL; AY564233; AAS87325.1; -; Genomic_DNA.
DR EMBL; U76219; AAC17596.1; -; Genomic_DNA.
DR PIR; I59327; I59327.
DR RefSeq; NP_445948.2; NM_053496.2.
DR AlphaFoldDB; Q64359; -.
DR SMR; Q64359; -.
DR DIP; DIP-61290N; -.
DR IntAct; Q64359; 1.
DR STRING; 10116.ENSRNOP00000023751; -.
DR ChEMBL; CHEMBL4523657; -.
DR PaxDb; Q64359; -.
DR GeneID; 85258; -.
DR KEGG; rno:85258; -.
DR UCSC; RGD:619844; rat.
DR CTD; 1262; -.
DR RGD; 619844; Cnga4.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q64359; -.
DR PhylomeDB; Q64359; -.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q64359; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IDA:RGD.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IDA:RGD.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IDA:RGD.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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:0007608; P:sensory perception of smell; ISO:RGD.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032406; CLZ_dom.
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 Pfam; PF16526; CLZ; 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 2: Evidence at transcript level;
KW cAMP; cAMP-binding; Coiled coil; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Olfaction;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..575
FT /note="Cyclic nucleotide-gated cation channel alpha-4"
FT /id="PRO_0000219322"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 537..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..536
FT /evidence="ECO:0000250"
FT MOTIF 292..302
FT /note="IQ-type"
FT /evidence="ECO:0000250"
FT BINDING 348..471
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 575 AA; 65675 MW; FCF01C563214F575 CRC64;
MSQDGKVKTT ESTPPAPTKA RKWLPVLDPS GDYYYWWLNT MVFPIMYNLI IVVCRACFPD
LQHSYLVAWF VLDYTSDLLY LLDIGVRFHT GFLEQGILVV DKGMIASRYV RTWSFLLDLA
SLVPTDAAYV QLGPHIPTLR LNRFLRVPRL FEAFDRTETR TAYPNAFRIA KLMLYIFVVI
HWNSCLYFAL SRYLGFGRDA WVYPDPAQPG FERLRRQYLY SFYFSTLILT TVGDTPLPDR
EEEYLFMVGD FLLAVMGFAT IMGSMSSVIY NMNTADAAFY PDHALVKKYM KLQHVNKRLE
RRVIDWYQHL QINKKMTNEV AILQHLPERL RAEVAVSVHL STLSRVQIFQ NCEASLLEEL
VLKLQPQTYS PGEYVCRKGD IGREMYIIRE GQLAVVADDG VTQYAVLGAG LYFGEISIIN
IKGNMSGNRR TANIKSLGYS DLFCLSKEDL REVLSEYPQA QAVMEEKGRE ILLKMNKLDV
NAEAAEIALQ EATESRLKGL DQQLDDLQTK FARLLAELES SALKIAYRIE RLEWQTREWP
MPEDMGEADD EAEPGEGTSK DGEGKAGQAG PSGIE
