GenomeNet

Database: UniProt
Entry: CNGA4_RAT
LinkDB: CNGA4_RAT
Original site: 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   22-NOV-2017, entry version 123.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   that 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
RT   confers 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   ENZYME 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
RT   under 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
CC       depolarization of the neuron (olfactory sensory neurons, OSNs).
CC       CNGA4 is the modulatory subunit of this channel which is known to
CC       play a central role in the transduction of odorant signals and
CC       subsequent adaptation. By accelerating the calcium-mediated
CC       negative feedback in olfactory signaling it allows rapid
CC       adaptation to odor stimulation and extends its range of odor
CC       detection (By similarity). {ECO:0000250}.
CC   -!- ENZYME REGULATION: Calcium-calmodulin exerts its inhibitory effect
CC       in cAMP sensitivity by binding to IQ-like motif of CNGA4 and
CC       preferably binds to the channel in the closed state. Inhibition by
CC       PIP3 of the CNG channel probably occurs via CGNA2 binding.
CC       {ECO:0000269|PubMed:15195096}.
CC   -!- SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of
CC       CNGA4 and one of CNGB1b. The complex forms the cyclic nucleotide-
CC       gated (CNG) channel of olfactory sensory neurons.
CC       {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
CC       of CNGA subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. CNGA4 subfamily. {ECO:0000305}.
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   UniGene; Rn.91104; -.
DR   ProteinModelPortal; Q64359; -.
DR   SMR; Q64359; -.
DR   DIP; DIP-61290N; -.
DR   IntAct; Q64359; 1.
DR   STRING; 10116.ENSRNOP00000023751; -.
DR   PaxDb; Q64359; -.
DR   PRIDE; 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   eggNOG; ENOG410YWWI; LUCA.
DR   HOGENOM; HOG000007898; -.
DR   HOVERGEN; HBG000281; -.
DR   InParanoid; Q64359; -.
DR   KO; K04951; -.
DR   PhylomeDB; Q64359; -.
DR   PRO; PR:Q64359; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0051290; P:protein heterotetramerization; IDA:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; 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; Complete proteome; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Olfaction; Reference proteome; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    575       Cyclic nucleotide-gated cation channel
FT                                alpha-4.
FT                                /FTId=PRO_0000219322.
FT   TOPO_DOM      1     33       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     34     54       Helical; Name=H1. {ECO:0000255}.
FT   TOPO_DOM     55     65       Extracellular. {ECO:0000255}.
FT   TRANSMEM     66     86       Helical; Name=H2. {ECO:0000255}.
FT   TOPO_DOM     87    112       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    113    133       Helical; Name=H3. {ECO:0000255}.
FT   TOPO_DOM    134    168       Extracellular. {ECO:0000255}.
FT   TRANSMEM    169    189       Helical; Name=H4. {ECO:0000255}.
FT   TOPO_DOM    190    218       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    219    239       Helical; Name=H5. {ECO:0000255}.
FT   TOPO_DOM    240    244       Extracellular. {ECO:0000255}.
FT   TRANSMEM    245    265       Helical; Name=H6. {ECO:0000255}.
FT   TOPO_DOM    266    575       Cytoplasmic. {ECO:0000255}.
FT   NP_BIND     348    471       cNMP.
FT   COILED      493    536       {ECO:0000250}.
FT   MOTIF       292    302       IQ-type. {ECO:0000250}.
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
//
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