CNGA2_BOVIN
ID CNGA2_BOVIN Reviewed; 663 AA.
AC Q03041;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cyclic nucleotide-gated olfactory channel;
DE AltName: Full=Cyclic nucleotide-gated cation channel 2;
DE AltName: Full=Cyclic nucleotide-gated channel alpha-2;
DE Short=CNG channel alpha-2;
DE Short=CNG-2;
DE Short=CNG2;
GN Name=CNGA2; Synonyms=CNCG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=1699793; DOI=10.1016/0014-5793(90)81226-e;
RA Ludwig J., Margalit T., Eismann E., Lancet D., Kaupp U.B.;
RT "Primary structure of cAMP-gated channel from bovine olfactory
RT epithelium.";
RL FEBS Lett. 270:24-29(1990).
RN [2]
RP STRUCTURE BY NMR OF 60-85 IN COMPLEX WITH CALMODULIN.
RX PubMed=15803393; DOI=10.1007/s10858-005-0165-1;
RA Contessa G.M., Orsale M., Melino S., Torre V., Paci M., Desideri A.,
RA Cicero D.O.;
RT "Structure of calmodulin complexed with an olfactory CNG channel fragment
RT and role of the central linker: residual dipolar couplings to evaluate
RT calmodulin binding modes outside the kinase family.";
RL J. Biomol. NMR 31:185-199(2005).
CC -!- FUNCTION: Odorant signal transduction is probably mediated by a G-
CC protein coupled cascade using cAMP as second messenger. The olfactory
CC channel can be shown to be activated by cyclic nucleotides which leads
CC to a depolarization of olfactory sensory neurons.
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 (By similarity). {ECO:0000250}.
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 -!- MISCELLANEOUS: The olfactory channel is activated by both cAMP and cGMP
CC at similar concentrations, whereas the cGMP-gated channel is much less
CC sensitive to cAMP.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA2 subfamily. {ECO:0000305}.
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DR EMBL; X55010; CAA38754.1; -; mRNA.
DR PIR; S11521; S11521.
DR RefSeq; NP_001001139.1; NM_001001139.2.
DR PDB; 1SY9; NMR; -; B=60-85.
DR PDBsum; 1SY9; -.
DR AlphaFoldDB; Q03041; -.
DR BMRB; Q03041; -.
DR SMR; Q03041; -.
DR IntAct; Q03041; 1.
DR MINT; Q03041; -.
DR STRING; 9913.ENSBTAP00000027618; -.
DR PaxDb; Q03041; -.
DR GeneID; 407172; -.
DR KEGG; bta:407172; -.
DR CTD; 1260; -.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q03041; -.
DR OrthoDB; 1073751at2759; -.
DR EvolutionaryTrace; Q03041; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; ISS:AgBase.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; ISS:AgBase.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR IDEAL; IID50188; -.
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 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; cAMP; cAMP-binding; Coiled coil;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Nucleotide-binding; Olfaction; Reference proteome;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..663
FT /note="Cyclic nucleotide-gated olfactory channel"
FT /id="PRO_0000219311"
FT TOPO_DOM 1..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..160
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..192
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..236
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..297
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..369
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..453
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..640
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462..584
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:1SY9"
SQ SEQUENCE 663 AA; 76014 MW; AB66D4F9203844EF CRC64;
MTEKANGVKS SPANNHNHHA PPAIKASGKD DHRASSRPQS AAADDTSSEL QQLAEMDAPQ
QRRGGFRRIA RLVGVLREWA YRNFREEEPR PDSFLERFRG PELHTVTTQQ GDGKGDKDGE
GKGTKKKFEL FVLDPAGDWY YRWLFLIALP VLYNWCLLVA RACFSDLQKG YYIVWLVLDY
VSDVVYIADL FIRLRTGFLE QGLLVKDTKK LRDNYIHTMQ FKLDVASIIP TDLIYFAVGI
HNPEVRFNRL LHFARMFEFF DRTETRTSYP NIFRISNLIL YILIIIHWNA CIYYAISKSI
GFGVDTWVYP NITDPEYGYL SREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKEMEAKVI RWFDYLWTNK
KSVDEREVLK NLPAKLRAEI AINVHLSTLK KVRIFQDCEA GLLVELVLKL RPQVFSPGDY
ICRKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI
RSLGYSDLFC LSKDDLMEAV TEYPDAKRVL EERGREILMK EGLLDENEVA ASMEVDVQEK
LEQLETNMDT LYTRFARLLA EYTGAQQKLK QRITVLETKM KQNNEDDSLS DGMNSPEPPA
EKP
