ID CNGA2_RABIT Reviewed; 664 AA.
AC Q28718;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 08-NOV-2023, entry version 116.
DE RecName: Full=Cyclic nucleotide-gated olfactory channel;
DE AltName: Full=Aorta CNG channel;
DE Short=RACNG;
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=7689061; DOI=10.1016/0014-5793(93)80209-d;
RA Biel M., Altenhofen W., Hullin R., Ludwig J., Freichel M., Flockerzi V.,
RA Dascal N., Kaupp U.B., Hofmann F.;
RT "Primary structure and functional expression of a cyclic nucleotide-gated
RT channel from rabbit aorta.";
RL FEBS Lett. 329:134-138(1993).
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 -!- 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. CNGA2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X59668; CAA42201.1; ALT_INIT; mRNA.
DR PIR; S35691; S35691.
DR RefSeq; NP_001075863.1; NM_001082394.1.
DR AlphaFoldDB; Q28718; -.
DR SMR; Q28718; -.
DR STRING; 9986.ENSOCUP00000008136; -.
DR GlyCosmos; Q28718; 1 site, No reported glycans.
DR PaxDb; 9986-ENSOCUP00000008136; -.
DR GeneID; 100009269; -.
DR KEGG; ocu:100009269; -.
DR CTD; 1260; -.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q28718; -.
DR OrthoDB; 74296at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.5.300; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR PANTHER; PTHR45638:SF3; CYCLIC NUCLEOTIDE-GATED OLFACTORY CHANNEL; 1.
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; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 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 Calmodulin-binding; cAMP; cAMP-binding; Coiled coil; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Nucleotide-binding; Olfaction; Reference proteome; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..664
FT /note="Cyclic nucleotide-gated olfactory channel"
FT /id="PRO_0000219314"
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..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..640
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic 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:0000255"
FT BINDING 536
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 664 AA; 76206 MW; 5E9170D0B322B3E9 CRC64;
MTEKSNGVKS SPANNHNNHV PATIKANGKD ESRTRSRPQS AADDDTSSEL QRLAEMDAPQ
QRRGGFRRIV RLVGVIRQWA NRNFREEEAR PDSFLERFRG PELQTVTTQQ GDGKGDKDGD
GKGTKKKFEL FVLDPAGDWY YRWLFVIAMP VLYNWCLLVA RACFSDLQRG YFLVWLVLDY
FSDVVYIADL FIRLRTGFLE QGLLVKDPKK LRDNYIHTLQ FKLDVASIIP TDLIYFAVGI
HNPELRFNRL LHFARMFEFF DRTETRTSYP NIFRISNLVL YILVIIHWNA CIYYAISKSI
GFGVDTWVYP NITDPEYGYL AREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKEMEAKVI KWFDYLWTNK
KTVDEREVLK NLPAKLRAEI AINVHLSTLK KVRIFQDCEA GLLVELVLKL RPQVFSPGDY
ICRKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI
RSLGYSDLFC LSKDDLMEAV TEYPDAKKVL EERGREILMK EGLLDENEVA ASMEVDVQEK
LKQLETNMET LYTRFGRLLA EYTGAQQKLK QRITVLEVKM KQNTEDDYLS DGMNSPEPAA
AEQP
//
