CNGA2_RAT
ID CNGA2_RAT Reviewed; 664 AA.
AC Q00195; Q549G7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 145.
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;
DE AltName: Full=Cyclic nucleotide-gated olfactory channel subunit OCNC1;
GN Name=Cnga2; Synonyms=Cncg2;
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 TISSUE=Olfactory sensory neuron;
RX PubMed=1697649; DOI=10.1038/347184a0;
RA Dhallan R.S., Yau K.-W., Schrader K.A., Reed R.R.;
RT "Primary structure and functional expression of a cyclic nucleotide-
RT activated channel from olfactory neurons.";
RL Nature 347:184-187(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10594674; DOI=10.1046/j.1460-9568.1999.00893.x;
RA Strijbos P.J., Pratt G.D., Khan S., Charles I.G., Garthwaite J.;
RT "Molecular characterization and in situ localization of a full-length
RT cyclic nucleotide-gated channel in rat brain.";
RL Eur. J. Neurosci. 11:4463-4467(1999).
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 -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA2 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X55519; CAA39135.1; -; mRNA.
DR EMBL; AF126808; AAD41473.1; -; mRNA.
DR PIR; S11517; S11517.
DR RefSeq; NP_037060.1; NM_012928.1.
DR RefSeq; XP_017455916.1; XM_017600427.1.
DR PDB; 2M0J; NMR; -; B=60-87.
DR PDB; 2M0K; NMR; -; B=60-87.
DR PDBsum; 2M0J; -.
DR PDBsum; 2M0K; -.
DR AlphaFoldDB; Q00195; -.
DR BMRB; Q00195; -.
DR SMR; Q00195; -.
DR DIP; DIP-61291N; -.
DR IntAct; Q00195; 1.
DR STRING; 10116.ENSRNOP00000016415; -.
DR BindingDB; Q00195; -.
DR ChEMBL; CHEMBL4523272; -.
DR GuidetoPHARMACOLOGY; 395; -.
DR GlyGen; Q00195; 1 site.
DR iPTMnet; Q00195; -.
DR PaxDb; Q00195; -.
DR GeneID; 25411; -.
DR KEGG; rno:25411; -.
DR CTD; 1260; -.
DR RGD; 2367; Cnga2.
DR eggNOG; KOG0500; Eukaryota.
DR InParanoid; Q00195; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q00195; -.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q00195; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI: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:0005216; F:ion channel activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0051899; P:membrane depolarization; IDA:RGD.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEP: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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF16526; CLZ; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
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..664
FT /note="Cyclic nucleotide-gated olfactory channel"
FT /id="PRO_0000219315"
FT TOPO_DOM 1..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..162
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..194
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..238
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..299
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..371
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 599..642
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..586
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT BINDING 538
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 212
FT /note="K -> R"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2M0K"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:2M0J"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2M0K"
SQ SEQUENCE 664 AA; 76177 MW; 720806950EC27F3C CRC64;
MMTEKSNGVK SSPANNHNHH PPPSIKANGK DDHRAGSRPQ SVAADDDTSP ELQRLAEMDT
PRRGRGGFQR IVRLVGVIRD WANKNFREEE PRPDSFLERF RGPELQTVTT HQGDDKGGKD
GEGKGTKKKF ELFVLDPAGD WYYRWLFVIA MPVLYNWCLL VARACFSDLQ RNYFVVWLVL
DYFSDTVYIA DLIIRLRTGF LEQGLLVKDP KKLRDNYIHT LQFKLDVASI IPTDLIYFAV
GIHSPEVRFN RLLHFARMFE FFDRTETRTS YPNIFRISNL VLYILVIIHW NACIYYVISK
SIGFGVDTWV YPNITDPEYG YLAREYIYCL YWSTLTLTTI GETPPPVKDE EYLFVIFDFL
IGVLIFATIV GNVGSMISNM NATRAEFQAK IDAVKHYMQF RKVSKDMEAK VIKWFDYLWT
NKKTVDEREV LKNLPAKLRA EIAINVHLST LKKVRIFQDC EAGLLVELVL KLRPQVFSPG
DYICRKGDIG KEMYIIKEGK LAVVADDGVT QYALLSAGSC FGEISILNIK GSKMGNRRTA
NIRSLGYSDL FCLSKDDLME AVTEYPDAKK VLEERGREIL MKEGLLDENE VAASMEVDVQ
EKLEQLETNM DTLYTRFARL LAEYTGAQQK LKQRITVLET KMKQNHEDDY LSDGINTPEP
TAAE
