CNG_CAEEL
ID CNG_CAEEL Reviewed; 733 AA.
AC Q03611; P90800;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cyclic nucleotide-gated cation channel;
DE AltName: Full=Abnormal chemotaxis protein 4;
GN Name=tax-4; ORFNames=ZC84.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8893027; DOI=10.1016/s0896-6273(00)80202-0;
RA Komatsu H., Mori I., Rhee J.S., Akaike N., Ohshima Y.;
RT "Mutations in a cyclic nucleotide-gated channel lead to abnormal
RT thermosensation and chemosensation in C. elegans.";
RL Neuron 17:707-718(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION.
RX PubMed=9486798; DOI=10.1242/dev.125.2.249;
RA Coburn C.M., Mori I., Ohshima Y., Bargmann C.I.;
RT "A cyclic nucleotide-gated channel inhibits sensory axon outgrowth in
RT larval and adult Caenorhabditis elegans: a distinct pathway for maintenance
RT of sensory axon structure.";
RL Development 125:249-258(1998).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 510-GLN--LYS-733.
RX PubMed=20713521; DOI=10.1101/gad.1932610;
RA Lesch B.J., Bargmann C.I.;
RT "The homeodomain protein hmbx-1 maintains asymmetric gene expression in
RT adult C. elegans olfactory neurons.";
RL Genes Dev. 24:1802-1815(2010).
RN [6]
RP FUNCTION.
RX PubMed=21173231; DOI=10.1073/pnas.1017354108;
RA Hallem E.A., Spencer W.C., McWhirter R.D., Zeller G., Henz S.R., Ratsch G.,
RA Miller D.M., Horvitz H.R., Sternberg P.W., Ringstad N.;
RT "Receptor-type guanylate cyclase is required for carbon dioxide sensation
RT by Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:254-259(2011).
RN [7]
RP FUNCTION.
RX PubMed=23664973; DOI=10.1016/j.cub.2013.04.052;
RA Murayama T., Takayama J., Fujiwara M., Maruyama I.N.;
RT "Environmental alkalinity sensing mediated by the transmembrane guanylyl
RT cyclase GCY-14 in C. elegans.";
RL Curr. Biol. 23:1007-1012(2013).
RN [8]
RP FUNCTION.
RX PubMed=25303524; DOI=10.1016/j.cell.2014.09.011;
RA Meisel J.D., Panda O., Mahanti P., Schroeder F.C., Kim D.H.;
RT "Chemosensation of bacterial secondary metabolites modulates neuroendocrine
RT signaling and behavior of C. elegans.";
RL Cell 159:267-280(2014).
RN [9]
RP FUNCTION.
RX PubMed=25009271; DOI=10.1523/jneurosci.0012-14.2014;
RA Harris G., Shen Y., Ha H., Donato A., Wallis S., Zhang X., Zhang Y.;
RT "Dissecting the signaling mechanisms underlying recognition and preference
RT of food odors.";
RL J. Neurosci. 34:9389-9403(2014).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 82-GLU--LYS-733.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Required for normal thermosensation and chemosensation
CC sensory behavior (PubMed:8893027). Required, downstream of receptor-
CC type guanylate cyclase gcy-9, for CO2-mediated responses in BAG neurons
CC (PubMed:21173231). Required, downstream of receptor-type guanylate
CC cyclase gcy-14, for alkaline pH-mediated responses in ASE-left (ASEL)
CC neurons (PubMed:23664973). Involved in the development of ASJ sensory
CC neuron axon during late larval stages and in the maintenance of normal
CC axon morphology in the adult. Regulates dauer formation
CC (PubMed:9486798). Required for the calcium flux to the cytoplasm in the
CC ASJ sensory neurons upon the onset and removal of a nitric oxide (NO)
CC stimulus, thereby promoting the ASJ-mediated behavioral avoidance
CC response to NO-producing organisms like P.aeruginosa (PubMed:30014846).
CC In ASI and ASJ sensory neurons, controls behavioral response to
CC P.aeruginosa by up-regulating the transcription of daf-7, a member of
CC the TGF-beta family (PubMed:25303524). In AWB and AWC sensory neurons,
CC mediates the recognition of food odors which subsequently allows for
CC the detection of preferred food sources (PubMed:25009271). In AWC
CC neurons, acts to promote expression of srsx-3, a member of the GPCR
CC family. {ECO:0000269|PubMed:20713521, ECO:0000269|PubMed:21173231,
CC ECO:0000269|PubMed:23664973, ECO:0000269|PubMed:25009271,
CC ECO:0000269|PubMed:25303524, ECO:0000269|PubMed:30014846,
CC ECO:0000269|PubMed:8893027, ECO:0000269|PubMed:9486798}.
CC -!- INTERACTION:
CC Q03611; Q03611: tax-4; NbExp=3; IntAct=EBI-20710167, EBI-20710167;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at the sensory endings of thermosensory,
CC gustatory, and olfactory neurons.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. {ECO:0000305}.
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DR EMBL; D86922; BAA13180.1; -; mRNA.
DR EMBL; Z19157; CAB63418.2; -; Genomic_DNA.
DR PIR; S28292; S28292.
DR RefSeq; NP_499033.1; NM_066632.4.
DR PDB; 5H3O; EM; 3.50 A; A/B/C/D=1-733.
DR PDB; 6WEJ; EM; 2.60 A; A/B/C/D=1-733.
DR PDB; 6WEK; EM; 2.70 A; A/B/C/D=1-733.
DR PDB; 6WEL; EM; 2.50 A; A/B/C/D=1-733.
DR PDB; 7N15; EM; 2.90 A; A/B/C/D=1-733.
DR PDB; 7N16; EM; 3.20 A; A/B/C/D=1-733.
DR PDB; 7N17; EM; 3.10 A; A/B/C/D=1-733.
DR PDBsum; 5H3O; -.
DR PDBsum; 6WEJ; -.
DR PDBsum; 6WEK; -.
DR PDBsum; 6WEL; -.
DR PDBsum; 7N15; -.
DR PDBsum; 7N16; -.
DR PDBsum; 7N17; -.
DR AlphaFoldDB; Q03611; -.
DR SMR; Q03611; -.
DR BioGRID; 41496; 3.
DR STRING; 6239.ZC84.2; -.
DR TCDB; 1.A.1.5.20; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q03611; -.
DR EnsemblMetazoa; ZC84.2.1; ZC84.2.1; WBGene00006526.
DR GeneID; 176297; -.
DR KEGG; cel:CELE_ZC84.2; -.
DR UCSC; ZC84.2; c. elegans.
DR CTD; 176297; -.
DR WormBase; ZC84.2; CE27352; WBGene00006526; tax-4.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000171789; -.
DR HOGENOM; CLU_005746_12_1_1; -.
DR InParanoid; Q03611; -.
DR OMA; DMIAMIP; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q03611; -.
DR Reactome; R-CEL-2485179; Activation of the phototransduction cascade.
DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-CEL-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q03611; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006526; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR GO; GO:0034703; C:cation channel complex; IDA:WormBase.
DR GO; GO:0097543; C:ciliary inversin compartment; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IDA:WormBase.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IDA:WormBase.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0009454; P:aerotaxis; IMP:WormBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:CACAO.
DR GO; GO:0003031; P:detection of carbon dioxide; IMP:UniProtKB.
DR GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IMP:UniProtKB.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; IMP:UniProtKB.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IGI:WormBase.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IMP:WormBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:WormBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:WormBase.
DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040010; P:positive regulation of growth rate; IGI:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0030516; P:regulation of axon extension; IMP:WormBase.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:WormBase.
DR GO; GO:0055093; P:response to hyperoxia; IMP:WormBase.
DR GO; GO:0070482; P:response to oxygen levels; IMP:WormBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IMP:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR DisProt; DP02989; -.
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; cGMP; cGMP-binding; Chemotaxis; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Neurogenesis; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..733
FT /note="Cyclic nucleotide-gated cation channel"
FT /id="PRO_0000219328"
FT TOPO_DOM 1..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..623
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT BINDING 575
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT MUTAGEN 82..733
FT /note="Missing: In p678; defects in the avoidance of
FT P.aeruginosa and of nitric oxide. In nu629; abolishes the
FT calcium flux to the cytoplasm in the ASJ sensory neurons in
FT response to the addition and removal of a nitric oxide
FT stimulus."
FT /evidence="ECO:0000269|PubMed:30014846"
FT MUTAGEN 510..733
FT /note="Missing: In ky791; reduces expression of the G
FT protein-coupled receptor (GPCR) srsx-3 in the AWC neuron."
FT /evidence="ECO:0000269|PubMed:20713521"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5H3O"
FT HELIX 119..144
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6WEL"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 194..223
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:6WEK"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:6WEL"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 304..334
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:6WEL"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 386..416
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 419..437
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:6WEL"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 473..488
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:6WEK"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:6WEK"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:6WEK"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:6WEL"
FT STRAND 579..589
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 592..599
FT /evidence="ECO:0007829|PDB:6WEL"
FT HELIX 603..618
FT /evidence="ECO:0007829|PDB:6WEL"
SQ SEQUENCE 733 AA; 83893 MW; 1EC7EB0179F9355E CRC64;
MSTAEPAPDP TNPSTSGLAP TTNGIGSPPP TASAATKFSI LTKFLRRKNQ VHTTTAQQNE
FMQKYMPNGN SNAVQPAATG GQPASSDGGS AIEVPPPKES YAVRIRKYLA NYTQDPSTDN
FYYWTCVVTV AYIYNLLFVI ARQVFNDLIG PSSQSLCRFY NGTLNSTTQV ECTYNMLTNM
KEMPTYSQYP DLGWSKYWHF RMLWVFFDLL MDCVYLIDTF LNYRMGYMDQ GLVVREAEKV
TKAYWQSKQY RIDGISLIPL DYILGWPIPY INWRGLPILR LNRLIRYKRV RNCLERTETR
SSMPNAFRVV VVVWYIVIII HWNACLYFWI SEWIGLGTDA WVYGHLNKQS LPDDITDTLL
RRYVYSFYWS TLILTTIGEV PSPVRNIEYA FVTLDLMCGV LIFATIVGNV GSMISNMSAA
RTEFQNKMDG IKQYMELRKV SKQLEIRVIK WFDYLWTNKQ SLSDQQVLKV LPDKLQAEIA
MQVHFETLRK VRIFQDCEAG LLAELVLKLQ LQVFSPGDFI CKKGDIGREM YIVKRGRLQV
VDDDGKKVFV TLQEGSVFGE LSILNIAGSK NGNRRTANVR SVGYTDLFVL SKTDLWNALR
EYPDARKLLL AKGREILKKD NLLDENAPEE QKTVEEIAEH LNNAVKVLQT RMARLIVEHS
STEGKLMKRI EMLEKHLSRY KALARRQKTM HGVSIDGGDI STDGVDERVR PPRLRQTKTI
DLPTGTESES LLK
