CNGA_DROME
ID CNGA_DROME Reviewed; 665 AA.
AC Q24278; Q9V7L5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cyclic nucleotide-gated cation channel subunit A;
DE AltName: Full=Cyclic nucleotide-gated ion channel subunit A;
DE Short=CNG channel;
GN Name=CngA; Synonyms=Cng; ORFNames=CG7779;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7957070; DOI=10.1002/j.1460-2075.1994.tb06833.x;
RA Baumann A., Frings S., Godde M., Seifert R., Kaupp U.B.;
RT "Primary structure and functional expression of a Drosophila cyclic
RT nucleotide-gated channel present in eyes and antennae.";
RL EMBO J. 13:5040-5050(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC -!- FUNCTION: Approximately 50-fold more sensitive to cGMP than to cAMP.
CC May be involved in transduction cascades of both invertebrate
CC photoreceptors and olfactory sensillae. {ECO:0000269|PubMed:7957070}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in antennae and the visual system.
CC {ECO:0000269|PubMed:7957070}.
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; X89601; CAA61760.1; -; mRNA.
DR EMBL; AE013599; AAF58033.1; -; Genomic_DNA.
DR RefSeq; NP_477116.1; NM_057768.3.
DR AlphaFoldDB; Q24278; -.
DR SMR; Q24278; -.
DR IntAct; Q24278; 2.
DR STRING; 7227.FBpp0292051; -.
DR TCDB; 1.A.1.5.18; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q24278; 1 site.
DR PaxDb; Q24278; -.
DR EnsemblMetazoa; FBtr0302924; FBpp0292050; FBgn0261612.
DR GeneID; 36806; -.
DR KEGG; dme:Dmel_CG42701; -.
DR CTD; 36806; -.
DR FlyBase; FBgn0261612; CngA.
DR VEuPathDB; VectorBase:FBgn0261612; -.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000171789; -.
DR HOGENOM; CLU_005746_12_1_1; -.
DR InParanoid; Q24278; -.
DR OMA; FQFKLDF; -.
DR PhylomeDB; Q24278; -.
DR Reactome; R-DME-2485179; Activation of the phototransduction cascade.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DME-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q24278; -.
DR BioGRID-ORCS; 36806; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36806; -.
DR PRO; PR:Q24278; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261612; Expressed in crop (Drosophila) and 14 other tissues.
DR ExpressionAtlas; Q24278; baseline and differential.
DR Genevisible; Q24278; DM.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IBA:GO_Central.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IDA:FlyBase.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:FlyBase.
DR GO; GO:0006812; P:cation transport; IDA:FlyBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:FlyBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
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 cGMP; cGMP-binding; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..665
FT /note="Cyclic nucleotide-gated cation channel subunit A"
FT /id="PRO_0000219327"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..665
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 633..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..559
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT BINDING 511
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="G -> R (in Ref. 1; CAA61760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 75823 MW; 6EFFC9A7CA243660 CRC64;
MRHFKVKAMV QSLDISAITG QQTDAEPSKR SKPSALRRTL QALRQRLTKR NRPKPPDWFL
EKFSNTTNTD KIGKGCPAME DAALSSEIRG SSVLCNRLSV DPTLQSHYRW LAIVSLAVLY
NIIFVVGRAV FWEINKSAPA FWYTLDYLCD FIYLLDTLVH MHEGFLDQGL LVRDAFRLRR
HYFHTKGWYL DVLSMLPTDL AYIWWPPETC SSLYLPCPVI VRLNRLLRIN RLWEWFDRTE
TATGYPNAFR ICKVVLAILV LIHWNACMYF AISYEIGFSS DSWVYNLNGT RNNTLQRQYI
YSFYWSTLTL TTIGETPTPE NDVEYLFVVA DFLAGVLIFA TIVGNIGSMI SNMNVARVEF
QNRMDGVKQY MAFRRVGHEL EARVIRWFAY TWSQSGALDE ERVLAALPDK LKAEIAIQVH
MDTLKQVRIF HDTEPGLLEA LVLKLKLQVF SPGDYICRKG DVGKEMYIVK RGKLSVVGDD
GITVLATLGA GSVFGEVSVL EIAGNRTGNR RTANVRSLGY SDLFCLAKRD LWETLSDYPE
ARSTLTQRGC QLLRKDGLLD EQIFADSQRV HDSIEGGIEK LELSVENLNM RLARLLAEYT
ASQAKIKQRL AKLEMNGGPG TWRLECEPQS RARSGRLYSL QPKRRPRSRP DATAKSSDAA
KQNTL