CNGC1_ARATH
ID CNGC1_ARATH Reviewed; 716 AA.
AC O65717;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cyclic nucleotide-gated ion channel 1;
DE Short=AtCNGC1;
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 1;
GN Name=CNGC1; OrderedLocusNames=At5g53130; ORFNames=MFH8.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RA Koehler C., Neuhaus G.;
RT "Cloning and partial characterization of two putative cyclic nucleotide-
RT regulated ion channels from Arabidopsis thaliana, designated CNGC1 and
RT CNGC2.";
RL (er) Plant Gene Register PGR98-062(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INTERACTION WITH CALMODULIN.
RX PubMed=10341447; DOI=10.1046/j.1365-313x.1999.00422.x;
RA Koehler C., Merkle T., Neuhaus G.;
RT "Characterisation of a novel gene family of putative cyclic nucleotide- and
RT calmodulin-regulated ion channels in Arabidopsis thaliana.";
RL Plant J. 18:97-104(1999).
RN [6]
RP CALMODULIN-BINDING DOMAIN.
RX PubMed=10767408; DOI=10.1016/s0014-5793(00)01383-1;
RA Koehler C., Neuhaus G.;
RT "Characterisation of calmodulin binding to cyclic nucleotide-gated ion
RT channels from Arabidopsis thaliana.";
RL FEBS Lett. 471:133-136(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11115134; DOI=10.1046/j.1365-313x.2000.00901.x;
RA Sunkar R., Kaplan B., Bouche N., Arazi T., Dolev D., Talke I.N.,
RA Maathuis F.J.M., Sanders D., Bouchez D., Fromm H.;
RT "Expression of a truncated tobacco NtCBP4 channel in transgenic plants and
RT disruption of the homologous Arabidopsis CNGC1 gene confer Pb2+
RT tolerance.";
RL Plant J. 24:533-542(2000).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [9]
RP CHARACTERIZATION, AND FUNCTION.
RX PubMed=11842144; DOI=10.1104/pp.010832;
RA Leng Q., Mercier R.W., Hua B.-G., Fromm H., Berkowitz G.A.;
RT "Electrophysiological analysis of cloned cyclic nucleotide-gated ion
RT channels.";
RL Plant Physiol. 128:400-410(2002).
CC -!- FUNCTION: Acts as cyclic nucleotide-gated ion channel. Can be activated
CC by cyclic AMP which leads to an opening of the cation channel. May be
CC responsible for cAMP-induced calcium entry in cells and thus should be
CC involved in the calcium signal transduction. Could transport K(+),
CC Na(+) and Pb(2+). {ECO:0000269|PubMed:11115134,
CC ECO:0000269|PubMed:11842144}.
CC -!- SUBUNIT: Homotetramer or heterotetramer (Potential). Binds calmodulin-
CC 2/3/5 with a higher affinity than calmodulin-1/4. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant but only weakly in
CC roots.
CC -!- DOMAIN: The binding of calmodulin to the C-terminus might interfere
CC with cyclic nucleotide binding and thus channel activation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit an improved tolerance to Pb(2+).
CC {ECO:0000269|PubMed:11115134}.
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; Y16327; CAA76178.1; -; mRNA.
DR EMBL; AB025622; BAB08416.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96311.1; -; Genomic_DNA.
DR EMBL; AF370139; AAK43954.1; -; mRNA.
DR EMBL; BT000991; AAN41391.1; -; mRNA.
DR PIR; T51354; T51354.
DR RefSeq; NP_200125.1; NM_124692.3.
DR AlphaFoldDB; O65717; -.
DR BioGRID; 20638; 4.
DR IntAct; O65717; 2.
DR STRING; 3702.AT5G53130.1; -.
DR TCDB; 1.A.1.5.5; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; O65717; -.
DR PaxDb; O65717; -.
DR PRIDE; O65717; -.
DR ProteomicsDB; 220294; -.
DR EnsemblPlants; AT5G53130.1; AT5G53130.1; AT5G53130.
DR GeneID; 835393; -.
DR Gramene; AT5G53130.1; AT5G53130.1; AT5G53130.
DR KEGG; ath:AT5G53130; -.
DR Araport; AT5G53130; -.
DR TAIR; locus:2163776; AT5G53130.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR InParanoid; O65717; -.
DR OMA; RHTFRLY; -.
DR OrthoDB; 281394at2759; -.
DR PhylomeDB; O65717; -.
DR PRO; PR:O65717; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65717; baseline and differential.
DR Genevisible; O65717; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; cAMP; cAMP-binding; Cell membrane; cGMP; cGMP-binding;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..716
FT /note="Cyclic nucleotide-gated ion channel 1"
FT /id="PRO_0000219329"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 622..651
FT /note="IQ"
FT REGION 602..617
FT /note="Calmodulin-binding"
FT REGION 689..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..610
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 557
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
SQ SEQUENCE 716 AA; 83097 MW; 5883CA949B6E7BF2 CRC64;
MNFRQEKFVR FQDWKSDKTS SDVEYSGKNE IQTGIFQRTI SSISDKFYRS FESSSARIKL
FKRSYKSYSF KEAVSKGIGS THKILDPQGP FLQRWNKIFV LACIIAVSLD PLFFYVPIID
DAKKCLGIDK KMEITASVLR SFTDVFYVLH IIFQFRTGFI APSSRVFGRG VLVEDKREIA
KRYLSSHFII DILAVLPLPQ MVILIIIPHM RGSSSLNTKN MLKFIVFFQY IPRFIRIYPL
YKEVTRTSGI LTETAWAGAA FNLFLYMLAS HVFGAFWYLF SIERETVCWK QACERNNPPC
ISKLLYCDPE TAGGNAFLNE SCPIQTPNTT LFDFGIFLDA LQSGVVESQD FPQKFFYCFW
WGLQNLSSLG QNLKTSTYIW EICFAVFISI AGLVLFSFLI GNMQTYLQST TTRLEEMRVK
RRDAEQWMSH RLLPENLRKR IRRYEQYKWQ ETRGVDEENL LSNLPKDLRR DIKRHLCLAL
LMRVPMFEKM DEQLLDALCD RLQPVLYTEE SYIVREGDPV DEMLFIMRGK LLTITTNGGR
TGFLNSEYLG AGDFCGEELL TWALDPHSSS NLPISTRTVR ALMEVEAFAL KADDLKFVAS
QFRRLHSKQL RHTFRYYSQQ WKTWAACFIQ AAWRRYIKKK LEESLKEEEN RLQDALAKEA
CGSSPSLGAT IYASRFAANI LRTIRRSGSV RKPRMPERMP PMLLQKPAEP DFNSDD
