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Database: UniProt
Entry: CNGC1_ARATH
LinkDB: CNGC1_ARATH
Original site: 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   25-OCT-2017, entry version 136.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   nucleotide-regulated ion channels from Arabidopsis thaliana,
RT   designated CNGC1 and 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;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   nucleotide- and calmodulin-regulated ion channels in Arabidopsis
RT   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
RT   and 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.,
RA   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
CC       activated by cyclic AMP which leads to an opening of the cation
CC       channel. May be responsible for cAMP-induced calcium entry in
CC       cells and thus should be involved in the calcium signal
CC       transduction. Could transport K(+), Na(+) and Pb(2+).
CC       {ECO:0000269|PubMed:11115134, ECO:0000269|PubMed:11842144}.
CC   -!- SUBUNIT: Homotetramer or heterotetramer (Potential). Binds
CC       calmodulin-2/3/5 with a higher affinity than calmodulin-1/4.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the whole plant but only weakly
CC       in roots.
CC   -!- DOMAIN: The binding of calmodulin to the C-terminus might
CC       interfere with cyclic nucleotide binding and thus channel
CC       activation. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Plants exhibit an improved tolerance to
CC       Pb(2+). {ECO:0000269|PubMed:11115134}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. {ECO:0000305}.
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   UniGene; At.21042; -.
DR   UniGene; At.49166; -.
DR   ProteinModelPortal; O65717; -.
DR   SMR; O65717; -.
DR   BioGrid; 20638; 4.
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   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   eggNOG; ENOG410XPSE; LUCA.
DR   HOGENOM; HOG000238338; -.
DR   InParanoid; O65717; -.
DR   KO; K05391; -.
DR   OMA; SVPMFEN; -.
DR   OrthoDB; EOG09360404; -.
DR   PhylomeDB; O65717; -.
DR   Reactome; R-ATH-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-ATH-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-ATH-5620916; VxPx cargo-targeting to cilium.
DR   PRO; PR:O65717; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; O65717; AT.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
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;
KW   cGMP-binding; Complete proteome; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    716       Cyclic nucleotide-gated ion channel 1.
FT                                /FTId=PRO_0000219329.
FT   TOPO_DOM      1     97       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     98    118       Helical; Name=H1. {ECO:0000255}.
FT   TOPO_DOM    119    132       Extracellular. {ECO:0000255}.
FT   TRANSMEM    133    153       Helical; Name=H2. {ECO:0000255}.
FT   TOPO_DOM    154    187       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    188    208       Helical; Name=H3. {ECO:0000255}.
FT   TOPO_DOM    209    220       Extracellular. {ECO:0000255}.
FT   TRANSMEM    221    241       Helical; Name=H4. {ECO:0000255}.
FT   TOPO_DOM    242    259       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    260    280       Helical; Name=H5. {ECO:0000255}.
FT   TOPO_DOM    281    379       Extracellular. {ECO:0000255}.
FT   TRANSMEM    380    400       Helical; Name=H6. {ECO:0000255}.
FT   TOPO_DOM    401    716       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      622    651       IQ.
FT   NP_BIND     486    610       cNMP.
FT   REGION      602    617       Calmodulin-binding.
FT   BINDING     557    557       cNMP. {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
//
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