CNGC2_ARATH
ID CNGC2_ARATH Reviewed; 726 AA.
AC O65718;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cyclic nucleotide-gated ion channel 2;
DE Short=AtCNGC2;
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 2;
DE AltName: Full=Protein DEFENSE NO DEATH 1;
GN Name=CNGC2; Synonyms=DND1; OrderedLocusNames=At5g15410; ORFNames=T20K14_20;
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 [GENOMIC DNA], 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 [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=10557223; DOI=10.1104/pp.121.3.753;
RA Leng Q., Mercier R.W., Yao W., Berkowitz G.A.;
RT "Cloning and first functional characterization of a plant cyclic
RT nucleotide-gated cation channel.";
RL Plant Physiol. 121:753-761(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTANT DND1-1.
RC STRAIN=cv. Columbia;
RX PubMed=10900264; DOI=10.1073/pnas.150005697;
RA Clough S.J., Fengler K.A., Yu I.-C., Lippok B., Smith R.K. Jr., Bent A.F.;
RT "The Arabidopsis dnd1 'defense, no death' gene encodes a mutated cyclic
RT nucleotide-gated ion channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9323-9328(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11506354; DOI=10.1007/s004250000510;
RA Koehler C., Merkle T., Roby D., Neuhaus G.;
RT "Developmentally regulated expression of a cyclic nucleotide-gated ion
RT channel from Arabidopsis indicates its involvement in programmed cell
RT death.";
RL Planta 213:327-332(2001).
RN [9]
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 [10]
RP NULL MUTANTS.
RX PubMed=12805601; DOI=10.1104/pp.102.019216;
RA Chan C.W.M., Schorrak L.M., Smith R.K. Jr., Bent A.F., Sussman M.R.;
RT "A cyclic nucleotide-gated ion channel, CNGC2, is crucial for plant
RT development and adaptation to calcium stress.";
RL Plant Physiol. 132:728-731(2003).
CC -!- FUNCTION: Acts as cyclic nucleotide-gated ion channel. Permeable to
CC potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or
CC cGMP). Could also transport lithium, cesium and rubium and displays a
CC strong selectivity against sodium. Seems to directly participate in
CC pathogen-induced calcium influx. May function in homeostasis, re-
CC establishing ionic balance after defense action and/or other stimuli.
CC Could mediate the initiation of the developmentally regulated cell
CC death programs. {ECO:0000269|PubMed:10900264,
CC ECO:0000269|PubMed:11506354}.
CC -!- SUBUNIT: Homotetramer or heterotetramer (Potential). Binds calmodulin-
CC 1/4 with a higher affinity than calmodulin-2/3/5. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O65718-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant but only weakly in
CC roots. Strongly expressed in the expanded cotyledons of 14-day-old
CC seedlings and detected later in leaves after the transition to
CC flowering. Also detected in flowers during organ senescence and in the
CC dehiscence zone of siliques. {ECO:0000269|PubMed:11506354}.
CC -!- INDUCTION: Up-regulated by light. Transiently induced during leaf and
CC culture senescence. {ECO:0000269|PubMed:11506354}.
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 -!- MISCELLANEOUS: Loss-of-function mutations cngc2-1 (dnd1-1) or cncg2-2
CC results in the loss of the hypersensitive response and leads to a broad
CC spectrum disease resistance. These mutations lead to a specific and
CC dramatic calcium hypersensitivity that results in severe reductions in
CC plant size and seed yield.
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; Y16328; CAA76179.1; -; Genomic_DNA.
DR EMBL; AF067798; AAC78613.1; -; mRNA.
DR EMBL; AF280939; AAF86351.1; -; Genomic_DNA.
DR EMBL; AL391143; CAC01740.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92158.1; -; Genomic_DNA.
DR PIR; T51519; T51519.
DR RefSeq; NP_197045.1; NM_121545.5. [O65718-1]
DR AlphaFoldDB; O65718; -.
DR STRING; 3702.AT5G15410.1; -.
DR TCDB; 1.A.1.5.6; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; O65718; -.
DR PRIDE; O65718; -.
DR ProteomicsDB; 220539; -. [O65718-1]
DR EnsemblPlants; AT5G15410.1; AT5G15410.1; AT5G15410. [O65718-1]
DR GeneID; 831393; -.
DR Gramene; AT5G15410.1; AT5G15410.1; AT5G15410. [O65718-1]
DR KEGG; ath:AT5G15410; -.
DR Araport; AT5G15410; -.
DR TAIR; locus:2180867; AT5G15410.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; O65718; -.
DR OMA; TEQFRYK; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; O65718; -.
DR PRO; PR:O65718; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65718; baseline and differential.
DR Genevisible; O65718; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; TAS:TAIR.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IDA:TAIR.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IMP:TAIR.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IGI:TAIR.
DR GO; GO:0070509; P:calcium ion import; IDA:TAIR.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
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 Alternative splicing; Calmodulin-binding; cAMP; cAMP-binding;
KW Cell membrane; cGMP; cGMP-binding; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..726
FT /note="Cyclic nucleotide-gated ion channel 2"
FT /id="PRO_0000219330"
FT TOPO_DOM 1..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..424
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 666..695
FT /note="IQ"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..661
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT BINDING 531..661
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 600
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
SQ SEQUENCE 726 AA; 83241 MW; 450097F2C392D8D4 CRC64;
MPSHPNFIFR WIGLFSDKFR RQTTGIDENS NLQINGGDSS SSGSDETPVL SSVECYACTQ
VGVPAFHSTS CDQAHAPEWR ASAGSSLVPI QEGSVPNPAR TRFRRLKGPF GEVLDPRSKR
VQRWNRALLL ARGMALAVDP LFFYALSIGR TTGPACLYMD GAFAAVVTVL RTCLDAVHLW
HVWLQFRLAY VSRESLVVGC GKLVWDPRAI ASHYARSLTG FWFDVIVILP VPQAVFWLVV
PKLIREEKVK LIMTILLLIF LFQFLPKIYH CICLMRRMQK VTGYIFGTIW WGFALNLIAY
FIASHVAGGC WYVLAIQRVA SCIRQQCMRT GNCNLSLACK EEVCYQFVSP TSTVGYPCLS
GNLTSVVNKP MCLDSNGPFR YGIYRWALPV ISSNSLAVKI LYPIFWGLMT LSTFANDLEP
TSNWLEVIFS IVMVLSGLLL FTLLIGNIQV FLHAVMAKKR KMQIRCRDME WWMKRRQLPS
RLRQRVRRFE RQRWNALGGE DELELIHDLP PGLRRDIKRY LCFDLINKVP LFRGMDDLIL
DNICDRAKPR VFSKDEKIIR EGDPVQRMIF IMRGRVKRIQ SLSKGVLATS TLEPGGYLGD
ELLSWCLRRP FLDRLPPSSA TFVCLENIEA FSLGSEDLRY ITDHFRYKFA NERLKRTARY
YSSNWRTWAA VNIQMAWRRR RKRTRGENIG GSMSPVSENS IEGNSERRLL QYAAMFMSIR
PHDHLE
