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Cyclic nucleotide-gated ion channel 2 (AtCNGC2) (Cyclic nucleotide- and calmodulin-regulated ion channel 2) (Protein DEFENSE NO DEATH 1)

 CNGC2_ARATH             Reviewed;         726 AA.
O65718;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
23-MAY-2018, entry version 142.
RecName: Full=Cyclic nucleotide-gated ion channel 2;
Short=AtCNGC2;
AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 2;
AltName: Full=Protein DEFENSE NO DEATH 1;
Name=CNGC2; Synonyms=DND1; OrderedLocusNames=At5g15410;
ORFNames=T20K14_20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=cv. Columbia;
Koehler C., Neuhaus G.;
"Cloning and partial characterization of two putative cyclic
nucleotide-regulated ion channels from Arabidopsis thaliana,
designated CNGC1 and CNGC2.";
(er) Plant Gene Register PGR98-062(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=cv. Columbia;
PubMed=10557223; DOI=10.1104/pp.121.3.753;
Leng Q., Mercier R.W., Yao W., Berkowitz G.A.;
"Cloning and first functional characterization of a plant cyclic
nucleotide-gated cation channel.";
Plant Physiol. 121:753-761(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTANT DND1-1.
STRAIN=cv. Columbia;
PubMed=10900264; DOI=10.1073/pnas.150005697;
Clough S.J., Fengler K.A., Yu I.-C., Lippok B., Smith R.K. Jr.,
Bent A.F.;
"The Arabidopsis dnd1 'defense, no death' gene encodes a mutated
cyclic nucleotide-gated ion channel.";
Proc. Natl. Acad. Sci. U.S.A. 97:9323-9328(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
INTERACTION WITH CALMODULIN.
PubMed=10341447; DOI=10.1046/j.1365-313X.1999.00422.x;
Koehler C., Merkle T., Neuhaus G.;
"Characterisation of a novel gene family of putative cyclic
nucleotide- and calmodulin-regulated ion channels in Arabidopsis
thaliana.";
Plant J. 18:97-104(1999).
[7]
CALMODULIN-BINDING DOMAIN.
PubMed=10767408; DOI=10.1016/S0014-5793(00)01383-1;
Koehler C., Neuhaus G.;
"Characterisation of calmodulin binding to cyclic nucleotide-gated ion
channels from Arabidopsis thaliana.";
FEBS Lett. 471:133-136(2000).
[8]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11506354; DOI=10.1007/s004250000510;
Koehler C., Merkle T., Roby D., Neuhaus G.;
"Developmentally regulated expression of a cyclic nucleotide-gated ion
channel from Arabidopsis indicates its involvement in programmed cell
death.";
Planta 213:327-332(2001).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11500563; DOI=10.1104/pp.126.4.1646;
Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
Guerinot M.L.;
"Phylogenetic relationships within cation transporter families of
Arabidopsis.";
Plant Physiol. 126:1646-1667(2001).
[10]
NULL MUTANTS.
PubMed=12805601; DOI=10.1104/pp.102.019216;
Chan C.W.M., Schorrak L.M., Smith R.K. Jr., Bent A.F., Sussman M.R.;
"A cyclic nucleotide-gated ion channel, CNGC2, is crucial for plant
development and adaptation to calcium stress.";
Plant Physiol. 132:728-731(2003).
-!- FUNCTION: Acts as cyclic nucleotide-gated ion channel. Permeable
to potassium and calcium in a cyclic nucleotide-dependent fashion
(cAMP or cGMP). Could also transport lithium, cesium and rubium
and displays a strong selectivity against sodium. Seems to
directly participate in pathogen-induced calcium influx. May
function in homeostasis, re-establishing ionic balance after
defense action and/or other stimuli. Could mediate the initiation
of the developmentally regulated cell death programs.
{ECO:0000269|PubMed:10900264, ECO:0000269|PubMed:11506354}.
-!- SUBUNIT: Homotetramer or heterotetramer (Potential). Binds
calmodulin-1/4 with a higher affinity than calmodulin-2/3/5.
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=O65718-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in the whole plant but only weakly
in roots. Strongly expressed in the expanded cotyledons of 14-day-
old seedlings and detected later in leaves after the transition to
flowering. Also detected in flowers during organ senescence and in
the dehiscence zone of siliques. {ECO:0000269|PubMed:11506354}.
-!- INDUCTION: Up-regulated by light. Transiently induced during leaf
and culture senescence. {ECO:0000269|PubMed:11506354}.
-!- DOMAIN: The binding of calmodulin to the C-terminus might
interfere with cyclic nucleotide binding and thus channel
activation. {ECO:0000250}.
-!- MISCELLANEOUS: Loss-of-function mutations cngc2-1 (dnd1-1) or
cncg2-2 results in the loss of the hypersensitive response and
leads to a broad spectrum disease resistance. These mutations lead
to a specific and dramatic calcium hypersensitivity that results
in severe reductions in plant size and seed yield.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Y16328; CAA76179.1; -; Genomic_DNA.
EMBL; AF067798; AAC78613.1; -; mRNA.
EMBL; AF280939; AAF86351.1; -; Genomic_DNA.
EMBL; AL391143; CAC01740.1; -; Genomic_DNA.
EMBL; CP002688; AED92158.1; -; Genomic_DNA.
PIR; T51519; T51519.
RefSeq; NP_197045.1; NM_121545.5. [O65718-1]
UniGene; At.20813; -.
UniGene; At.74751; -.
ProteinModelPortal; O65718; -.
SMR; O65718; -.
STRING; 3702.AT5G15410.1; -.
TCDB; 1.A.1.5.6; the voltage-gated ion channel (vic) superfamily.
PaxDb; O65718; -.
EnsemblPlants; AT5G15410.1; AT5G15410.1; AT5G15410. [O65718-1]
GeneID; 831393; -.
Gramene; AT5G15410.1; AT5G15410.1; AT5G15410. [O65718-1]
KEGG; ath:AT5G15410; -.
Araport; AT5G15410; -.
TAIR; locus:2180867; AT5G15410.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
HOGENOM; HOG000238338; -.
InParanoid; O65718; -.
KO; K05391; -.
OMA; TEQFRYK; -.
OrthoDB; EOG0936045S; -.
PhylomeDB; O65718; -.
PRO; PR:O65718; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O65718; baseline and differential.
Genevisible; O65718; AT.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005262; F:calcium channel activity; IDA:TAIR.
GO; GO:0005516; F:calmodulin binding; TAS:TAIR.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0005222; F:intracellular cAMP activated cation channel activity; IDA:TAIR.
GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IMP:TAIR.
GO; GO:0005242; F:inward rectifier potassium channel activity; IGI:TAIR.
GO; GO:0070509; P:calcium ion import; IDA:TAIR.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:TAIR.
GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; cAMP; cAMP-binding;
Cell membrane; cGMP; cGMP-binding; Complete proteome; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
Plant defense; Reference proteome; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 726 Cyclic nucleotide-gated ion channel 2.
/FTId=PRO_0000219330.
TOPO_DOM 1 127 Cytoplasmic. {ECO:0000255}.
TRANSMEM 128 148 Helical; Name=H1. {ECO:0000255}.
TOPO_DOM 149 162 Extracellular. {ECO:0000255}.
TRANSMEM 163 183 Helical; Name=H2. {ECO:0000255}.
TOPO_DOM 184 219 Cytoplasmic. {ECO:0000255}.
TRANSMEM 220 240 Helical; Name=H3. {ECO:0000255}.
TOPO_DOM 241 254 Extracellular. {ECO:0000255}.
TRANSMEM 255 275 Helical; Name=H4. {ECO:0000255}.
TOPO_DOM 276 282 Cytoplasmic. {ECO:0000255}.
TRANSMEM 283 303 Helical; Name=H5. {ECO:0000255}.
TOPO_DOM 304 424 Extracellular. {ECO:0000255}.
TRANSMEM 425 445 Helical; Name=H6. {ECO:0000255}.
TOPO_DOM 446 726 Cytoplasmic. {ECO:0000255}.
DOMAIN 666 695 IQ.
NP_BIND 531 661 cNMP.
REGION 645 661 Calmodulin-binding. {ECO:0000250}.
BINDING 600 600 cNMP. {ECO:0000250}.
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


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