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CNGC4_ARATH
ID   CNGC4_ARATH             Reviewed;         694 AA.
AC   Q94AS9; Q9XFS2;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Cyclic nucleotide-gated ion channel 4;
DE            Short=AtCNGC4;
DE   AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 4;
DE            Short=AtHLM1;
GN   Name=CNGC4; Synonyms=HLM1; OrderedLocusNames=At5g54250; ORFNames=MDK4.7;
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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] (ISOFORMS 1 AND 2).
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   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   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12566578; DOI=10.1105/tpc.006999;
RA   Balague C., Lin B., Alcon C., Flottes G., Malmstroem S., Koehler C.,
RA   Neuhaus G., Pelletier G., Gaymard F., Roby D.;
RT   "HLM1, an essential signaling component in the hypersensitive response, is
RT   a member of the cyclic nucleotide-gated channel ion channel family.";
RL   Plant Cell 15:365-379(2003).
CC   -!- FUNCTION: Acts as cyclic nucleotide-gated ion channel. Permeable to
CC       potassium and sodium in a cyclic nucleotide-dependent fashion (cAMP or
CC       cGMP). Might constitute a common downstream component of the signaling
CC       pathways leading to hypersensitive response (HR).
CC       {ECO:0000269|PubMed:12566578}.
CC   -!- SUBUNIT: Homotetramer or heterotetramer. {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=2;
CC       Name=1;
CC         IsoId=Q94AS9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94AS9-2; Sequence=VSP_008985, VSP_008986;
CC   -!- INDUCTION: Induced by both ethylene and methyl jasmonate treatments, or
CC       after pathogen attack.
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: Loss-of-function mutation results in the loss of
CC       the hypersensitive response leading to broad spectrum disease
CC       resistance, and displays a lesion-mimic phenotype.
CC       {ECO:0000269|PubMed:12566578}.
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; Y17912; CAB40129.1; -; mRNA.
DR   EMBL; AB010695; BAB10748.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96473.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96474.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70509.1; -; Genomic_DNA.
DR   EMBL; AY045822; AAK76496.1; -; mRNA.
DR   EMBL; AY057691; AAL15321.1; -; mRNA.
DR   EMBL; AY133734; AAM91668.1; -; mRNA.
DR   PIR; T52574; T52574.
DR   RefSeq; NP_001332114.1; NM_001345080.1. [Q94AS9-1]
DR   RefSeq; NP_200236.1; NM_124805.3. [Q94AS9-1]
DR   RefSeq; NP_851188.1; NM_180857.2. [Q94AS9-1]
DR   AlphaFoldDB; Q94AS9; -.
DR   STRING; 3702.AT5G54250.2; -.
DR   TCDB; 1.A.1.5.7; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; Q94AS9; -.
DR   PaxDb; Q94AS9; -.
DR   PRIDE; Q94AS9; -.
DR   ProteomicsDB; 220482; -. [Q94AS9-1]
DR   EnsemblPlants; AT5G54250.1; AT5G54250.1; AT5G54250. [Q94AS9-1]
DR   EnsemblPlants; AT5G54250.2; AT5G54250.2; AT5G54250. [Q94AS9-1]
DR   EnsemblPlants; AT5G54250.4; AT5G54250.4; AT5G54250. [Q94AS9-1]
DR   GeneID; 835513; -.
DR   Gramene; AT5G54250.1; AT5G54250.1; AT5G54250. [Q94AS9-1]
DR   Gramene; AT5G54250.2; AT5G54250.2; AT5G54250. [Q94AS9-1]
DR   Gramene; AT5G54250.4; AT5G54250.4; AT5G54250. [Q94AS9-1]
DR   KEGG; ath:AT5G54250; -.
DR   Araport; AT5G54250; -.
DR   TAIR; locus:2162605; AT5G54250.
DR   eggNOG; KOG0498; Eukaryota.
DR   HOGENOM; CLU_013069_3_1_1; -.
DR   InParanoid; Q94AS9; -.
DR   OMA; KGPNPIT; -.
DR   PhylomeDB; Q94AS9; -.
DR   PRO; PR:Q94AS9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q94AS9; baseline and differential.
DR   Genevisible; Q94AS9; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008324; F:cation transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
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; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calmodulin-binding; cAMP; cAMP-binding;
KW   Cell membrane; cGMP; cGMP-binding; Hypersensitive response; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Plant defense; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..694
FT                   /note="Cyclic nucleotide-gated ion channel 4"
FT                   /id="PRO_0000219332"
FT   TOPO_DOM        1..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical; Name=H1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical; Name=H2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..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..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=H4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..392
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical; Name=H6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..694
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          631..660
FT                   /note="IQ"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..626
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         496..626
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   BINDING         565
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         274..293
FT                   /note="AAGACWYLLGVQRSAKCLKE -> VSYLINCFVLLNILVNTKFQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_008985"
FT   VAR_SEQ         294..694
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_008986"
SQ   SEQUENCE   694 AA;  80081 MW;  E3F843AE1B0F1EA0 CRC64;
     MATEQEFTRA SRFSRDSSSV GYYSEEDNTE EEDEEEEEME EIEEEEEEEE EEDPRIGLTC
     GGRRNGSSNN NKWMMLGRIL DPRSKWVREW NKVFLLVCAT GLFVDPLFLY TLSVSDTCMC
     LLVDGWLALT VTALRSMTDL LHLWNIWIQF KIARRWPYPG GDSDGDTNKG GGTRGSTRVA
     PPYVKKNGFF FDLFVILPLP QVVLWVVIPS LLKRGSVTLV VSVLLVTFLF QYLPKIYHSI
     RHLRRNATLS GYIFGTVWWG IALNMIAYFV AAHAAGACWY LLGVQRSAKC LKEQCENTIG
     CDLRMLSCKE PVYYGTTVMV LDRARLAWAQ NHQARSVCLD INTNYTYGAY QWTIQLVSSE
     SRLEKILFPI FWGLMTLSTF GNLESTTEWS EVVFNIIVLT SGLLLVTMLI GNIKVFLHAT
     TSKKQAMHLK MRNIEWWMKK RHLPIGFRQR VRNYERQRWA AMRGVDECEM VQNLPEGLRR
     DIKYHLCLDL VRQVPLFQHM DDLVLENICD RVKSLIFTKG ETIQKEGDAV QRMLFVVRGH
     LQSSQLLRDG VKSCCMLGPG NFSGDELLSW CLRRPFVERL PPSSSTLVTL ETTEAFGLDA
     EDVKYVTQHF RYTFVNEKVK RSARYYSPGW RTWAAVAVQL AWRRYKHRLT LTSLSFIRPR
     RPLSRCASLG EDKLRLYAAI LTSPKPNPDD FDDY
 
 
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