ID CNG15_ARATH Reviewed; 678 AA.
AC Q9SL29;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 152.
DE RecName: Full=Putative cyclic nucleotide-gated ion channel 15;
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 15;
GN Name=CNGC15; OrderedLocusNames=At2g28260; ORFNames=T3B23.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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).
CC -!- FUNCTION: Putative cyclic nucleotide-gated ion channel.
CC -!- SUBUNIT: Homotetramer or heterotetramer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. {ECO:0000305}.
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DR EMBL; AC006202; AAD29827.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08097.1; -; Genomic_DNA.
DR PIR; G84682; G84682.
DR RefSeq; NP_180393.1; NM_128386.2.
DR AlphaFoldDB; Q9SL29; -.
DR STRING; 3702.Q9SL29; -.
DR TCDB; 1.A.1.5.27; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q9SL29; -.
DR PaxDb; 3702-AT2G28260-1; -.
DR EnsemblPlants; AT2G28260.1; AT2G28260.1; AT2G28260.
DR GeneID; 817372; -.
DR Gramene; AT2G28260.1; AT2G28260.1; AT2G28260.
DR KEGG; ath:AT2G28260; -.
DR Araport; AT2G28260; -.
DR TAIR; AT2G28260; CNGC15.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR InParanoid; Q9SL29; -.
DR OrthoDB; 3076617at2759; -.
DR PhylomeDB; Q9SL29; -.
DR PRO; PR:Q9SL29; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL29; baseline and differential.
DR Genevisible; Q9SL29; AT.
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:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0051592; P:response to calcium ion; IEP:TAIR.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45651:SF12; CYCLIC NUCLEOTIDE-GATED ION CHANNEL 15-RELATED; 1.
DR PANTHER; PTHR45651; CYCLIC NUCLEOTIDE-GATED ION CHANNEL 15-RELATED-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
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..678
FT /note="Putative cyclic nucleotide-gated ion channel 15"
FT /id="PRO_0000219343"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 607..638
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 587..602
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 656..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..595
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 542
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
SQ SEQUENCE 678 AA; 78723 MW; E020D14E44050E64 CRC64;
MGYGNSRSVR FQEDQEVVHG GESGVKLKFK INGTQINNVK MMSKGKFLKA KVLSRVFSED
LERVKTKILD PRGQTIRRWN KIFLIACLVS LFVDPLFFFL PVMRNEACIT IGVRLEVVLT
LIRSLADAFY IAQILIRFRT AYIAPPSRVF GRGELVIDSR KIAWRYLHKS FWIHLVAALP
LPQVLIWIII PNLRGSPMTN TKNVLRFIII FQYVPRMFLI FPLSRQIIKA TGVVTETAWA
GAAYNLMLYM LASHVLGACW YLLAVERQEA CWRHACNIEK QICQYRFFEC RRLEDPQRNS
WFEWSNITTI CKPASKFYEF GIFGDAVTST VTSSKFINKY FYCLWWGLKN LSSLGQNLAT
STYAGEILFA IIIATLGLVL FALLIGNMQT YLQSTTMRLE EWRIRRTDTE QWMHHRQLPP
ELRQAVRKYD QYKWLATRGV DEEALLISLP LDLRRDIKRH LCFDLVRRVP LFDQMDERML
DAICERLKPA LCTEGTFLVR EGDPVNEMLF IIRGHLDSYT TNGGRTGFFN SCLIGPGDFC
GEELLTWALD PRPVVILPSS TRTVKAICEV EAFALKAEDL QFVASQFRRL HTKQLRHKFR
FYSHQWRTWA ACFIQAAWRR HRKRKYKTEL RAKEEFHYRF EAATARLAVN GGKYTRSGSD
SGMMSSIQKP VEPDFSSE
//
