CNG17_ARATH
ID CNG17_ARATH Reviewed; 720 AA.
AC Q8L7Z0; Q9M0C4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cyclic nucleotide-gated ion channel 17 {ECO:0000303|PubMed:11500563};
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 17 {ECO:0000303|PubMed:11500563};
GN Name=CNGC17 {ECO:0000303|PubMed:11500563};
GN OrderedLocusNames=At4g30360 {ECO:0000312|Araport:AT4G30360};
GN ORFNames=F17I23_300 {ECO:0000312|EMBL:CAB81029.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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., 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 [4]
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 [5]
RP FUNCTION, INTERACTION WITH AHA1; AHA2 AND BAK1, LACK OF INTERACTION WITH
RP PSKR1 AND BRI1, AND SUBCELLULAR LOCATION.
RX PubMed=26071421; DOI=10.1105/tpc.15.00306;
RA Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K., Sauter M.;
RT "Phytosulfokine regulates growth in Arabidopsis through a response module
RT at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-
RT ATPase, and BAK1.";
RL Plant Cell 27:1718-1729(2015).
CC -!- FUNCTION: Probable cyclic nucleotide-gated ion channel
CC (PubMed:11500563). Forms a functional cation-translocating unit with
CC AHAs that is activated by PSKR1/BAK1 and possibly other BAK1/RLK
CC complexes (PubMed:26071421). Required for PSK-induced protoplast
CC expansion (PubMed:26071421). {ECO:0000269|PubMed:26071421,
CC ECO:0000305|PubMed:11500563}.
CC -!- SUBUNIT: Homotetramer or heterotetramer (Probable). Part of a
CC functional complex containing PSKR1, BAK1, CNGC17, and AHA
CC (PubMed:26071421). Interacts with AHA1, AHA2, and BAK1, but not with
CC PSKR1 or BRI1 (PubMed:26071421). {ECO:0000269|PubMed:26071421,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421};
CC Multi-pass membrane 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161576; CAB81029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85756.1; -; Genomic_DNA.
DR EMBL; AY124000; AAM74509.1; -; mRNA.
DR EMBL; BT002284; AAN72295.1; -; mRNA.
DR PIR; A85355; A85355.
DR RefSeq; NP_194765.2; NM_119182.4.
DR AlphaFoldDB; Q8L7Z0; -.
DR BioGRID; 14446; 19.
DR IntAct; Q8L7Z0; 16.
DR STRING; 3702.AT4G30360.1; -.
DR TCDB; 1.A.1.5.36; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q8L7Z0; -.
DR PRIDE; Q8L7Z0; -.
DR ProteomicsDB; 241237; -.
DR EnsemblPlants; AT4G30360.1; AT4G30360.1; AT4G30360.
DR GeneID; 829159; -.
DR Gramene; AT4G30360.1; AT4G30360.1; AT4G30360.
DR KEGG; ath:AT4G30360; -.
DR Araport; AT4G30360; -.
DR TAIR; locus:2118816; AT4G30360.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR InParanoid; Q8L7Z0; -.
DR OMA; RIACFVA; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q8L7Z0; -.
DR PRO; PR:Q8L7Z0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7Z0; baseline and differential.
DR Genevisible; Q8L7Z0; 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: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 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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
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; 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..720
FT /note="Cyclic nucleotide-gated ion channel 17"
FT /id="PRO_0000219345"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 617..646
FT /note="IQ"
FT REGION 597..612
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT BINDING 481..605
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 552
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 83361 MW; 423B6B7602A30E4B CRC64;
MELRKDKLLM FYSEGKESKE AKWAVNDPMS KSYKLSLPSA LRPDNLLPGN RLRYTDASKS
KSSKVSWYKT ILDPGSEIVL KWNWVFIVSC MVALFIDPLY FFVPAIGGDK NYPCARTDTS
LSILVTFFRT IADLFYLLHI FIKFRTGFIA PNSSTRVFGR GELVMDPKAI AWRYIKSDFI
IDLIATLPLP QIVIWFVIST TKSYRFDHNN NAIALIVLLQ YIPRFYLIIP LSSQIVKATG
VVTKTAWAGA AYNLLLYMLA SHVLGAAWYI LSVDRYTSCW KSRCNGEAGQ VNCQLYYLDC
DSMYDNNQMT WANVTKVFKL CDARNGEFKY GIFGNAITKN VVSSQFFERY FYCLWWGLQQ
LSSYGQNLST TMFMGETTFA VLIAIFGLVL FAHLIGNMQT YLQSLTVRLE EWRLKKRDTE
EWMRHRQLPE ELRNRVRRYE QYKWLATRGV DEEVLLQSLP TDLRRDIQRH LCLDLVRRVP
FFSQMDDQLL DAICERLVSS LCTEGTYLVR EGDLISEMLF IIRGRLESST TNGGRTGFFN
SIILRPGDFC GEELLSWALL PKSTLNLPSS TRTVRALVEV EAFALRAEDL KFVANQFRRL
HSKKLQHTFR FYSHHWRTWA ACFIQAAWRR YKRRVMENNL TAIESMENEE GEVGEELVVV
EEEECVEESP RTKMNLGVMV LASRFAANTR RGVAAQRVKD VELPRFKKPE EPDFSAEHDD
