GenomeNet

Database: UniProt
Entry: CNG17_ARATH
LinkDB: CNG17_ARATH
Original site: 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   25-OCT-2017, entry version 123.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   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 WITH AHA1; AHA2 AND BAK1, LACK OF
RP   INTERACTION WITH 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.,
RA   Sauter M.;
RT   "Phytosulfokine regulates growth in Arabidopsis through a response
RT   module at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED
RT   CHANNEL17, H+-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
CC       with AHAs that is activated by PSKR1/BAK1 and possibly other
CC       BAK1/RLK complexes (PubMed:26071421). Required for PSK-induced
CC       protoplast expansion (PubMed:26071421).
CC       {ECO:0000269|PubMed:26071421, 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
CC       with PSKR1 or BRI1 (PubMed:26071421).
CC       {ECO:0000269|PubMed:26071421, 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
CC       interfere with cyclic nucleotide binding and thus channel
CC       activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB81029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   UniGene; At.31840; -.
DR   UniGene; At.69303; -.
DR   ProteinModelPortal; Q8L7Z0; -.
DR   SMR; Q8L7Z0; -.
DR   BioGrid; 14446; 19.
DR   STRING; 3702.AT4G30360.1; -.
DR   PaxDb; Q8L7Z0; -.
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   eggNOG; ENOG410XPSE; LUCA.
DR   HOGENOM; HOG000238338; -.
DR   InParanoid; Q8L7Z0; -.
DR   KO; K05391; -.
DR   OMA; CFRTIAD; -.
DR   OrthoDB; EOG093603YI; -.
DR   PhylomeDB; Q8L7Z0; -.
DR   Reactome; R-ATH-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-ATH-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-ATH-5620916; VxPx cargo-targeting to cilium.
DR   PRO; PR:Q8L7Z0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8L7Z0; baseline and differential.
DR   Genevisible; Q8L7Z0; AT.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
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;
KW   cGMP-binding; Complete proteome; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    720       Cyclic nucleotide-gated ion channel 17.
FT                                /FTId=PRO_0000219345.
FT   TOPO_DOM      1     85       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     86    106       Helical; Name=H1. {ECO:0000255}.
FT   TOPO_DOM    107    121       Extracellular. {ECO:0000255}.
FT   TRANSMEM    122    142       Helical; Name=H2. {ECO:0000255}.
FT   TOPO_DOM    143    178       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    179    199       Helical; Name=H3. {ECO:0000255}.
FT   TOPO_DOM    200    211       Extracellular. {ECO:0000255}.
FT   TRANSMEM    212    232       Helical; Name=H4. {ECO:0000255}.
FT   TOPO_DOM    233    252       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    253    273       Helical; Name=H5. {ECO:0000255}.
FT   TOPO_DOM    274    377       Extracellular. {ECO:0000255}.
FT   TRANSMEM    378    398       Helical; Name=H6. {ECO:0000255}.
FT   TOPO_DOM    399    720       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      617    646       IQ.
FT   NP_BIND     481    605       cNMP.
FT   REGION      597    612       Calmodulin-binding. {ECO:0000250}.
FT   BINDING     552    552       cNMP. {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
//
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