ID CNG18_ARATH Reviewed; 706 AA.
AC Q9LEQ3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 152.
DE RecName: Full=Cyclic nucleotide-gated ion channel 18 {ECO:0000303|PubMed:11500563};
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 18 {ECO:0000303|PubMed:11500563};
GN Name=CNGC18 {ECO:0000303|PubMed:11500563};
GN OrderedLocusNames=At5g14870 {ECO:0000312|Araport:AT5G14870};
GN ORFNames=T9L3_170 {ECO:0000312|EMBL:CAC01886.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17726111; DOI=10.1073/pnas.0701781104;
RA Frietsch S., Wang Y.F., Sladek C., Poulsen L.R., Romanowsky S.M.,
RA Schroeder J.I., Harper J.F.;
RT "A cyclic nucleotide-gated channel is essential for polarized tip growth of
RT pollen.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14531-14536(2007).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24380879; DOI=10.1093/mp/sst174;
RA Gao Q.F., Fei C.F., Dong J.Y., Gu L.L., Wang Y.F.;
RT "Arabidopsis CNGC18 is a Ca(2+)-permeable channel.";
RL Mol. Plant 7:739-743(2014).
RN [6]
RP FUNCTION, INTERACTION WITH CPK32, AND SUBCELLULAR LOCATION.
RX PubMed=24121288; DOI=10.1093/mp/sst125;
RA Zhou L., Lan W., Jiang Y., Fang W., Luan S.;
RT "A calcium-dependent protein kinase interacts with and activates a calcium
RT channel to regulate pollen tube growth.";
RL Mol. Plant 7:369-376(2014).
RN [7]
RP FUNCTION, MUTAGENESIS OF ARG-491 AND ARG-578, AND DOMAIN.
RX PubMed=26929345; DOI=10.1073/pnas.1524629113;
RA Gao Q.F., Gu L.L., Wang H.Q., Fei C.F., Fang X., Hussain J., Sun S.J.,
RA Dong J.Y., Liu H., Wang Y.F.;
RT "Cyclic nucleotide-gated channel 18 is an essential Ca2+ channel in pollen
RT tube tips for pollen tube guidance to ovules in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3096-3101(2016).
CC -!- FUNCTION: Cyclic nucleotide-gated ion channel required for directional
CC pollen tube growth into the transmitting tract (PubMed:17726111,
CC PubMed:26929345). Acts as a Ca(2+)-permeable divalent cation-selective
CC channel inhibited by either lanthanum or gadolinium (PubMed:24380879).
CC Regulated by CPK32 to mediate Ca(2+) transport across the plasma
CC membrane in response to Ca(2+) oscillation (PubMed:24121288).
CC {ECO:0000269|PubMed:17726111, ECO:0000269|PubMed:24121288,
CC ECO:0000269|PubMed:24380879, ECO:0000269|PubMed:26929345}.
CC -!- SUBUNIT: Homomultimer (PubMed:24380879). Interacts with CPK32
CC (PubMed:24121288). {ECO:0000269|PubMed:24121288,
CC ECO:0000269|PubMed:24380879}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17726111,
CC ECO:0000269|PubMed:24121288}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17726111}; Multi-pass membrane protein
CC {ECO:0000305}. Note=focused at the cell perimeter of the growing pollen
CC tube tip. {ECO:0000269|PubMed:17726111, ECO:0000269|PubMed:24121288}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains. Not detected in leaves,
CC roots or root hairs. {ECO:0000269|PubMed:17726111}.
CC -!- DOMAIN: The transmembrane domains are indispensable for pollen tube
CC guidance. {ECO:0000269|PubMed:26929345}.
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: Male sterility. {ECO:0000269|PubMed:17726111}.
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; AL391149; CAC01886.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92084.1; -; Genomic_DNA.
DR PIR; T51432; T51432.
DR RefSeq; NP_196991.1; NM_121491.3.
DR AlphaFoldDB; Q9LEQ3; -.
DR BioGRID; 16616; 19.
DR IntAct; Q9LEQ3; 17.
DR STRING; 3702.Q9LEQ3; -.
DR TCDB; 1.A.1.5.26; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; 3702-AT5G14870-1; -.
DR ProteomicsDB; 241238; -.
DR EnsemblPlants; AT5G14870.1; AT5G14870.1; AT5G14870.
DR GeneID; 831339; -.
DR Gramene; AT5G14870.1; AT5G14870.1; AT5G14870.
DR KEGG; ath:AT5G14870; -.
DR Araport; AT5G14870; -.
DR TAIR; AT5G14870; CNGC18.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR InParanoid; Q9LEQ3; -.
DR OMA; SRADHAN; -.
DR OrthoDB; 3076617at2759; -.
DR PhylomeDB; Q9LEQ3; -.
DR PRO; PR:Q9LEQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LEQ3; baseline and differential.
DR Genevisible; Q9LEQ3; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IDA:TAIR.
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:0006874; P:intracellular calcium ion homeostasis; IDA:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP: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; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45651; CYCLIC NUCLEOTIDE-GATED ION CHANNEL 15-RELATED-RELATED; 1.
DR PANTHER; PTHR45651:SF102; CYCLIC NUCLEOTIDE-GATED ION CHANNEL 18; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
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.
PE 1: Evidence at protein level;
KW Calmodulin-binding; cAMP; cAMP-binding; Cell membrane; cGMP; cGMP-binding;
KW Cytoplasmic vesicle; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Cyclic nucleotide-gated ion channel 18"
FT /id="PRO_0000219346"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 585..614
FT /note="IQ"
FT REGION 565..580
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 661..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..579
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 520
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
FT MUTAGEN 491
FT /note="R->Q: Impaired cGMP activation of the Ca(2+) channel
FT and strong defects in pollen tube guidance."
FT /evidence="ECO:0000269|PubMed:26929345"
FT MUTAGEN 578
FT /note="R->K: Impaired cGMP activation of the Ca(2+) channel
FT and strong defects in pollen tube guidance."
FT /evidence="ECO:0000269|PubMed:26929345"
SQ SEQUENCE 706 AA; 80364 MW; 05122006E5A59CEB CRC64;
MNKIRSLRCL LPETITSAST AASNRGSDGS QFSVLWRHQI LDPDSNIVTY WNHVFLITSI
LALFLDPFYF YVPYVGGPAC LSIDISLAAT VTFFRTVADI FHLLHIFMKF RTAFVARSSR
VFGRGELVMD SREIAMRYLK TDFLIDVAAM LPLPQLVIWL VIPAATNGTA NHANSTLALI
VLVQYIPRSF IIFPLNQRII KTTGFIAKTA WAGAAYNLLL YILASHVLGA MWYLSSIGRQ
FSCWSNVCKK DNALRVLDCL PSFLDCKSLE QPERQYWQNV TQVLSHCDAT SSTTNFKFGM
FAEAFTTQVA TTDFVSKYLY CLWWGLRNLS SYGQNITTSV YLGETLFCIT ICIFGLILFT
LLIGNMQSSL QSMSVRVEEW RVKRRDTEEW MRHRQLPPEL QERVRRFVQY KWLATRGVDE
ESILHSLPTD LRREIQRHLC LSLVRRVPFF SQMDDQLLDA ICGCLVSSLS TAGTYIFREG
DPVNEMLFVI RGQIESSTTN GGRSGFFNST TLRPGDFCGE ELLTWALMPN STLNLPSSTR
SVRALSEVEA FALSAEDLKF VAHQFKRLQS KKLQHAFRYY SHQWRAWGAC FVQSAWRRYK
RRKLAKELSL HESSGYYYPD ETGYNEEDEE TREYYYGSDE EGGSMDNTNL GATILASKFA
ANTRRGTNQK ASSSSTGKKD GSSTSLKMPQ LFKPDEPDFS IDKEDV
//
