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Cyclic nucleotide-gated ion channel 18 (Cyclic nucleotide- and calmodulin-regulated ion channel 18)

 CNG18_ARATH             Reviewed;         706 AA.
Q9LEQ3;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
18-JUL-2018, entry version 129.
RecName: Full=Cyclic nucleotide-gated ion channel 18 {ECO:0000303|PubMed:11500563};
AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 18 {ECO:0000303|PubMed:11500563};
Name=CNGC18 {ECO:0000303|PubMed:11500563};
OrderedLocusNames=At5g14870 {ECO:0000312|Araport:AT5G14870};
ORFNames=T9L3_170 {ECO:0000312|EMBL:CAC01886.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11500563; DOI=10.1104/pp.126.4.1646;
Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
Guerinot M.L.;
"Phylogenetic relationships within cation transporter families of
Arabidopsis.";
Plant Physiol. 126:1646-1667(2001).
[4]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=17726111; DOI=10.1073/pnas.0701781104;
Frietsch S., Wang Y.F., Sladek C., Poulsen L.R., Romanowsky S.M.,
Schroeder J.I., Harper J.F.;
"A cyclic nucleotide-gated channel is essential for polarized tip
growth of pollen.";
Proc. Natl. Acad. Sci. U.S.A. 104:14531-14536(2007).
[5]
FUNCTION, AND SUBUNIT.
PubMed=24380879; DOI=10.1093/mp/sst174;
Gao Q.F., Fei C.F., Dong J.Y., Gu L.L., Wang Y.F.;
"Arabidopsis CNGC18 is a Ca(2+)-permeable channel.";
Mol. Plant 7:739-743(2014).
[6]
FUNCTION, INTERACTION WITH CPK32, AND SUBCELLULAR LOCATION.
PubMed=24121288; DOI=10.1093/mp/sst125;
Zhou L., Lan W., Jiang Y., Fang W., Luan S.;
"A calcium-dependent protein kinase interacts with and activates a
calcium channel to regulate pollen tube growth.";
Mol. Plant 7:369-376(2014).
[7]
FUNCTION, MUTAGENESIS OF ARG-491 AND ARG-578, AND DOMAIN.
PubMed=26929345; DOI=10.1073/pnas.1524629113;
Gao Q.F., Gu L.L., Wang H.Q., Fei C.F., Fang X., Hussain J., Sun S.J.,
Dong J.Y., Liu H., Wang Y.F.;
"Cyclic nucleotide-gated channel 18 is an essential Ca2+ channel in
pollen tube tips for pollen tube guidance to ovules in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 113:3096-3101(2016).
-!- FUNCTION: Cyclic nucleotide-gated ion channel required for
directional pollen tube growth into the transmitting tract
(PubMed:17726111, PubMed:26929345). Acts as a Ca(2+)-permeable
divalent cation-selective channel inhibited by either lanthanum or
gadolinium (PubMed:24380879). Regulated by CPK32 to mediate Ca(2+)
transport across the plasma membrane in response to Ca(2+)
oscillation (PubMed:24121288). {ECO:0000269|PubMed:17726111,
ECO:0000269|PubMed:24121288, ECO:0000269|PubMed:24380879,
ECO:0000269|PubMed:26929345}.
-!- SUBUNIT: Homomultimer (PubMed:24380879). Interacts with CPK32
(PubMed:24121288). {ECO:0000269|PubMed:24121288,
ECO:0000269|PubMed:24380879}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17726111,
ECO:0000269|PubMed:24121288}; Multi-pass membrane protein
{ECO:0000305}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:17726111}; Multi-pass membrane protein
{ECO:0000305}. Note=focused at the cell perimeter of the growing
pollen tube tip. {ECO:0000269|PubMed:17726111,
ECO:0000269|PubMed:24121288}.
-!- TISSUE SPECIFICITY: Expressed in pollen grains. Not detected in
leaves, roots or root hairs. {ECO:0000269|PubMed:17726111}.
-!- DOMAIN: The transmembrane domains are indispensable for pollen
tube guidance. {ECO:0000269|PubMed:26929345}.
-!- DOMAIN: The binding of calmodulin to the C-terminus might
interfere with cyclic nucleotide binding and thus channel
activation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Male sterility.
{ECO:0000269|PubMed:17726111}.
-!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
(TC 1.A.1.5) family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL391149; CAC01886.1; -; Genomic_DNA.
EMBL; CP002688; AED92084.1; -; Genomic_DNA.
PIR; T51432; T51432.
RefSeq; NP_196991.1; NM_121491.3.
UniGene; At.31874; -.
ProteinModelPortal; Q9LEQ3; -.
SMR; Q9LEQ3; -.
BioGrid; 16616; 19.
IntAct; Q9LEQ3; 17.
STRING; 3702.AT5G14870.1; -.
TCDB; 1.A.1.5.26; the voltage-gated ion channel (vic) superfamily.
PaxDb; Q9LEQ3; -.
EnsemblPlants; AT5G14870.1; AT5G14870.1; AT5G14870.
GeneID; 831339; -.
Gramene; AT5G14870.1; AT5G14870.1; AT5G14870.
KEGG; ath:AT5G14870; -.
Araport; AT5G14870; -.
TAIR; locus:2185510; AT5G14870.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
HOGENOM; HOG000238338; -.
InParanoid; Q9LEQ3; -.
KO; K05391; -.
OMA; NIVTYWN; -.
OrthoDB; EOG093603YI; -.
PhylomeDB; Q9LEQ3; -.
PRO; PR:Q9LEQ3; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LEQ3; baseline and differential.
Genevisible; Q9LEQ3; AT.
GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005262; F:calcium channel activity; IDA:TAIR.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
1: Evidence at protein level;
Calmodulin-binding; cAMP; cAMP-binding; Cell membrane; cGMP;
cGMP-binding; Complete proteome; Cytoplasmic vesicle; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 706 Cyclic nucleotide-gated ion channel 18.
/FTId=PRO_0000219346.
TOPO_DOM 1 53 Cytoplasmic. {ECO:0000255}.
TRANSMEM 54 74 Helical; Name=H1. {ECO:0000255}.
TOPO_DOM 75 86 Extracellular. {ECO:0000255}.
TRANSMEM 87 107 Helical; Name=H2. {ECO:0000255}.
TOPO_DOM 108 142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 143 163 Helical; Name=H3. {ECO:0000255}.
TOPO_DOM 164 174 Extracellular. {ECO:0000255}.
TRANSMEM 175 195 Helical; Name=H4. {ECO:0000255}.
TOPO_DOM 196 217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 218 238 Helical; Name=H5. {ECO:0000255}.
TOPO_DOM 239 345 Extracellular. {ECO:0000255}.
TRANSMEM 346 366 Helical; Name=H6. {ECO:0000255}.
TOPO_DOM 367 706 Cytoplasmic. {ECO:0000255}.
DOMAIN 585 614 IQ.
NP_BIND 449 579 cNMP.
REGION 565 580 Calmodulin-binding. {ECO:0000250}.
BINDING 520 520 cNMP. {ECO:0000250}.
MUTAGEN 491 491 R->Q: Impaired cGMP activation of the
Ca(2+) channel and strong defects in
pollen tube guidance.
{ECO:0000269|PubMed:26929345}.
MUTAGEN 578 578 R->K: Impaired cGMP activation of the
Ca(2+) channel and strong defects in
pollen tube guidance.
{ECO:0000269|PubMed:26929345}.
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


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