CNG10_ARATH
ID CNG10_ARATH Reviewed; 711 AA.
AC Q9LNJ0; Q9LKL3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable cyclic nucleotide-gated ion channel 10;
DE AltName: Full=CaM-regulated potassium ion channel;
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 10;
GN Name=CNGC10; Synonyms=ACBK1; OrderedLocusNames=At1g01340; ORFNames=F6F3.13;
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 [MRNA] (ISOFORM 2).
RA Li X., Dharmasiri M.A., Harrington M.H.;
RT "CaM-regulated potassium ion channel.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [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).
CC -!- FUNCTION: Probable 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LNJ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LNJ0-2; Sequence=VSP_008988;
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97331.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF272002; AAF76224.3; -; mRNA.
DR EMBL; AC023628; AAF97331.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27273.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27274.1; -; Genomic_DNA.
DR PIR; F86143; F86143.
DR RefSeq; NP_001184885.1; NM_001197956.2. [Q9LNJ0-1]
DR RefSeq; NP_563625.1; NM_100016.3. [Q9LNJ0-2]
DR AlphaFoldDB; Q9LNJ0; -.
DR BioGRID; 24071; 34.
DR STRING; 3702.AT1G01340.2; -.
DR PaxDb; Q9LNJ0; -.
DR PRIDE; Q9LNJ0; -.
DR ProteomicsDB; 220392; -. [Q9LNJ0-1]
DR EnsemblPlants; AT1G01340.1; AT1G01340.1; AT1G01340. [Q9LNJ0-2]
DR EnsemblPlants; AT1G01340.2; AT1G01340.2; AT1G01340. [Q9LNJ0-1]
DR GeneID; 838832; -.
DR Gramene; AT1G01340.1; AT1G01340.1; AT1G01340. [Q9LNJ0-2]
DR Gramene; AT1G01340.2; AT1G01340.2; AT1G01340. [Q9LNJ0-1]
DR KEGG; ath:AT1G01340; -.
DR Araport; AT1G01340; -.
DR TAIR; locus:2035347; AT1G01340.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q9LNJ0; -.
DR OMA; QMVILAM; -.
DR PhylomeDB; Q9LNJ0; -.
DR PRO; PR:Q9LNJ0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNJ0; baseline and differential.
DR Genevisible; Q9LNJ0; 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:0005216; F:ion 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; 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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calmodulin-binding; cAMP; cAMP-binding;
KW Cell membrane; cGMP; cGMP-binding; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..711
FT /note="Probable cyclic nucleotide-gated ion channel 10"
FT /id="PRO_0000219338"
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..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..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..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 609..638
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 589..604
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 689..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..603
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 544
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..9
FT /note="MAFSHDNRV -> MILF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_008988"
SQ SEQUENCE 711 AA; 81895 MW; D38AA46664B50928 CRC64;
MAFSHDNRVR FKDEGKPLSS EYGYGRKARP SLDRVFKNVK WGFKKPLSFP SHKDPDHKET
SSVTRKNIIN PQDSFLQNWN KIFLFACVVA LAIDPLFFYI PIVDSARHCL TLDSKLEIAA
SLLRTLIDAF YIIHIVFQFR TAYIAPSSRV FGRGELVDDA KAIALKYLSS YFIIDLLSIL
PLPQIVVLAV IPSVNQPVSL LTKDYLKFSI IAQYVPRILR MYPLYTEVTR TSGIVTETAW
AGAAWNLSLY MLASHVFGAL WYLISVERED RCWQEACEKT KGCNMKFLYC ENDRNVSNNF
LTTSCPFLDP GDITNSTIFN FGIFTDALKS GVVESHDFWK KFFYCFWWGL RNLSALGQNL
QTSKFVGEII FAISICISGL VLFALLIGNM QKYLESTTVR EEEMRVRKRD AEQWMSHRML
PEDLRKRIRR YEQYRWQETR GVEEETLLRN LPKDLRRDIK RHLCLDLLKK VPLFEIMDEQ
LLDAVCDRLR PVLYTENSYV IREGDPVGEM LFVMRGRLVS ATTNGGRSGF FNAVNLKASD
FCGEDLLPWA LDPQSSSHFP ISTRTVQALT EVEAFALTAE DLKSVASQFR RLHSKQLQHT
FRFYSVQWRT WSVSFIQAAW RRYCRRKLAK SLRDEEDRLR EALASQDKEH NAATVSSSLS
LGGALYASRF ASNALHNLRH NISNLPPRYT LPLLPQKPTE PDFTANHTTD P
