CNGC3_ARATH
ID CNGC3_ARATH Reviewed; 706 AA.
AC Q9SKD7; Q9XFS1; Q9ZPK1;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable cyclic nucleotide-gated ion channel 3;
DE Short=AtCNGC3;
DE AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 3;
GN Name=CNGC3; OrderedLocusNames=At2g46430; ORFNames=F11C10.12;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10341447; DOI=10.1046/j.1365-313x.1999.00422.x;
RA Koehler C., Merkle T., Neuhaus G.;
RT "Characterisation of a novel gene family of putative cyclic nucleotide- and
RT calmodulin-regulated ion channels in Arabidopsis thaliana.";
RL Plant J. 18:97-104(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chattaway J., Fischer M., Sanders D.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
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 -!- 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}.
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DR EMBL; Y17911; CAB40128.1; -; Genomic_DNA.
DR EMBL; AF107726; AAD19610.1; -; mRNA.
DR EMBL; AC006526; AAD23045.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10694.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10695.1; -; Genomic_DNA.
DR EMBL; AY058167; AAL25581.1; -; mRNA.
DR PIR; G84902; G84902.
DR RefSeq; NP_001118537.1; NM_001125065.2.
DR RefSeq; NP_566075.1; NM_130207.4.
DR AlphaFoldDB; Q9SKD7; -.
DR STRING; 3702.AT2G46430.1; -.
DR TCDB; 1.A.1.5.8; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q9SKD7; -.
DR PRIDE; Q9SKD7; -.
DR ProteomicsDB; 220296; -.
DR EnsemblPlants; AT2G46430.1; AT2G46430.1; AT2G46430.
DR EnsemblPlants; AT2G46430.2; AT2G46430.2; AT2G46430.
DR GeneID; 819251; -.
DR Gramene; AT2G46430.1; AT2G46430.1; AT2G46430.
DR Gramene; AT2G46430.2; AT2G46430.2; AT2G46430.
DR KEGG; ath:AT2G46430; -.
DR Araport; AT2G46430; -.
DR TAIR; locus:2039084; AT2G46430.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR InParanoid; Q9SKD7; -.
DR OMA; IDAFYVV; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q9SKD7; -.
DR PRO; PR:Q9SKD7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKD7; baseline and differential.
DR Genevisible; Q9SKD7; 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 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; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 2: Evidence at transcript 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..706
FT /note="Probable cyclic nucleotide-gated ion channel 3"
FT /id="PRO_0000219331"
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..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 611..640
FT /note="IQ"
FT REGION 591..606
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT BINDING 477..600
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT BINDING 548
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="T -> N (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> N (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..291
FT /note="NCTHAY -> DCSHEK (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> S (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="P -> A (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="R -> K (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="L -> V (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="E -> Q (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="G -> GG (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="Y -> N (in Ref. 2; AAD19610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 81669 MW; FF721536599A04BC CRC64;
MMNPQRNKFV RFNGNDDEFS TKTTRPSVSS VMKTVRRSFE KGSEKIRTFK RPLSVHSNKN
KENNKKKKIL RVMNPNDSYL QSWNKIFLLL SVVALAFDPL FFYIPYVKPE RFCLNLDKKL
QTIACVFRTF IDAFYVVHML FQFHTGFITP SSSGFGRGEL NEKHKDIALR YLGSYFLIDL
LSILPIPQVV VLAIVPRMRR PASLVAKELL KWVIFCQYVP RIARIYPLFK EVTRTSGLVT
ETAWAGAALN LFLYMLASHV FGSFWYLISI ERKDRCWREA CAKIQNCTHA YLYCSPTGED
NRLFLNGSCP LIDPEEITNS TVFNFGIFAD ALQSGVVESR DFPKKFFYCF WWGLRNLSAL
GQNLKTSAFE GEIIFAIVIC ISGLVLFALL IGNMQKYLQS TTVRVEEMRV KRRDAEQWMS
HRMLPDDLRK RIRKYEQYKW QETKGVEEEA LLSSLPKDLR KDIKRHLCLK LLKKVPWFQA
MDDRLLDALC ARLKTVLYTE KSYIVREGEP VEDMLFIMRG NLISTTTYGG RTGFFNSVDL
VAGDFCGDLL TWALDPLSSQ FPISSRTVQA LTEVEGFLLS ADDLKFVATQ YRRLHSKQLR
HMFRFYSVQW QTWAACFIQA AWKRHCRRKL SKALREEEGK LHNTLQNDDS GGNKLNLGAA
IYASRFASHA LRNLRANAAA RNSRFPHMLT LLPQKPADPE FPMDET
