ID CN15C_MEDTR Reviewed; 703 AA.
AC A0A072VMJ3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein CNGC15c {ECO:0000303|PubMed:27230377};
DE AltName: Full=Cyclic nucleotide-gated ion channel protein 15 c {ECO:0000303|PubMed:27230377};
GN Name=CNGC15C {ECO:0000303|PubMed:27230377};
GN OrderedLocusNames=MTR_2g094860 {ECO:0000312|EnsemblPlants:KEH39345};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000312|Proteomes:UP000002051};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH DMI1,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=27230377; DOI=10.1126/science.aae0109;
RA Charpentier M., Sun J., Martins T.V., Radhakrishnan G.V., Findlay K.,
RA Soumpourou E., Thouin J., Very A.A., Sanders D., Morris R.J., Oldroyd G.E.;
RT "Nuclear-localized cyclic nucleotide-gated channels mediate symbiotic
RT calcium oscillations.";
RL Science 352:1102-1105(2016).
CC -!- FUNCTION: Cyclic nucleotide-gated channel involved in the establishment
CC of both rhizobial and mycorrhizal associations (PubMed:27230377).
CC Required for full activation of nuclear-localized Ca(2+) oscillations
CC by Nod and Myc factors (PubMed:27230377). Simultaneous activation of
CC the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give
CC rise to sustained Ca(2+) oscillations (PubMed:27230377). May function
CC during fertilization in both female and male gametophytic Ca(2+)
CC signaling (PubMed:27230377). {ECO:0000269|PubMed:27230377}.
CC -!- SUBUNIT: Interacts (via N-terminus) with DMI1 (via c-terminus). The Nod
CC factor has no effect on this interaction, implying that the complex is
CC maintained after activation. {ECO:0000269|PubMed:27230377}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:27230377};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC pods. {ECO:0000269|PubMed:27230377}.
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; CM001218; KEH39345.1; -; Genomic_DNA.
DR RefSeq; XP_013465310.1; XM_013609856.1.
DR AlphaFoldDB; A0A072VMJ3; -.
DR STRING; 3880.A0A072VMJ3; -.
DR EnsemblPlants; KEH39345; KEH39345; MTR_2g094860.
DR GeneID; 25487817; -.
DR Gramene; KEH39345; KEH39345; MTR_2g094860.
DR KEGG; mtr:25487817; -.
DR HOGENOM; CLU_013069_3_0_1; -.
DR OrthoDB; 3076617at2759; -.
DR Proteomes; UP000002051; Chromosome 2.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45651; CYCLIC NUCLEOTIDE-GATED ION CHANNEL 15-RELATED-RELATED; 1.
DR PANTHER; PTHR45651:SF108; PROTEIN CNGC15C; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
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.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..703
FT /note="Protein CNGC15c"
FT /id="PRO_0000437094"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 616..644
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..565
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
SQ SEQUENCE 703 AA; 80770 MW; 3914EF145F87AEC4 CRC64;
MGFDNPRSER FEDDPEISKI PTTSGVKVKY HIDGTQIPEQ SSKKSRKNET RNKFLKTRVL
SRVFSEDYER VKKRVLVLDP RGQLIHRWNK IFLVACLVSL FVDPLFFYLP VVREEVCIDI
GKTLEVILTV VRSFGDLFYI VQICMKFRTA YVAPSSKVFG RGELVLTYSK IALRYFSKGF
WLDFIAALPL PQVLIWIIIP TLRGSTMANT KNVLRFFIIF QYIPRLYLIF PLSSQIVKAT
GVVTETAWAG AAYNLMLYML ASHILGACWY LLSIERQEAC WKSVCNMEKS NCQYGFFNCH
SIKDAPRVAW FIASNVTNLC SPNAGFYPFG IYADAMTSKV TSSPFFNKYF YCLWWGLRNL
SSLGQGLLTS TFIGEIMVAI VVATLGLVLF ALLIGNMQTY LQSITVRLEE WRVKRTDTEQ
WMHHRQLPPE LRESIRKYNQ YKWVATRGVE EEDLLKGLPL DLRREIKRHL CLELVRGVPL
FDQMDERMLD AICERLKPAL CTEGTYLVRE GDPVNEMLFI IRGHLDSYTT NGGRDGFFNS
CRIGPGDFCG EELLTWALDP RPSVILPSST RTVKAFSEVE AFALIAEDLK FVASQFRRLH
SKQLRHKFRF YSHQWRTWAA CFIQAAWRRH KKRKEAAELR AKENLVAASE AENEIAKKYG
KGFVVYGTRV ARSTRKGVNM HSGTNSGVVS SLQKPTEPDF SDE
//
