CN15A_MEDTR
ID CN15A_MEDTR Reviewed; 710 AA.
AC G7IBJ4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Protein CNGC15a {ECO:0000303|PubMed:27230377};
DE AltName: Full=Cyclic nucleotide-gated ion channel protein 15 a {ECO:0000303|PubMed:27230377};
GN Name=CNGC15A {ECO:0000303|PubMed:27230377};
GN OrderedLocusNames=MTR_1g064240 {ECO:0000312|EnsemblPlants:AES60733};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001217; AES60733.1; -; Genomic_DNA.
DR RefSeq; XP_003590482.1; XM_003590434.2.
DR AlphaFoldDB; G7IBJ4; -.
DR STRING; 3880.AES60733; -.
DR EnsemblPlants; AES60733; AES60733; MTR_1g064240.
DR GeneID; 11433273; -.
DR Gramene; AES60733; AES60733; MTR_1g064240.
DR KEGG; mtr:MTR_1g064240; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR OMA; INIWNKC; -.
DR OrthoDB; 1073751at2759; -.
DR Proteomes; UP000002051; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 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..710
FT /note="Protein CNGC15a"
FT /id="PRO_0000437092"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 474..559
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
SQ SEQUENCE 710 AA; 81946 MW; 1CFA701DD65423D9 CRC64;
MASVISRAVR FHDDLEKEKL QEGEESHMEM RAYEMSSEYK HGKDAINKPS SNGRGLSRVF
SEDYDAGEIL VFDPRGPRIN LWNKIFLAAC LISLFVDPLF FYLPVAKKEK CIDMSIGLEV
SLTIIRTFVD AFYIIHIYIR FQTAYIAPSS RVSGRGELII DSSKIASNYM KKELWSDLVA
ALPLPQVLIW AVIPNIKGSE MIASRHVVRL VSIFQYLLRL YLIYPLSSKI TKASGVMMEK
AWAGAAYYLT LYMLASHVLG STWYLLSIER QDECWKKACT LQYPHCQYHY LDCQSLSDPN
RNAWLKSSNL SGLCDQNSHF FQFGIFDDAV TLEITSSNFL TKYYYCLWWG LRNLSSSGEN
LLTSTHVAEI NFAVIVAILG LVLFALLIGN MQTYLQSTTI RLEEWRIRRT DTERWMHHRQ
LPHYLKENVR RHDQFRWVAT RGVDEEAILR DLPVDLRRDI KRHLCLNLVR QVPLFDQMDD
RMLDAICERL KPTLCTPGTC IVREGDPVDE MLFIVRGRLD SCTTNGGRTG FFNTCRIGSG
DFCGEELLPW ALDPRPTAVL PSSTRTVRAI TEVEAFALIA EDLKFVAAQF RRLHSKQLRQ
TFRFYSHQWR TWAACFIQAA WFRYKRMKET NEVKEKENLM MMSNVKYYGN DDSQYFSAPL
QVPKGSSYSM YSGKLVGSLR RGRSMRYGSE LDMLGTLRKP IEPDFNDDGD
