CN15B_MEDTR
ID CN15B_MEDTR Reviewed; 620 AA.
AC G7JND3; A0A0C3WX45;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Protein CNGC15b {ECO:0000303|PubMed:27230377};
DE AltName: Full=Cyclic nucleotide-gated ion channel protein 15 b {ECO:0000303|PubMed:27230377};
GN Name=CNGC15B {ECO:0000303|PubMed:27230377};
GN OrderedLocusNames=MTR_4g058730 {ECO:0000312|EnsemblPlants:AES88563};
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; CM001220; AES88563.2; -; Genomic_DNA.
DR RefSeq; XP_003606366.2; XM_003606318.2.
DR AlphaFoldDB; G7JND3; -.
DR STRING; 3880.AES88563; -.
DR PRIDE; G7JND3; -.
DR EnsemblPlants; AES88563; AES88563; MTR_4g058730.
DR Gramene; AES88563; AES88563; MTR_4g058730.
DR KEGG; mtr:MTR_4g058730; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_013069_3_0_1; -.
DR OrthoDB; 1073751at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
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..620
FT /note="Protein CNGC15b"
FT /id="PRO_0000437093"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 462..559
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
SQ SEQUENCE 620 AA; 71425 MW; DAA300299FBBF9B4 CRC64;
MVTPKFMSDL FEGDHLELAK LTSPNGDNGI KFNEKHVAPR VLSRVFSEDY KRVKRRRRIF
DPRGQTIHQW NKIFLVACLI SLFVDPLFFY LPIVQDEVCI DIGIAVEVFL IIIRSIADVF
YVIHIFMRFH TAYVAPSSRV FGRGELVIDS SKIASRYLHK GFFLDFIAAL PLPQVLIWIV
IPNLGGSTIA NTKNVLRFII IIQYLPRLFL IFPLSSQIVK ATGVVTETAW AGAAYNLMLY
MLASHVLGAC WYLLSIERQE ACWKSVCKLE ESSCQFDFFD CNMVKDSLRV SWFVTSNVTN
LCSPNSLFYQ FGIYGDAVTS KVTTSAFFNK YFFCLWWGLR NLSSLGQGLL TSTFVGEIMF
AIVIATLGLV LFALLIGNMQ TYLQSTTVRL EEWRVKRTDT EQWMHHRQLP QELRQSVRKY
DQYKWIATRG VDEESLLRGL PLDLRRDIKR HLCLELVRRV PLFDAMDERM LDAICERLKP
ALCTENTYLV REGDPVNEML FIIRGNLDSY TTDGGRTGFF NSCRIGPGDF CGEELLTWAL
DPRPTMVIPS STRTVKAISE VEAFALIAED LKFVASQFRR LHSKQLRNKL RFHSHQWRTW
AACFIQVAWR RTIQEKKGSC
