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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}.
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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
 
 
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