CCLOP_MEDTR
ID CCLOP_MEDTR Reviewed; 513 AA.
AC A7TUE1;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Protein CYCLOPS {ECO:0000303|PubMed:19074278};
DE Short=MtCYCLOPS {ECO:0000303|PubMed:19074278};
DE AltName: Full=DMI3-interacting protein IPD3 {ECO:0000305};
DE AltName: Full=Interacting protein of DMI3 {ECO:0000303|PubMed:17722695};
DE Short=MtIPD3 {ECO:0000303|PubMed:17722695};
DE AltName: Full=MtSYM1 {ECO:0000303|PubMed:21787150};
GN Name=IPD3 {ECO:0000303|PubMed:17722695};
GN OrderedLocusNames=MTR_5g026850 {ECO:0000312|EMBL:AES95561.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], HOMODIMERIZATION, INTERACTION WITH
RP CCAMK, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17722695; DOI=10.1094/mpmi-20-8-0912;
RA Messinese E., Mun J.H., Yeun L.H., Jayaraman D., Rouge P., Barre A.,
RA Lougnon G., Schornack S., Bono J.J., Cook D.R., Ane J.M.;
RT "A novel nuclear protein interacts with the symbiotic DMI3 calcium- and
RT calmodulin-dependent protein kinase of Medicago truncatula.";
RL Mol. Plant Microbe Interact. 20:912-921(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19074278; DOI=10.1073/pnas.0806858105;
RA Yano K., Yoshida S., Mueller J., Singh S., Banba M., Vickers K.,
RA Markmann K., White C., Schuller B., Sato S., Asamizu E., Tabata S.,
RA Murooka Y., Perry J., Wang T.L., Kawaguchi M., Imaizumi-Anraku H.,
RA Hayashi M., Parniske M.;
RT "CYCLOPS, a mediator of symbiotic intracellular accommodation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20540-20545(2008).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=17449807; DOI=10.1105/tpc.106.048264;
RA Middleton P.H., Jakab J., Penmetsa R.V., Starker C.G., Doll J., Kalo P.,
RA Prabhu R., Marsh J.F., Mitra R.M., Kereszt A., Dudas B., Vandenbosch K.,
RA Long S.R., Cook D.R., Kiss G.B., Oldroyd G.E.;
RT "An ERF transcription factor in Medicago truncatula that is essential for
RT Nod factor signal transduction.";
RL Plant Cell 19:1221-1234(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21787150; DOI=10.1094/mpmi-01-11-0013;
RA Ovchinnikova E., Journet E.P., Chabaud M., Cosson V., Ratet P., Duc G.,
RA Fedorova E., Liu W., den Camp R.O., Zhukov V., Tikhonovich I., Borisov A.,
RA Bisseling T., Limpens E.;
RT "IPD3 controls the formation of nitrogen-fixing symbiosomes in pea and
RT Medicago Spp.";
RL Mol. Plant Microbe Interact. 24:1333-1344(2011).
RN [7]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH CCAMK, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21692638; DOI=10.1094/mpmi-01-11-0015;
RA Horvath B., Yeun L.H., Domonkos A., Halasz G., Gobbato E., Ayaydin F.,
RA Miro K., Hirsch S., Sun J., Tadege M., Ratet P., Mysore K.S., Ane J.M.,
RA Oldroyd G.E., Kalo P.;
RT "Medicago truncatula IPD3 is a member of the common symbiotic signaling
RT pathway required for rhizobial and mycorrhizal symbioses.";
RL Mol. Plant Microbe Interact. 24:1345-1358(2011).
CC -!- FUNCTION: Involved symbiotic signaling. Required for root infection by
CC symbiotic rhizobia, infection thread (IT) formation, and nodule
CC development. Required for proper induction of early nodulin gene
CC expression. Probably not involved in nodule organogenesis. Involved in
CC arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of
CC the outer cortical cell layers, and for arbuscule development during
CC the AM symbiosis. Acts downstream of CCAMK (PubMed:21692638). Required
CC for symbiosome formation (i.e. the release of the bacteria from the
CC ITs) and subsequent symbiosome development. Required for the expression
CC of the nodule-specific RPG gene, which controls proper IT growth and is
CC essential for symbiosome formation (PubMed:21787150). Acts upstream of
CC ERN1, a transcriptional regulator required for nodulation
CC (PubMed:17449807). {ECO:0000269|PubMed:17449807,
CC ECO:0000269|PubMed:21692638, ECO:0000269|PubMed:21787150}.
CC -!- SUBUNIT: Forms homodimers. Interacts with CCAMK.
CC {ECO:0000269|PubMed:17722695, ECO:0000269|PubMed:21692638}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17722695,
CC ECO:0000269|PubMed:21787150}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in root hairs
CC and nodules. Not detected in leaves or flowers.
CC {ECO:0000269|PubMed:17722695}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but roots of mutant plants are impaired in the interaction
CC with both rhizobia and the arbuscular mycorrhiza (AM) fungus Glomus
CC intraradices. Stunted growth when grown in nitrogen-limiting conditions
CC and in presence of Sinorhizobium meliloti.
CC {ECO:0000269|PubMed:21692638}.
CC -!- SIMILARITY: Belongs to the CYCLOPS family. {ECO:0000305}.
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DR EMBL; EF117279; ABN45743.1; -; Genomic_DNA.
DR EMBL; EF569224; ABU63671.1; -; mRNA.
DR EMBL; CM001221; AES95561.1; -; Genomic_DNA.
DR RefSeq; XP_003612603.1; XM_003612555.2.
DR AlphaFoldDB; A7TUE1; -.
DR STRING; 3880.AES95561; -.
DR iPTMnet; A7TUE1; -.
DR EnsemblPlants; AES95561; AES95561; MTR_5g026850.
DR GeneID; 11408651; -.
DR Gramene; AES95561; AES95561; MTR_5g026850.
DR eggNOG; ENOG502QQ45; Eukaryota.
DR OMA; FLAKAWF; -.
DR Proteomes; UP000002051; Chromosome 5.
DR ExpressionAtlas; A7TUE1; differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR InterPro; IPR040036; CYCLOPS.
DR PANTHER; PTHR36890; PTHR36890; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nodulation; Nucleus; Reference proteome.
FT CHAIN 1..513
FT /note="Protein CYCLOPS"
FT /id="PRO_0000444703"
FT REGION 329..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..513
FT /evidence="ECO:0000255"
FT MOTIF 397..400
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 421..424
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 329..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57971 MW; D476C877F8F27333 CRC64;
MEGRGFSGLY KNSSEELFLK TVMESPIGMP VPTMEMLGFK TVSQSFRTDS EELFKRWLTN
DQEGYNSSSM GLNSRLSKRI STEIANMSNQ QHIGVASEGR NNDKSCLQNN FLANDVSSDF
NFPIRDPVDR ELQSSNLFLA KAWFITDQRM TRSRSSELRR RYTEMQNSQA PQGLDSMFMV
PEHDTNTIKE ELANFNGFDY LSMCELPSQK GTFMSPSNSS SSTFNTHQLV DVDKVSSCVS
MLKGTLQRKK LECQVEKEAA EDGLNEIFCI REPLFQSAFN EEESWNQQKL VNVQGDFTDQ
VNDPGVMQTL EGTTNFVLDG FANQTNQIQG RTASGEPSQS ESSAAAPVIS SGLDACEGPS
NSNQTLGDSS WKQVGESTQN KVRGVREQIM DNLKDDRKRK SLERYGSVTS AVSDGKMDNT
KKRRVERSRK MAEAKERNLT PTIPSDMQAI LKRCENLEKE VRSLKLNLSF MNRKDSEQTK
QIEDLQKQNE DLADEKERLL EEIERILSET GKI
