NOOT2_MEDTR
ID NOOT2_MEDTR Reviewed; 492 AA.
AC A0A072VIM5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=BTB/POZ domain and ankyrin repeat-containing protein NOOT2 {ECO:0000305};
DE AltName: Full=Protein NODULE ROOT 2 {ECO:0000303|PubMed:30026291};
DE Short=MtNOOT2 {ECO:0000303|PubMed:30026291};
GN Name=NOOT2 {ECO:0000303|PubMed:30026291};
GN OrderedLocusNames=MTR_1g051025 {ECO:0000312|EMBL:KEH41446.1};
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30026291; DOI=10.1104/pp.18.00610;
RA Magne K., Couzigou J.M., Schiessl K., Liu S., George J., Zhukov V.,
RA Sahl L., Boyer F., Iantcheva A., Mysore K.S., Wen J., Citerne S.,
RA Oldroyd G.E.D., Ratet P.;
RT "MtNODULE ROOT1 and MtNODULE ROOT2 are essential for indeterminate nodule
RT identity.";
RL Plant Physiol. 178:295-316(2018).
CC -!- FUNCTION: Involved in the regulation of indeterminate nodule identity
CC in association with NOOT1. {ECO:0000269|PubMed:30026291}.
CC -!- INDUCTION: Induced in roots during early nodule formation.
CC {ECO:0000269|PubMed:30026291}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:30026291). The double mutants noot1 and noot2
CC exhibit complete loss of nodule identity and develop only non-fixing
CC root-like structures that are no longer able to host symbiotic rhizobia
CC (PubMed:30026291). {ECO:0000269|PubMed:30026291}.
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; KEH41446.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN78974.1; -; Genomic_DNA.
DR RefSeq; XP_013467409.1; XM_013611955.1.
DR AlphaFoldDB; A0A072VIM5; -.
DR SMR; A0A072VIM5; -.
DR EnsemblPlants; KEH41446; KEH41446; MTR_1g051025.
DR GeneID; 25483282; -.
DR Gramene; KEH41446; KEH41446; MTR_1g051025.
DR KEGG; mtr:MTR_1g051025; -.
DR HOGENOM; CLU_028148_0_0_1; -.
DR OrthoDB; 651575at2759; -.
DR Proteomes; UP000002051; Chromosome 1.
DR Proteomes; UP000265566; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR044284; NPR5/6.
DR InterPro; IPR024228; NPR_central_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46668; PTHR46668; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF11900; DUF3420; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Nodulation; Reference proteome; Repeat.
FT CHAIN 1..492
FT /note="BTB/POZ domain and ankyrin repeat-containing protein
FT NOOT2"
FT /id="PRO_0000445728"
FT DOMAIN 25..107
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 248..277
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 278..307
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 312..341
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REGION 395..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54118 MW; 57742FE67F6530EE CRC64;
MSLEETLRSL SLDYLNLLIN GQAFSDVTFQ VEGRLVHAHR CILAARSLFF RKFFCGPDPP
SGLDPIGGGS SRQPTVRPGV IPVNSVGYEV FLLLLQFLYS GQVSIVPQKH EPRPNCGERG
CWHTHCTSAV DLALDTLAAA RYFGVEQLAL LTQKQLVSMV EKASIDDVMK VLIASRKQEM
PQLWTTCSHL VAKSGLPPEI LAKHLSIDVV AKIEELRLKS SLARRSLMPL HHHHHHHHHH
DFGDLEDQKI RRMRRALDSS DVELVKLMVM GEGLNLDEAL ALHYAVENCS REVVKALLEL
GAADVNYPAG PAGKTSLHVA AEMVSPEMVA VLLDHHADPT VRTVDGVTPL DILRTLTSDF
LFKGAVPGLN HIEPNKLRLC LELVQSAALV LSREENNASN NNNNNNNASS SAAPVYPPMS
EDHSSSSSGN NNNNNNSIGN LNLDSRLVYL NLGATQMGGD DDNRHNNSHR EAMNRQGGHG
CDPSMYHHSH DF