NSP2_MEDTR
ID NSP2_MEDTR Reviewed; 508 AA.
AC Q5NE24; G7J334;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein NODULATION SIGNALING PATHWAY 2 {ECO:0000303|PubMed:15961668};
GN Name=NSP2 {ECO:0000303|PubMed:15961668};
GN OrderedLocusNames=MTR_3g072710 {ECO:0000312|EMBL:AES71327.1};
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], FUNCTION, MUTAGENESIS OF
RP 160-ARG--PRO-304, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15961668; DOI=10.1126/science.1110951;
RA Kalo P., Gleason C., Edwards A., Marsh J., Mitra R.M., Hirsch S., Jakab J.,
RA Sims S., Long S.R., Rogers J., Kiss G.B., Downie J.A., Oldroyd G.E.D.;
RT "Nodulation signaling in legumes requires NSP2, a member of the GRAS family
RT of transcriptional regulators.";
RL Science 308:1786-1789(2005).
RN [2]
RP IDENTIFICATION, AND MUTAGENESIS OF GLU-232.
RC STRAIN=cv. Jemalong A17;
RX PubMed=11006338; DOI=10.2307/3871180;
RA Catoira R., Galera C., de Billy F., Penmetsa R.V., Journet E.-P.,
RA Maillet F., Rosenberg C., Cook D., Gough C., Denarie J.;
RT "Four genes of Medicago truncatula controlling components of a nod factor
RT transduction pathway.";
RL Plant Cell 12:1647-1666(2000).
RN [3]
RP IDENTIFICATION.
RX PubMed=12644655; DOI=10.1104/pp.102.010710;
RA Oldroyd G.E.D., Long S.R.;
RT "Identification and characterization of nodulation-signaling pathway 2, a
RT gene of Medicago truncatula involved in Nod actor signaling.";
RL Plant Physiol. 131:1027-1032(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22039214; DOI=10.1105/tpc.111.089771;
RA Liu W., Kohlen W., Lillo A., Op den Camp R., Ivanov S., Hartog M.,
RA Limpens E., Jamil M., Smaczniak C., Kaufmann K., Yang W.C., Hooiveld G.J.,
RA Charnikhova T., Bouwmeester H.J., Bisseling T., Geurts R.;
RT "Strigolactone biosynthesis in Medicago truncatula and rice requires the
RT symbiotic GRAS-type transcription factors NSP1 and NSP2.";
RL Plant Cell 23:3853-3865(2011).
RN [7]
RP FUNCTION.
RX PubMed=26503135; DOI=10.1186/s12870-015-0651-x;
RA van Zeijl A., Liu W., Xiao T.T., Kohlen W., Yang W.C., Bisseling T.,
RA Geurts R.;
RT "The strigolactone biosynthesis gene DWARF27 is co-opted in rhizobium
RT symbiosis.";
RL BMC Plant Biol. 15:260-260(2015).
RN [8]
RP INTERACTION WITH RAM1.
RX PubMed=26511916; DOI=10.1104/pp.15.01155;
RA Park H.-J., Floss D.S., Levesque-Tremblay V., Bravo A., Harrison M.J.;
RT "Hyphal branching during arbuscule development requires reduced arbuscular
RT mycorrhiza1.";
RL Plant Physiol. 169:2774-2788(2015).
CC -!- FUNCTION: Transcriptional regulator essential for Nod-factor-induced
CC gene expression (PubMed:15961668). Acts downstream of calcium spiking
CC and DMI3, a calcium/calmodulin-dependent protein kinase (CCaMK)
CC (PubMed:15961668). Transcription factor involved in the control of
CC strigolactone biosynthesis in roots through the activation of the beta-
CC carotene isomerase D27, which participates in a pathway leading to
CC biosynthesis of strigolactones (PubMed:22039214, PubMed:26503135).
CC {ECO:0000269|PubMed:15961668, ECO:0000269|PubMed:22039214,
CC ECO:0000269|PubMed:26503135}.
CC -!- SUBUNIT: Interacts with RAM1 (PubMed:26511916). Interacts with IPN2 and
CC RAD1 (By similarity). {ECO:0000250|UniProtKB:Q2PEG7,
CC ECO:0000269|PubMed:26511916}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15961668}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:15961668}. Note=Mainly
CC localized to the nuclear envelope. Also found in the endoplasmic
CC reticulum. Upon Nod-factor application, the nuclear envelope
CC localization disappears and the protein accumulates in the nucleus.
CC {ECO:0000269|PubMed:15961668}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots and leaves.
CC {ECO:0000269|PubMed:15961668}.
CC -!- INDUCTION: Induced 24 hours after treatment with Nod factor or
CC Sinorhizobium meliloti. {ECO:0000269|PubMed:15961668}.
CC -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000305}.
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DR EMBL; AJ832138; CAH55768.1; -; Genomic_DNA.
DR EMBL; CM001219; AES71327.1; -; Genomic_DNA.
DR RefSeq; XP_003601076.1; XM_003601028.2.
DR AlphaFoldDB; Q5NE24; -.
DR SMR; Q5NE24; -.
DR STRING; 3880.AES71327; -.
DR EnsemblPlants; AES71327; AES71327; MTR_3g072710.
DR GeneID; 11406790; -.
DR Gramene; AES71327; AES71327; MTR_3g072710.
DR KEGG; mtr:MTR_3g072710; -.
DR eggNOG; ENOG502R0MM; Eukaryota.
DR HOGENOM; CLU_011924_0_2_1; -.
DR OMA; AYEETNG; -.
DR OrthoDB; 542322at2759; -.
DR Proteomes; UP000002051; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR InterPro; IPR030028; SCL26/NSP2.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR PANTHER; PTHR31636:SF25; PTHR31636:SF25; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nodulation; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..508
FT /note="Protein NODULATION SIGNALING PATHWAY 2"
FT /id="PRO_0000132233"
FT DOMAIN 108..500
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 75..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..190
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 209..273
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 289..321
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 331..422
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 425..500
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 240..244
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MUTAGEN 160..304
FT /note="Missing: In nsp2-1 and nsp2-2; loss of nodulation."
FT /evidence="ECO:0000269|PubMed:15961668"
FT MUTAGEN 232
FT /note="E->K: In nsp2-3; decreased size and number of
FT nodules."
FT /evidence="ECO:0000269|PubMed:11006338"
SQ SEQUENCE 508 AA; 56337 MW; FB8B88512FD20AF3 CRC64;
MDLMDMDAIN DLHFSGHSSL TNTPTSDEDY GCTWNHWSPI VNWDTFTGAP DDFHHLMDTI
IEDRTTVLEQ LSPSITTTTT TTTTTDEEEE EMETTTTTTT TAIKTHEVGD DSKGLKLVHL
LMAGAEALTG STKNRDLARV ILIRLKELVS QHANGSNMER LAAHFTEALH GLLEGAGGAH
NNHHHHNNNK HYLTTNGPHD NQNDTLAAFQ LLQDMSPYVK FGHFTANQAI IEAVAHERRV
HVIDYDIMEG VQWASLIQSL ASNNNGPHLR ITALSRTGTG RRSIATVQET GRRLTSFAAS
LGQPFSFHHC RLDSDETFRP SALKLVRGEA LVFNCMLNLP HLSYRAPESV ASFLNGAKTL
NPKLVTLVEE EVGSVIGGFV ERFMDSLHHY SAVFDSLEAG FPMQNRARTL VERVFFGPRI
AGSLGRIYRT GGEEERRSWG EWLGEVGFRG VPVSFANHCQ AKLLLGLFND GYRVEEVGVG
SNKLVLDWKS RRLLSASLWT CSSSDSDL
