NOD13_MEDTR
ID NOD13_MEDTR Reviewed; 163 AA.
AC P93330;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nodulin-13;
DE Short=MtN13;
DE AltName: Full=Pathogenesis-related PR10-like protein;
GN Name=N13;
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 [MRNA], AND INDUCTION.
RC STRAIN=cv. Jemalong J5;
RX PubMed=8634476; DOI=10.1094/mpmi-9-0233;
RA Gamas P., de Carvalho Niebel F., Lescure N., Cullimore J.;
RT "Use of a subtractive hybridization approach to identify new Medicago
RT truncatula genes induced during root nodule development.";
RL Mol. Plant Microbe Interact. 9:233-242(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Jemalong J5;
RX PubMed=9574507; DOI=10.1094/mpmi.1998.11.5.393;
RA Gamas P., de Billy F., Truchet G.;
RT "Symbiosis-specific expression of two Medicago truncatula nodulin genes,
RT MtN1 and MtN13, encoding products homologous to plant defense proteins.";
RL Mol. Plant Microbe Interact. 11:393-403(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:4GY9, ECO:0007744|PDB:4JHG, ECO:0007744|PDB:4JHH, ECO:0007744|PDB:4JHI}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH THE CYTOKININS
RP TRANS-ZEATIN; N(6)-DIMETHYLALLYLADENINE AND KINETIN, AND SUBUNIT.
RC STRAIN=cv. Jemalong J5;
RX PubMed=24311578; DOI=10.1107/s0907444913021975;
RA Ruszkowski M., Szpotkowski K., Sikorski M., Jaskolski M.;
RT "The landscape of cytokinin binding by a plant nodulin.";
RL Acta Crystallogr. D 69:2365-2380(2013).
CC -!- FUNCTION: May be involved in nodule organogenesis rather in the
CC processes related to nitrogen fixation or interactions with the
CC bacteria. May regulate nodulation by controlling the levels of freely
CC available cytokinins.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24311578}.
CC -!- TISSUE SPECIFICITY: Expressed in nodules, but not in leaves, stems,
CC flowers and roots. Specifically located in the nodule cortex.
CC {ECO:0000269|PubMed:9574507}.
CC -!- INDUCTION: Up-regulated during nodulation, but not by Nod factors or
CC pathogen infection. {ECO:0000269|PubMed:8634476}.
CC -!- MISCELLANEOUS: The NT13 molecules that have dimerized without cytokinin
CC ligand most probably lose their binding properties because it seems
CC unlikely that the dimer can dissociate back to the monomer. Asp-62 from
CC the complementary protein molecule forms hydrogen bonds with the
CC cytokinin scaffold. {ECO:0000305|PubMed:24311578}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; BT145081; AFK44875.1; -; mRNA.
DR EMBL; Y10455; CAA71481.1; -; mRNA.
DR RefSeq; XP_013458290.1; XM_013602836.1.
DR PDB; 4GY9; X-ray; 2.04 A; A=1-163.
DR PDB; 4JHG; X-ray; 1.85 A; A=1-163.
DR PDB; 4JHH; X-ray; 2.20 A; A=1-163.
DR PDB; 4JHI; X-ray; 2.60 A; A=1-163.
DR PDBsum; 4GY9; -.
DR PDBsum; 4JHG; -.
DR PDBsum; 4JHH; -.
DR PDBsum; 4JHI; -.
DR AlphaFoldDB; P93330; -.
DR SMR; P93330; -.
DR PRIDE; P93330; -.
DR EnsemblPlants; KEH32321; KEH32321; MTR_4g120950.
DR GeneID; 25494100; -.
DR Gramene; KEH32321; KEH32321; MTR_4g120950.
DR HOGENOM; CLU_081988_2_0_1; -.
DR OrthoDB; 1381244at2759; -.
DR ExpressionAtlas; P93330; differential.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokinin signaling pathway; Nodulation;
KW Pathogenesis-related protein; Plant defense.
FT CHAIN 1..163
FT /note="Nodulin-13"
FT /id="PRO_0000429363"
FT BINDING 68
FT /ligand="kinetin"
FT /ligand_id="ChEBI:CHEBI:27407"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4JHH"
FT BINDING 68
FT /ligand="N(6)-dimethylallyladenine"
FT /ligand_id="ChEBI:CHEBI:17660"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4GY9"
FT BINDING 68
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4JHG"
FT BINDING 82
FT /ligand="kinetin"
FT /ligand_id="ChEBI:CHEBI:27407"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4JHH"
FT BINDING 82
FT /ligand="N(6)-dimethylallyladenine"
FT /ligand_id="ChEBI:CHEBI:17660"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4GY9"
FT BINDING 82
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4JHG"
FT BINDING 133
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:24311578,
FT ECO:0007744|PDB:4JHG"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:4JHG"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4JHG"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:4JHG"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:4JHG"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:4JHG"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4JHG"
FT HELIX 131..154
FT /evidence="ECO:0007829|PDB:4JHG"
SQ SEQUENCE 163 AA; 18180 MW; 62AE7F26A52405FC CRC64;
MGVITSESEY VSSLSAEKLY RGIVEDGNII YPKALPRFIE KAETLEGDGG PGTIKKLTFV
GDFGSTKQHI DMVDRENCAY TYSVYEGIAL SDQPLEKIVF EFKLVPTPEE GCIVKSTTKY
YTKGDDIELS KDYLEAGIER FEGFTKAVES FLLANPDYNK DSN
