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Protein

Nodulin-13

Gene

N13

Organism
Medicago truncatula (Barrel medic) (Medicago tribuloides)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in nodule organogenesis rather in the processes related to nitrogen fixation or interactions with the bacteria. May regulate nodulation by controlling the levels of freely available cytokinins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei68 – 681CytokininCombined sources1 Publication
Binding sitei82 – 821CytokininCombined sources1 Publication
Binding sitei133 – 1331CytokininCombined sources1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Pathogenesis-related protein

Keywords - Biological processi

Cytokinin signaling pathway, Nodulation, Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Nodulin-13
Short name:
MtN13
Alternative name(s):
Pathogenesis-related PR10-like protein
Gene namesi
Name:N13
OrganismiMedicago truncatula (Barrel medic) (Medicago tribuloides)
Taxonomic identifieri3880 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Nodulin-13PRO_0000429363Add
BLAST

Expressioni

Tissue specificityi

Expressed in nodules, but not in leaves, stems, flowers and roots. Specifically located in the nodule cortex.1 Publication

Inductioni

Up-regulated during nodulation, but not by Nod factors or pathogen infection.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412Combined sources
Helixi16 – 249Combined sources
Helixi27 – 348Combined sources
Turni36 – 383Combined sources
Beta strandi39 – 5012Combined sources
Beta strandi54 – 6310Combined sources
Beta strandi65 – 7410Combined sources
Turni75 – 784Combined sources
Beta strandi79 – 846Combined sources
Beta strandi95 – 10612Combined sources
Beta strandi112 – 12211Combined sources
Beta strandi124 – 1263Combined sources
Helixi131 – 15424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GY9X-ray2.04A1-163[»]
4JHGX-ray1.85A1-163[»]
4JHHX-ray2.20A1-163[»]
4JHIX-ray2.60A1-163[»]
ProteinModelPortaliP93330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the BetVI family.Curated

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR000916. Bet_v_I/MLP.
IPR024949. Bet_v_I_allergen.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF00407. Bet_v_1. 1 hit.
[Graphical view]
PRINTSiPR00634. BETALLERGEN.

Sequencei

Sequence statusi: Complete.

P93330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVITSESEY VSSLSAEKLY RGIVEDGNII YPKALPRFIE KAETLEGDGG
60 70 80 90 100
PGTIKKLTFV GDFGSTKQHI DMVDRENCAY TYSVYEGIAL SDQPLEKIVF
110 120 130 140 150
EFKLVPTPEE GCIVKSTTKY YTKGDDIELS KDYLEAGIER FEGFTKAVES
160
FLLANPDYNK DSN
Length:163
Mass (Da):18,180
Last modified:May 1, 1997 - v1
Checksum:i62AE7F26A52405FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT145081 mRNA. Translation: AFK44875.1.
Y10455 mRNA. Translation: CAA71481.1.
RefSeqiXP_013458290.1. XM_013602836.1.
UniGeneiMtr.5942.

Genome annotation databases

EnsemblPlantsiKEH32321; KEH32321; MTR_4g120950.
GeneIDi25494100.
GrameneiKEH32321; KEH32321; MTR_4g120950.
KEGGimtr:MTR_4g120950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT145081 mRNA. Translation: AFK44875.1.
Y10455 mRNA. Translation: CAA71481.1.
RefSeqiXP_013458290.1. XM_013602836.1.
UniGeneiMtr.5942.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GY9X-ray2.04A1-163[»]
4JHGX-ray1.85A1-163[»]
4JHHX-ray2.20A1-163[»]
4JHIX-ray2.60A1-163[»]
ProteinModelPortaliP93330.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiKEH32321; KEH32321; MTR_4g120950.
GeneIDi25494100.
GrameneiKEH32321; KEH32321; MTR_4g120950.
KEGGimtr:MTR_4g120950.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR000916. Bet_v_I/MLP.
IPR024949. Bet_v_I_allergen.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF00407. Bet_v_1. 1 hit.
[Graphical view]
PRINTSiPR00634. BETALLERGEN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Use of a subtractive hybridization approach to identify new Medicago truncatula genes induced during root nodule development."
    Gamas P., de Carvalho Niebel F., Lescure N., Cullimore J.
    Mol. Plant Microbe Interact. 9:233-242(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Jemalong J5.
  2. "Symbiosis-specific expression of two Medicago truncatula nodulin genes, MtN1 and MtN13, encoding products homologous to plant defense proteins."
    Gamas P., de Billy F., Truchet G.
    Mol. Plant Microbe Interact. 11:393-403(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Jemalong J5.
  3. Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.
    Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYTOKININS, SUBUNIT.
    Strain: cv. Jemalong J5.

Entry informationi

Entry nameiNOD13_MEDTR
AccessioniPrimary (citable) accession number: P93330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The NT13 molecules that have dimerized without cytokinin ligand most probably lose their binding properties because it seems unlikely that the dimer can dissociate back to the monomer. Asp-62 from the complementary protein molecule forms hydrogen bonds with the cytokinin scaffold.1 Publication

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.