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Protein

Non-specific lipid-transfer protein 1

Gene
N/A
Organism
Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Has antifungal activity against F.solani, F.oxysporum, P.aphanidermatum and S.rolfsii. Has antibacterial activity against the Gram-positive bacterium S.aureus but not against the Gram-negative bacterium S.typhimurium.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei44Lipid headgroupCurated1
Binding sitei79Lipid headgroupCurated1

GO - Molecular functioni

  • lipid binding Source: UniProtKB
  • transporter activity Source: UniProtKB

GO - Biological processi

  • defense response to fungus Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB-KW
  • lipid transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein 1
Short name:
LTP 1
Short name:
NS-LTP1
OrganismiVigna radiata var. radiata (Mung bean) (Phaseolus aureus)Curated
Taxonomic identifieri3916 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001538751 – 91Non-specific lipid-transfer protein 1Add BLAST91

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 50Combined sources1 Publication
Disulfide bondi13 ↔ 27
Disulfide bondi28 ↔ 73
Disulfide bondi48 ↔ 87

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP83434.

Interactioni

Subunit structurei

Monomer.Curated1 Publication

Structurei

Secondary structure

191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Helixi7 – 17Combined sources11
Helixi25 – 35Combined sources11
Turni36 – 38Combined sources3
Helixi42 – 54Combined sources13
Helixi63 – 73Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SIYNMR-A1-91[»]
ProteinModelPortaliP83434.
SMRiP83434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83434.

Family & Domainsi

Sequence similaritiesi

Belongs to the plant LTP family.By similarity

Family and domain databases

InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000528. Plant_LTP.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00382. LIPIDTRNSFER.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
PROSITEiPS00597. PLANT_LTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTCGQVQGNL AQCIGFLQKG GVVPPSCCTG VKNILNSSRT TADRRAVCSC
60 70 80 90
LKAAAGAVRG INPNNAEALP GKCGVNIPYK ISTSTNCNSI N
Length:91
Mass (Da):9,299
Last modified:October 1, 2002 - v1
Checksum:i0A966C1FDBB76E09
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18Q → E AA sequence (PubMed:15350690).Curated1

Mass spectrometryi

Molecular mass is 9030 Da from positions 1 - 91. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SIYNMR-A1-91[»]
ProteinModelPortaliP83434.
SMRiP83434.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP83434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP83434.

Family and domain databases

InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000528. Plant_LTP.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00382. LIPIDTRNSFER.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
PROSITEiPS00597. PLANT_LTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNLTP1_VIGRR
AccessioniPrimary (citable) accession number: P83434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.