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Protein

Non-specific lipid-transfer protein 1

Gene

LTP1

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. Binds cis-unsaturated fatty acids and jasmonic acid with a higher affinity than linear chain fatty acids. Formation of the complex with jasmonic acid results in a conformational change facilitating the LPT1 binding on the elicitin plasma membrane receptor that is known to be involved in plant defense induction. May also play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Pathogenesis-related protein

Keywords - Biological processi

Plant defense, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein 1
Short name:
LTP 1
Alternative name(s):
Pathogenesis-related protein 14
Short name:
PR-14
Gene namesi
Name:LTP1
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 11491Non-specific lipid-transfer protein 1PRO_0000018411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 73Combined sources1 Publication
Disulfide bondi37 ↔ 50Combined sources1 Publication
Disulfide bondi51 ↔ 96Combined sources1 Publication
Disulfide bondi71 ↔ 110Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

High expression in leaf epidermis and shoot apex, and also in root epidermis during seedling germination.1 Publication

Structurei

Secondary structure

1
114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 337Combined sources
Helixi35 – 417Combined sources
Helixi50 – 5910Combined sources
Helixi65 – 8016Combined sources
Helixi86 – 9510Combined sources
Beta strandi104 – 1085Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T12NMR-A24-114[»]
ProteinModelPortaliQ42952.
SMRiQ42952. Positions 24-114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ42952.

Family & Domainsi

Sequence similaritiesi

Belongs to the plant LTP family.Curated

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIAGKIACF VVLCMVVAAP CAEAITCGQV TSNLAPCLAY LRNTGPLGRC
60 70 80 90 100
CGGVKALVNS ARTTEDRQIA CTCLKSAAGA ISGINLGKAA GLPSTCGVNI
110
PYKISPSTDC SKVQ
Length:114
Mass (Da):11,524
Last modified:November 1, 1996 - v1
Checksum:i25E2A85212DADDC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62395 Genomic DNA. Translation: CAA44267.1.
PIRiS22168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62395 Genomic DNA. Translation: CAA44267.1.
PIRiS22168.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T12NMR-A24-114[»]
ProteinModelPortaliQ42952.
SMRiQ42952. Positions 24-114.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ42952.

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...

Publicationsi

  1. "Expression pattern of a tobacco lipid transfer protein gene within the shoot apex."
    Fleming A.J., Mandel T., Hofmann S., Sterk P., de Vries S.C., Kuhlemeier C.
    Plant J. 2:855-862(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Samsun.
  2. "Tissue-specific expression and promoter analysis of the tobacco Ltp1 gene."
    Canevascini S., Caderas D., Mandel T., Fleming A.J., Dupuis I., Kuhlemeier C.
    Plant Physiol. 112:513-524(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  3. "Modulation of the biological activity of a tobacco LTP1 by lipid complexation."
    Buhot N., Gomes E., Milat M.L., Ponchet M., Marion D., Lequeu J., Delrot S., Coutos-Thevenot P., Blein J.P.
    Mol. Biol. Cell 15:5047-5052(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Solution structure of a tobacco lipid transfer protein exhibiting new biophysical and biological features."
    Da Silva P., Landon C., Industri B., Marais A., Marion D., Ponchet M., Vovelle F.
    Proteins 59:356-367(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-114, DISULFIDE BONDS.

Entry informationi

Entry nameiNLTP1_TOBAC
AccessioniPrimary (citable) accession number: Q42952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 66 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

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.