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Protein

Non-specific lipid-transfer protein

Gene
N/A
Organism
Triticum aestivum (Wheat)
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. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein
Short name:
LTP
Alternative name(s):
Phospholipid transfer protein
Short name:
PLTP
ns-LTP1
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Protein family/group databases

Allergomei1059. Tri a 14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 24›241 PublicationAdd
BLAST
Chaini25 – 11389Non-specific lipid-transfer proteinPRO_0000018414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 73Combined sources1 Publication
Lipidationi30 – 301Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester1 Publication
Disulfide bondi36 ↔ 50Combined sources1 Publication
Disulfide bondi51 ↔ 96Combined sources1 Publication
Disulfide bondi71 ↔ 110Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Lipoprotein

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 338Combined sources
Helixi34 – 363Combined sources
Helixi37 – 404Combined sources
Helixi48 – 6013Combined sources
Helixi64 – 7815Combined sources
Helixi86 – 905Combined sources
Helixi92 – 965Combined sources
Beta strandi105 – 1084Combined sources
Helixi110 – 1123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWOX-ray2.10A/B24-113[»]
1CZ2NMR-A24-113[»]
1GH1NMR-A24-113[»]
ProteinModelPortaliP24296.
SMRiP24296. Positions 24-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24296.

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: Fragment.

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

P24296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AQVMLMAVAL VLMLAAVPRA AVAIDCGHVD SLVRPCLSYV QGGPGPSGQC
60 70 80 90 100
CDGVKNLHNQ ARSQSDRQSA CNCLKGIARG IHNLNEDNAR SIPPKCGVNL
110
PYTISLNIDC SRV
Length:113
Mass (Da):11,899
Last modified:October 1, 1993 - v2
Checksum:i4D48FB628D98EE5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63669 mRNA. Translation: CAA45210.1.
PIRiS21757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63669 mRNA. Translation: CAA45210.1.
PIRiS21757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWOX-ray2.10A/B24-113[»]
1CZ2NMR-A24-113[»]
1GH1NMR-A24-113[»]
ProteinModelPortaliP24296.
SMRiP24296. Positions 24-113.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1059. Tri a 14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP24296.

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. "Nucleotide sequence of a cDNA encoding a lipid transfer protein from wheat (Triticum durum Desf.)."
    Dieryck W., Gautier M.-F., Lullien V., Joudrier P.
    Plant Mol. Biol. 19:707-709(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Amino acid sequence of a non-specific wheat phospholipid transfer protein and its conformation as revealed by infrared and Raman spectroscopy. Role of disulfide bridges and phospholipids in the stabilization of the alpha-helix structure."
    Desormeaux A., Blochet J.-E., Pezolet M., Marion D.
    Biochim. Biophys. Acta 1121:137-152(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-113.
    Tissue: Seed.
  3. "Identification of a new form of lipid transfer protein (LTP1) in wheat seeds."
    Douliez J.-P., Jegou S., Pato C., Larre C., Molle D., Marion D.
    J. Agric. Food Chem. 49:1805-1808(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION AT ASP-30, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Seed.
  4. "Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure."
    Simorre J.-P., Caille A., Marion D., Marion D., Ptak M.
    Biochemistry 30:11600-11608(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
    Tissue: Seed.
  5. "Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects."
    Bonmatin J.-M., Genest M., Petit M.-C., Gincel E., Simorre J.-P., Cornet B., Gallet X., Caille A., Labbe H., Vovelle F., Ptak M.
    Biochimie 74:825-836(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers."
    Gincel E., Simorre J.-P., Caille A., Marion D., Ptak M., Vovelle F.
    Eur. J. Biochem. 226:413-422(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1-A resolution."
    Charvolin D., Douliez J.-P., Marion D., Cohen-Addad C., Pebay-Peyroula E.
    Eur. J. Biochem. 264:562-568(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiNLTP1_WHEAT
AccessioniPrimary (citable) accession number: P24296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.