NLTP1_WHEAT
ID NLTP1_WHEAT Reviewed; 113 AA.
AC P24296;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Non-specific lipid-transfer protein;
DE Short=LTP;
DE AltName: Full=Phospholipid transfer protein;
DE Short=PLTP;
DE AltName: Full=ns-LTP1;
DE Flags: Precursor; Fragment;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1627784; DOI=10.1007/bf00026798;
RA Dieryck W., Gautier M.-F., Lullien V., Joudrier P.;
RT "Nucleotide sequence of a cDNA encoding a lipid transfer protein from wheat
RT (Triticum durum Desf.).";
RL Plant Mol. Biol. 19:707-709(1992).
RN [2]
RP PROTEIN SEQUENCE OF 25-113.
RC TISSUE=Seed;
RX PubMed=1599935; DOI=10.1016/0167-4838(92)90347-g;
RA Desormeaux A., Blochet J.-E., Pezolet M., Marion D.;
RT "Amino acid sequence of a non-specific wheat phospholipid transfer protein
RT and its conformation as revealed by infrared and Raman spectroscopy. Role
RT of disulfide bridges and phospholipids in the stabilization of the alpha-
RT helix structure.";
RL Biochim. Biophys. Acta 1121:137-152(1992).
RN [3]
RP LIPIDATION AT ASP-30, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed;
RX PubMed=11308329; DOI=10.1021/jf001327m;
RA Douliez J.-P., Jegou S., Pato C., Larre C., Molle D., Marion D.;
RT "Identification of a new form of lipid transfer protein (LTP1) in wheat
RT seeds.";
RL J. Agric. Food Chem. 49:1805-1808(2001).
RN [4]
RP STRUCTURE BY NMR.
RC TISSUE=Seed;
RX PubMed=1660724; DOI=10.1021/bi00113a016;
RA Simorre J.-P., Caille A., Marion D., Marion D., Ptak M.;
RT "Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer
RT protein: sequential resonance assignments and secondary structure.";
RL Biochemistry 30:11600-11608(1991).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=1467342; DOI=10.1016/0300-9084(92)90065-m;
RA Bonmatin J.-M., Genest M., Petit M.-C., Gincel E., Simorre J.-P.,
RA Cornet B., Gallet X., Caille A., Labbe H., Vovelle F., Ptak M.;
RT "Progress in multidimensional NMR investigations of peptide and protein 3-D
RT structures in solution. From structure to functional aspects.";
RL Biochimie 74:825-836(1992).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8001559; DOI=10.1111/j.1432-1033.1994.tb20066.x;
RA Gincel E., Simorre J.-P., Caille A., Marion D., Ptak M., Vovelle F.;
RT "Three-dimensional structure in solution of a wheat lipid-transfer protein
RT from multidimensional 1H-NMR data. A new folding for lipid carriers.";
RL Eur. J. Biochem. 226:413-422(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=10491104; DOI=10.1046/j.1432-1327.1999.00667.x;
RA Charvolin D., Douliez J.-P., Marion D., Cohen-Addad C., Pebay-Peyroula E.;
RT "The crystal structure of a wheat nonspecific lipid transfer protein (ns-
RT LTP1) complexed with two molecules of phospholipid at 2.1-A resolution.";
RL Eur. J. Biochem. 264:562-568(1999).
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. May play a
CC role in wax or cutin deposition in the cell walls of expanding
CC epidermal cells and certain secretory tissues.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; X63669; CAA45210.1; -; mRNA.
DR PIR; S21757; S21757.
DR PDB; 1BWO; X-ray; 2.10 A; A/B=24-113.
DR PDB; 1CZ2; NMR; -; A=24-113.
DR PDB; 1GH1; NMR; -; A=24-113.
DR PDBsum; 1BWO; -.
DR PDBsum; 1CZ2; -.
DR PDBsum; 1GH1; -.
DR AlphaFoldDB; P24296; -.
DR BMRB; P24296; -.
DR SMR; P24296; -.
DR STRING; 4565.Traes_5BL_628390692.1; -.
DR Allergome; 1059; Tri a 14.
DR PRIDE; P24296; -.
DR EnsemblPlants; TraesCAD_scaffold_127787_01G000100.1; TraesCAD_scaffold_127787_01G000100.1; TraesCAD_scaffold_127787_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_156805_01G000100.1; TraesCLE_scaffold_156805_01G000100.1; TraesCLE_scaffold_156805_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_199943_01G000100.1; TraesPAR_scaffold_199943_01G000100.1; TraesPAR_scaffold_199943_01G000100.
DR EnsemblPlants; TraesROB_scaffold_157986_01G000100.1; TraesROB_scaffold_157986_01G000100.1; TraesROB_scaffold_157986_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_056410_01G000100.1; TraesWEE_scaffold_056410_01G000100.1; TraesWEE_scaffold_056410_01G000100.
DR Gramene; TraesCAD_scaffold_127787_01G000100.1; TraesCAD_scaffold_127787_01G000100.1; TraesCAD_scaffold_127787_01G000100.
DR Gramene; TraesCLE_scaffold_156805_01G000100.1; TraesCLE_scaffold_156805_01G000100.1; TraesCLE_scaffold_156805_01G000100.
DR Gramene; TraesPAR_scaffold_199943_01G000100.1; TraesPAR_scaffold_199943_01G000100.1; TraesPAR_scaffold_199943_01G000100.
DR Gramene; TraesROB_scaffold_157986_01G000100.1; TraesROB_scaffold_157986_01G000100.1; TraesROB_scaffold_157986_01G000100.
DR Gramene; TraesWEE_scaffold_056410_01G000100.1; TraesWEE_scaffold_056410_01G000100.1; TraesWEE_scaffold_056410_01G000100.
DR eggNOG; ENOG502S4CI; Eukaryota.
DR EvolutionaryTrace; P24296; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P24296; baseline and differential.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076; PTHR33076; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00597; PLANT_LTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Lipoprotein; Reference proteome; Signal; Transport.
FT SIGNAL <1..24
FT /evidence="ECO:0000269|PubMed:1599935"
FT CHAIN 25..113
FT /note="Non-specific lipid-transfer protein"
FT /id="PRO_0000018414"
FT LIPID 30
FT /note="Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid
FT aspartate ester"
FT /evidence="ECO:0000305|PubMed:11308329"
FT DISULFID 26..73
FT /evidence="ECO:0000269|PubMed:10491104,
FT ECO:0007744|PDB:1BWO"
FT DISULFID 36..50
FT /evidence="ECO:0000269|PubMed:10491104,
FT ECO:0007744|PDB:1BWO"
FT DISULFID 51..96
FT /evidence="ECO:0000269|PubMed:10491104,
FT ECO:0007744|PDB:1BWO"
FT DISULFID 71..110
FT /evidence="ECO:0000269|PubMed:10491104,
FT ECO:0007744|PDB:1BWO"
FT NON_TER 1
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1BWO"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:1BWO"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1CZ2"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1BWO"
SQ SEQUENCE 113 AA; 11899 MW; 4D48FB628D98EE5E CRC64;
AQVMLMAVAL VLMLAAVPRA AVAIDCGHVD SLVRPCLSYV QGGPGPSGQC CDGVKNLHNQ
ARSQSDRQSA CNCLKGIARG IHNLNEDNAR SIPPKCGVNL PYTISLNIDC SRV
