NLTP1_TOBAC
ID NLTP1_TOBAC Reviewed; 114 AA.
AC Q42952;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Non-specific lipid-transfer protein 1;
DE Short=LTP 1;
DE AltName: Full=Pathogenesis-related protein 14;
DE Short=PR-14;
DE Flags: Precursor;
GN Name=LTP1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Samsun;
RX PubMed=1302637; DOI=10.1111/j.1365-313x.1992.00855.x;
RA Fleming A.J., Mandel T., Hofmann S., Sterk P., de Vries S.C.,
RA Kuhlemeier C.;
RT "Expression pattern of a tobacco lipid transfer protein gene within the
RT shoot apex.";
RL Plant J. 2:855-862(1992).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=8883375; DOI=10.1104/pp.112.2.513;
RA Canevascini S., Caderas D., Mandel T., Fleming A.J., Dupuis I.,
RA Kuhlemeier C.;
RT "Tissue-specific expression and promoter analysis of the tobacco Ltp1
RT gene.";
RL Plant Physiol. 112:513-524(1996).
RN [3]
RP FUNCTION.
RX PubMed=15356262; DOI=10.1091/mbc.e04-07-0575;
RA Buhot N., Gomes E., Milat M.L., Ponchet M., Marion D., Lequeu J.,
RA Delrot S., Coutos-Thevenot P., Blein J.P.;
RT "Modulation of the biological activity of a tobacco LTP1 by lipid
RT complexation.";
RL Mol. Biol. Cell 15:5047-5052(2004).
RN [4]
RP STRUCTURE BY NMR OF 24-114, AND DISULFIDE BONDS.
RX PubMed=15726627; DOI=10.1002/prot.20405;
RA Da Silva P., Landon C., Industri B., Marais A., Marion D., Ponchet M.,
RA Vovelle F.;
RT "Solution structure of a tobacco lipid transfer protein exhibiting new
RT biophysical and biological features.";
RL Proteins 59:356-367(2005).
CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC phospholipids as well as galactolipids across membranes. Binds cis-
CC unsaturated fatty acids and jasmonic acid with a higher affinity than
CC linear chain fatty acids. Formation of the complex with jasmonic acid
CC results in a conformational change facilitating the LPT1 binding on the
CC elicitin plasma membrane receptor that is known to be involved in plant
CC defense induction. May also play a role in wax or cutin deposition in
CC the cell walls of expanding epidermal cells and certain secretory
CC tissues. {ECO:0000269|PubMed:15356262}.
CC -!- TISSUE SPECIFICITY: High expression in leaf epidermis and shoot apex,
CC and also in root epidermis during seedling germination.
CC {ECO:0000269|PubMed:8883375}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; X62395; CAA44267.1; -; Genomic_DNA.
DR PIR; S22168; S22168.
DR RefSeq; XP_016492874.1; XM_016637388.1.
DR PDB; 1T12; NMR; -; A=24-114.
DR PDBsum; 1T12; -.
DR AlphaFoldDB; Q42952; -.
DR SMR; Q42952; -.
DR GeneID; 107812329; -.
DR KEGG; nta:107812329; -.
DR OMA; ERQSACS; -.
DR OrthoDB; 1546493at2759; -.
DR EvolutionaryTrace; Q42952; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
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; Disulfide bond; Lipid-binding; Pathogenesis-related protein;
KW Plant defense; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..114
FT /note="Non-specific lipid-transfer protein 1"
FT /id="PRO_0000018411"
FT DISULFID 27..73
FT /evidence="ECO:0000269|PubMed:15726627,
FT ECO:0007744|PDB:1T12"
FT DISULFID 37..50
FT /evidence="ECO:0000269|PubMed:15726627,
FT ECO:0007744|PDB:1T12"
FT DISULFID 51..96
FT /evidence="ECO:0000269|PubMed:15726627,
FT ECO:0007744|PDB:1T12"
FT DISULFID 71..110
FT /evidence="ECO:0000269|PubMed:15726627,
FT ECO:0007744|PDB:1T12"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1T12"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:1T12"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:1T12"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:1T12"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:1T12"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1T12"
SQ SEQUENCE 114 AA; 11524 MW; 25E2A85212DADDC6 CRC64;
MEIAGKIACF VVLCMVVAAP CAEAITCGQV TSNLAPCLAY LRNTGPLGRC CGGVKALVNS
ARTTEDRQIA CTCLKSAAGA ISGINLGKAA GLPSTCGVNI PYKISPSTDC SKVQ
