ID   NLTP_SPIOL              Reviewed;         117 AA.
AC   P10976;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Non-specific lipid-transfer protein;
DE            Short=LTP;
DE   AltName: Full=Phospholipid transfer protein;
DE            Short=PLTP;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16667945; DOI=10.1104/pp.95.1.164;
RA   Bernhard W.R., Thoma S., Botella J., Somerville C.R.;
RT   "Isolation of a cDNA clone for spinach lipid transfer protein and evidence
RT   that the protein is synthesized by the secretory pathway.";
RL   Plant Physiol. 95:164-170(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-117.
RC   TISSUE=Leaf;
RX   PubMed=3609015; DOI=10.1111/j.1432-1033.1987.tb13527.x;
RA   Bouillon P., Drischel C., Vergnolle C., Duranton H., Kader J.-C.;
RT   "The primary structure of spinach-leaf phospholipid-transfer protein.";
RL   Eur. J. Biochem. 166:387-391(1987).
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; M58635; AAA34032.1; -; mRNA.
DR   PIR; T09155; T09155.
DR   AlphaFoldDB; P10976; -.
DR   SMR; P10976; -.
DR   OrthoDB; 1546493at2759; -.
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   Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW   Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:3609015"
FT   CHAIN           27..117
FT                   /note="Non-specific lipid-transfer protein"
FT                   /id="PRO_0000018409"
FT   DISULFID        30..76
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..113
FT                   /evidence="ECO:0000250"
FT   CONFLICT        53..54
FT                   /note="CC -> SS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   117 AA;  11426 MW;  19F969F94D58FA34 CRC64;
     MASSAVIKLA CAVLLCIVVA APYAEAGITC GMVSSKLAPC IGYLKGGPLG GGCCGGIKAL
     NAAAATTPDR KTACNCLKSA ANAIKGINYG KAAGLPGMCG VHIPYAISPS TNCNAVH