ID   NLTP1_NIGSA             Reviewed;          35 AA.
AC   P86527;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Non-specific lipid-transfer protein 1 {ECO:0000250|UniProtKB:P81402, ECO:0000303|PubMed:19621049};
DE            Short=LTP 1 {ECO:0000250|UniProtKB:P81402, ECO:0000303|PubMed:19621049};
DE   Flags: Fragment;
OS   Nigella sativa (Black cumin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC   Nigelleae; Nigella.
OX   NCBI_TaxID=555479;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RA   Barashkova A., Smirnov A., Rogozhin E.A., Zavries S.;
RT   "Diversity of cationic antimicrobial peptides from blackseed (Nigella
RT   sativa).";
RL   Submitted (MAR-2022) to UniProtKB.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-25, FUNCTION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:19621049};
RX   PubMed=19621049; DOI=10.1134/s1068162009030054;
RA   Oshchepkova I.U.I., Veshkurova O.N., Rogozhin E.A., Musoliamov A.K.H.,
RA   Smirnov A.N., Odintsova T.I., Egorov T.S.A., Grishin E.V., Salikhov S.H.I.;
RT   "Isolation of the lipid-transporting protein Ns-LTP1 from seeds of the
RT   garden fennel flower (Nigella sativa).";
RL   Bioorg. Khim. 35:344-349(2009).
CC   -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC       phospholipids as well as galactolipids across membranes (By
CC       similarity). May play a role in wax or cutin deposition in the cell
CC       walls of expanding epidermal cells and certain secretory tissues (By
CC       similarity). Inhibits the growth of F.oxysporum and P.infestans
CC       (PubMed:19621049, Ref.1). {ECO:0000250|UniProtKB:P81402,
CC       ECO:0000269|PubMed:19621049, ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Seeds. {ECO:0000269|PubMed:19621049,
CC       ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=9602; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19621049};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR   AlphaFoldDB; P86527; -.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Lipid-binding; Plant defense; Transport.
FT   CHAIN           1..>35
FT                   /note="Non-specific lipid-transfer protein 1"
FT                   /id="PRO_0000394465"
FT   DISULFID        3..?
FT                   /evidence="ECO:0000250|UniProtKB:P81402"
FT   DISULFID        13..28
FT                   /evidence="ECO:0000250|UniProtKB:P81402"
FT   DISULFID        29..?
FT                   /evidence="ECO:0000250|UniProtKB:P81402"
FT   NON_TER         35
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   35 AA;  3652 MW;  80378134BAE4CE40 CRC64;
     ISCQDVKQSL APCLPYVTGR APKPAPGCCN GINHL