ID   NLTP_ELECO              Reviewed;          95 AA.
AC   P23802;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Non-specific lipid-transfer protein;
DE            Short=LTP;
DE   AltName: Full=Alpha-amylase inhibitor I-2;
OS   Eleusine coracana (Indian finger millet) (Ragi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Cynodonteae; Eleusininae; Eleusine.
OX   NCBI_TaxID=4511;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RA   Campos F.A.P., Richardson M.;
RT   "The complete amino acid sequence of the alpha-amylase inhibitor I-2 from
RT   seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.).";
RL   FEBS Lett. 167:221-225(1984).
RN   [2]
RP   IDENTIFICATION AS A LTP.
RX   PubMed=2465737; DOI=10.1016/0003-9861(89)90154-9;
RA   Bernhard W.R., Somerville C.R.;
RT   "Coidentity of putative amylase inhibitors from barley and finger millet
RT   with phospholipid transfer proteins inferred from amino acid sequence
RT   homology.";
RL   Arch. Biochem. Biophys. 269:695-697(1989).
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   -!- TISSUE SPECIFICITY: Seeds.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be an inhibitor of alpha-
CC       amylase. {ECO:0000305}.
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DR   PIR; S28988; S28988.
DR   AlphaFoldDB; P23802; -.
DR   SMR; P23802; -.
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; Transport.
FT   CHAIN           1..95
FT                   /note="Non-specific lipid-transfer protein"
FT                   /id="PRO_0000153872"
FT   DISULFID        4..52
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..29
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..90
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   95 AA;  9332 MW;  BD8768CE8FAC4C9D CRC64;
     AISCGQVSSA IGPCLAYARG AGAAPSASCQ SGVRSLNAAA RTTADRRAAC NCSLKSAASR
     VSGLNAGKAS SIPGRCGVRL PYAISASIDC SRVNN