ID   NLT41_HORVU             Reviewed;         115 AA.
AC   Q43767;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Non-specific lipid-transfer protein 4.1;
DE            Short=LTP 4.1;
DE   AltName: Full=CW-21;
DE            Short=CW21;
DE   Flags: Precursor;
GN   Name=LTP4.1; Synonyms=LTP4;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bomi; TISSUE=Etiolated leaf;
RX   PubMed=8281190; DOI=10.1046/j.1365-313x.1993.04060983.x;
RA   Molina A., Garcia-Olmedo F.;
RT   "Developmental and pathogen-induced expression of three barley genes
RT   encoding lipid transfer proteins.";
RL   Plant J. 4:983-991(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-115.
RC   STRAIN=cv. Bomi; TISSUE=Leaf;
RX   PubMed=8420795; DOI=10.1016/0014-5793(93)81198-9;
RA   Molina A., Segura A., Garcia-Olmedo F.;
RT   "Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent
RT   inhibitors of bacterial and fungal plant pathogens.";
RL   FEBS Lett. 316:119-122(1993).
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; X68654; CAA48621.1; -; mRNA.
DR   PIR; S45371; S45371.
DR   AlphaFoldDB; Q43767; -.
DR   SMR; Q43767; -.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0188650.1; HORVU.MOREX.r2.3HG0188650.1.CDS.1; HORVU.MOREX.r2.3HG0188650.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0188660.1.mrna1; HORVU.MOREX.r2.3HG0188660.1.mrna1.cds1; HORVU.MOREX.r2.3HG0188660.1.
DR   Gramene; HORVU.MOREX.r2.3HG0188650.1; HORVU.MOREX.r2.3HG0188650.1.CDS.1; HORVU.MOREX.r2.3HG0188650.
DR   Gramene; HORVU.MOREX.r2.3HG0188660.1.mrna1; HORVU.MOREX.r2.3HG0188660.1.mrna1.cds1; HORVU.MOREX.r2.3HG0188660.1.
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..25
FT                   /evidence="ECO:0000269|PubMed:8420795"
FT   CHAIN           26..115
FT                   /note="Non-specific lipid-transfer protein 4.1"
FT                   /id="PRO_0000018383"
FT   DISULFID        29..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..111
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  11085 MW;  0CD95C6E0E591CEB CRC64;
     MARAAASQLV LVALVAAMLL VAADAAISCG QVSSALSPCI SYARGNGAKP PAACCSGVKR
     LAGAAQSTAD KQAACKCIKS AAGGLNAGKA AGIPSMCGVS VPYAISASVD CSKIR