ID   NLT42_HORVU             Reviewed;         115 AA.
AC   Q43875;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Non-specific lipid-transfer protein 4.2;
DE            Short=LTP 4.2;
DE   AltName: Full=Low-temperature-responsive protein 4.9;
DE   Flags: Precursor;
GN   Name=LTP4.2; Synonyms=BLT4.9;
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 [GENOMIC DNA].
RC   STRAIN=cv. Igri;
RA   White A.J., Dunn M.A., Brown K., Hughes M.A.;
RT   "Comparative analysis of genomic sequence and expression of a lipid
RT   transfer protein gene family in winter barley.";
RL   J. Exp. Bot. 45:1885-1892(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. NK 1558; TISSUE=Leaf;
RX   PubMed=8804389; DOI=10.1007/bf02173216;
RA   Molina A., Diaz I., Vasil I.K., Carbonero P., Garcia-Olmedo F.;
RT   "Two cold-inducible genes encoding lipid transfer protein LTP4 from barley
RT   show differential responses to bacterial pathogens.";
RL   Mol. Gen. Genet. 252:162-168(1996).
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   -!- INDUCTION: By cold.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; U63993; AAB05812.1; -; Genomic_DNA.
DR   EMBL; Z66529; CAA91436.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q43875; -.
DR   SMR; Q43875; -.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0188690.1; HORVU.MOREX.r2.3HG0188690.1; HORVU.MOREX.r2.3HG0188690.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0188690.1.mrna1; HORVU.MOREX.r2.3HG0188690.1.mrna1; HORVU.MOREX.r2.3HG0188690.1.
DR   Gramene; HORVU.MOREX.r2.3HG0188690.1; HORVU.MOREX.r2.3HG0188690.1; HORVU.MOREX.r2.3HG0188690.
DR   Gramene; HORVU.MOREX.r2.3HG0188690.1.mrna1; HORVU.MOREX.r2.3HG0188690.1.mrna1; HORVU.MOREX.r2.3HG0188690.1.
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   2: Evidence at transcript level;
KW   Disulfide bond; Lipid-binding; Signal; Stress response; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..115
FT                   /note="Non-specific lipid-transfer protein 4.2"
FT                   /id="PRO_0000018384"
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;  11175 MW;  4996FE643EADBFAF CRC64;
     MARAAATQLV LVAMVAAMLI VATDAAISCG QVSSALSPCI SYARGNGAKP PVACCSGVKR
     LAGAAQSTAD KQAACKCIKS AAGGLNAGKA AGIPSMCGVS VPYAISASVD CSKIR