ID   NLTP_ANEGR              Reviewed;         122 AA.
AC   A0A0B4JDK1;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Non-specific lipid-transfer protein {ECO:0000303|PubMed:26680443};
DE            Short=Ag-LTP {ECO:0000303|PubMed:26680443};
DE   Flags: Precursor;
OS   Anethum graveolens (Dill).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Anethum.
OX   NCBI_TaxID=40922 {ECO:0000303|PubMed:26680443};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-50, FUNCTION, SUBUNIT,
RP   MASS SPECTROMETRY, STRUCTURE BY NMR OF 30-122, DISULFIDE BONDS, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000303|PubMed:26680443};
RX   PubMed=26680443; DOI=10.1002/psc.2840;
RA   Melnikova D.N., Mineev K.S., Finkina E.I., Arseniev A.S.,
RA   Ovchinnikova T.V.;
RT   "A novel lipid transfer protein from the dill Anethum graveolens L.:
RT   isolation, structure, heterologous expression, and functional
RT   characteristics.";
RL   J. Pept. Sci. 22:59-66(2016).
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 (By similarity). Binds
CC       saturated fatty acids, unsaturated fatty acids, lysolipids and, with
CC       highest efficiency, jasmonic acid. Has weak antimicrobial activity
CC       against fungi. Inhibits spore germination and hyphae elongation in
CC       A.niger VKM F-2259 and N.crassa VKM F-184. Has no antibacterial
CC       activity against A.tumefaciens A281, C.michiganensis VKM Ac-144 and
CC       P.syringae VKM B-1546 (PubMed:26680443). {ECO:0000250|UniProtKB:Q42952,
CC       ECO:0000269|PubMed:26680443}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26680443}.
CC   -!- MASS SPECTROMETRY: Mass=9524.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26680443};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU000628}.
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DR   EMBL; JF823967; AEG79730.2; -; mRNA.
DR   PDB; 2N2Z; NMR; -; A=30-122.
DR   PDBsum; 2N2Z; -.
DR   AlphaFoldDB; A0A0B4JDK1; -.
DR   BMRB; A0A0B4JDK1; -.
DR   SMR; A0A0B4JDK1; -.
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   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   3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Lipid-binding; Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..29
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436565"
FT   CHAIN           30..122
FT                   /note="Non-specific lipid-transfer protein"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436566"
FT   DISULFID        32..81
FT                   /evidence="ECO:0007744|PDB:2N2Z"
FT   DISULFID        42..58
FT                   /evidence="ECO:0007744|PDB:2N2Z"
FT   DISULFID        59..104
FT                   /evidence="ECO:0007744|PDB:2N2Z"
FT   DISULFID        79..118
FT                   /evidence="ECO:0007744|PDB:2N2Z"
FT   HELIX           32..39
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   HELIX           56..68
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   HELIX           72..88
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   HELIX           94..104
FT                   /evidence="ECO:0007829|PDB:2N2Z"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:2N2Z"
SQ   SEQUENCE   122 AA;  12570 MW;  66B10E305EBD4B4D CRC64;
     MGVSRACFVV MVVVYMVVAA TPNVKLAEAL TCGQVTGALA PCLGYLRTAG SVPVPLTCCN
     GVRGLNNAAR TTIDRRTACN CLKQTANAIA DLNLNAAAGL PAKCGVNIPY KISPSTDCNR
     VV