ID   NLTP1_VIGRR             Reviewed;          91 AA.
AC   P83434;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Non-specific lipid-transfer protein 1;
DE            Short=LTP 1;
DE            Short=NS-LTP1;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, STRUCTURE BY NMR, AND DISULFIDE BONDS.
RC   TISSUE=Sprout;
RX   PubMed=15823028; DOI=10.1021/bi047608v;
RA   Lin K.-F., Liu Y.-N., Hsu S.-T., Samuel D., Cheng C.-S., Bonvin A.M.,
RA   Lyu P.-C.;
RT   "Characterization and structural analyses of nonspecific lipid transfer
RT   protein 1 from mung bean.";
RL   Biochemistry 44:5703-5712(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-21, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=15350690; DOI=10.1016/j.peptides.2004.06.004;
RA   Wang S.Y., Wu J.H., Ng T.B., Ye X.Y., Rao P.F.;
RT   "A non-specific lipid transfer protein with antifungal and antibacterial
RT   activities from the mung bean.";
RL   Peptides 25:1235-1242(2004).
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. Has antifungal activity
CC       against F.solani, F.oxysporum, P.aphanidermatum and S.rolfsii. Has
CC       antibacterial activity against the Gram-positive bacterium S.aureus but
CC       not against the Gram-negative bacterium S.typhimurium.
CC       {ECO:0000269|PubMed:15350690, ECO:0000269|PubMed:15823028}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15823028, ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=9030; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15350690};
CC   -!- SIMILARITY: Belongs to the plant LTP family.
CC       {ECO:0000250|UniProtKB:P07597}.
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DR   PDB; 1SIY; NMR; -; A=1-91.
DR   PDBsum; 1SIY; -.
DR   AlphaFoldDB; P83434; -.
DR   SMR; P83434; -.
DR   STRING; 3916.P83434; -.
DR   EvolutionaryTrace; P83434; -.
DR   Proteomes; UP000087766; Genome assembly.
DR   GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IDA:UniProtKB.
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; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Lipid-binding; Reference proteome; Transport.
FT   CHAIN           1..91
FT                   /note="Non-specific lipid-transfer protein 1"
FT                   /id="PRO_0000153875"
FT   BINDING         44
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT                   /evidence="ECO:0000305|PubMed:15823028"
FT   BINDING         79
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:57643"
FT                   /evidence="ECO:0000305|PubMed:15823028"
FT   DISULFID        3..50
FT                   /evidence="ECO:0000269|PubMed:15823028,
FT                   ECO:0007744|PDB:1SIY"
FT   DISULFID        13..27
FT   DISULFID        28..73
FT   DISULFID        48..87
FT   CONFLICT        18
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   TURN            3..6
FT                   /evidence="ECO:0007829|PDB:1SIY"
FT   HELIX           7..17
FT                   /evidence="ECO:0007829|PDB:1SIY"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:1SIY"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:1SIY"
FT   HELIX           42..54
FT                   /evidence="ECO:0007829|PDB:1SIY"
FT   HELIX           63..73
FT                   /evidence="ECO:0007829|PDB:1SIY"
SQ   SEQUENCE   91 AA;  9299 MW;  0A966C1FDBB76E09 CRC64;
     MTCGQVQGNL AQCIGFLQKG GVVPPSCCTG VKNILNSSRT TADRRAVCSC LKAAAGAVRG
     INPNNAEALP GKCGVNIPYK ISTSTNCNSI N