ID   NLTP2_LENCU             Reviewed;         118 AA.
AC   A0AT29; P84255;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Non-specific lipid-transfer protein 2;
DE            Short=LTP2;
DE   Contains:
DE     RecName: Full=Non-specific lipid-transfer protein 7;
DE              Short=LTP7;
DE   Flags: Precursor;
OS   Lens culinaris (Lentil) (Cicer lens).
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; Hologalegina; IRL clade; Fabeae; Lens.
OX   NCBI_TaxID=3864;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seedling;
RX   PubMed=17511608; DOI=10.1134/s0006297907040104;
RA   Finkina E.I., Balandin S.V., Serebryakova M.V., Potapenko N.A.,
RA   Tagaev A.A., Ovchinnikova T.V.;
RT   "Purification and primary structure of novel lipid transfer proteins from
RT   germinated lentil (Lens culinaris) seeds.";
RL   Biochemistry (Mosc.) 72:430-438(2007).
RN   [2]
RP   FUNCTION.
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).
RN   [3]
RP   STRUCTURE BY NMR OF 26-118, AND DISULFIDE BONDS.
RX   PubMed=23998937; DOI=10.1016/j.bbrc.2013.08.078;
RA   Gizatullina A.K., Finkina E.I., Mineev K.S., Melnikova D.N., Bogdanov I.V.,
RA   Telezhinskaya I.N., Balandin S.V., Shenkarev Z.O., Arseniev A.S.,
RA   Ovchinnikova T.V.;
RT   "Recombinant production and solution structure of lipid transfer protein
RT   from lentil Lens culinaris.";
RL   Biochem. Biophys. Res. Commun. 439:427-432(2013).
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, jasmonic acid and, with highest efficiency,
CC       unsaturated fatty acids and lysolipids (PubMed:26680443).
CC       {ECO:0000250|UniProtKB:Q42952, ECO:0000269|PubMed:26680443}.
CC   -!- MASS SPECTROMETRY: [Non-specific lipid-transfer protein 2]:
CC       Mass=9283.1; Method=MALDI; Note=LTP2.;
CC       Evidence={ECO:0000269|PubMed:17511608};
CC   -!- MASS SPECTROMETRY: [Non-specific lipid-transfer protein 7]:
CC       Mass=9135.9; Method=MALDI; Note=LTP7.;
CC       Evidence={ECO:0000269|PubMed:17511608};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR   EMBL; AY793554; AAX35807.1; -; mRNA.
DR   PDB; 2MAL; NMR; -; A=26-118.
DR   PDB; 5LQV; NMR; -; A=26-118.
DR   PDBsum; 2MAL; -.
DR   PDBsum; 5LQV; -.
DR   AlphaFoldDB; A0AT29; -.
DR   BMRB; A0AT29; -.
DR   SMR; A0AT29; -.
DR   Allergome; 8712; Len c 3.
DR   Allergome; 8713; Len c 3.0101.
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   3D-structure; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW   Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:17511608"
FT   CHAIN           26..118
FT                   /note="Non-specific lipid-transfer protein 2"
FT                   /id="PRO_5000147974"
FT   CHAIN           26..117
FT                   /note="Non-specific lipid-transfer protein 7"
FT                   /id="PRO_0000287336"
FT   DISULFID        29..76
FT                   /evidence="ECO:0000269|PubMed:23998937,
FT                   ECO:0007744|PDB:2MAL"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000269|PubMed:23998937,
FT                   ECO:0007744|PDB:2MAL"
FT   DISULFID        54..99
FT                   /evidence="ECO:0000269|PubMed:23998937,
FT                   ECO:0007744|PDB:2MAL"
FT   DISULFID        74..113
FT                   /evidence="ECO:0000269|PubMed:23998937,
FT                   ECO:0007744|PDB:2MAL"
FT   HELIX           30..43
FT                   /evidence="ECO:0007829|PDB:2MAL"
FT   HELIX           51..62
FT                   /evidence="ECO:0007829|PDB:2MAL"
FT   HELIX           67..81
FT                   /evidence="ECO:0007829|PDB:2MAL"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:2MAL"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:2MAL"
SQ   SEQUENCE   118 AA;  11880 MW;  BF6F4DE60A0D2703 CRC64;
     MARGMKLACV VLVICMVVIA PMAEGAISCG AVTSDLSPCL TYLTGGPGPS PQCCGGVKKL
     LAAANTTPDR QAACNCLKSA AGSITKLNTN NAAALPGKCG VNIPYKISTT TNCNTVKF