ID   NLTP1_PRUPE             Reviewed;          91 AA.
AC   P81402;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Non-specific lipid-transfer protein 1;
DE            Short=LTP 1;
DE   AltName: Full=Allergen Pru p 1;
DE   AltName: Full=Major allergen Pru p 3;
DE   AltName: Allergen=Pru p 3;
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=10614824; DOI=10.1515/bc.1999.167;
RA   Pastorello E.A., Ortolani C., Baroglio C., Pravettoni V., Ispano M.,
RA   Giuffrida M.G., Fortunato D., Farioli L., Monza M., Napolitano L.,
RA   Sacco M., Scibola E., Conti A.;
RT   "Complete amino acid sequence determination of the major allergen of peach
RT   (Prunus persica) Pru p 1.";
RL   Biol. Chem. 380:1315-1320(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-32; 53-66 AND 73-80.
RX   PubMed=10069889; DOI=10.1016/s0091-6749(99)70480-x;
RA   Pastorello E.A., Farioli L., Pravettoni V., Ortolani C., Ispano M.,
RA   Monza M., Baroglio C., Scibola E., Ansaloni R., Incorvaia C., Conti A.;
RT   "The major allergen of peach (Prunus persica) is a lipid transfer
RT   protein.";
RL   J. Allergy Clin. Immunol. 103:520-526(1999).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=16388823; DOI=10.1016/j.jmb.2005.11.063;
RA   Pasquato N., Berni R., Folli C., Folloni S., Cianci M., Pantano S.,
RA   Helliwell J.R., Zanotti G.;
RT   "Crystal structure of peach Pru p 3, the prototypic member of the family of
RT   plant non-specific lipid transfer protein pan-allergens.";
RL   J. Mol. Biol. 356:684-694(2006).
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   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   PDB; 2ALG; X-ray; 2.30 A; A/B=1-91.
DR   PDB; 2B5S; X-ray; 2.35 A; A/B=1-91.
DR   PDBsum; 2ALG; -.
DR   PDBsum; 2B5S; -.
DR   AlphaFoldDB; P81402; -.
DR   BMRB; P81402; -.
DR   SMR; P81402; -.
DR   STRING; 3760.EMJ07358; -.
DR   Allergome; 3454; Pru p 3.0101.
DR   Allergome; 603; Pru p 3.
DR   eggNOG; ENOG502S4CI; Eukaryota.
DR   EvolutionaryTrace; P81402; -.
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; Allergen; Direct protein sequencing; Disulfide bond;
KW   Lipid-binding; Transport.
FT   CHAIN           1..91
FT                   /note="Non-specific lipid-transfer protein 1"
FT                   /id="PRO_0000153880"
FT   DISULFID        3..50
FT                   /evidence="ECO:0000269|PubMed:16388823,
FT                   ECO:0007744|PDB:2ALG"
FT   DISULFID        13..27
FT                   /evidence="ECO:0000269|PubMed:16388823,
FT                   ECO:0007744|PDB:2ALG"
FT   DISULFID        28..73
FT                   /evidence="ECO:0000269|PubMed:16388823,
FT                   ECO:0007744|PDB:2ALG"
FT   DISULFID        48..87
FT                   /evidence="ECO:0000269|PubMed:16388823,
FT                   ECO:0007744|PDB:2ALG"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           14..19
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           25..37
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           41..57
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           63..72
FT                   /evidence="ECO:0007829|PDB:2ALG"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:2ALG"
SQ   SEQUENCE   91 AA;  9178 MW;  BB84569AA9E4B332 CRC64;
     ITCGQVSSAL APCIPYVRGG GAVPPACCNG IRNVNNLART TPDRQAACNC LKQLSASVPG
     VNPNNAAALP GKCGVHIPYK ISASTNCATV K