ID   NLTP2_ACTDE             Reviewed;          92 AA.
AC   P85206;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Non-specific lipid-transfer protein 2 {ECO:0000303|PubMed:22114713};
DE            Short=LTP2 {ECO:0000303|PubMed:22114713};
DE   AltName: Allergen=Act d 10.02 {ECO:0000303|PubMed:22114713};
OS   Actinidia deliciosa (Kiwi).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Actinidiaceae; Actinidia.
OX   NCBI_TaxID=3627;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND ALLERGENICITY.
RC   TISSUE=Seed {ECO:0000269|PubMed:22114713};
RX   PubMed=22114713; DOI=10.1371/journal.pone.0027856;
RA   Bernardi M.L., Giangrieco I., Camardella L., Ferrara R., Palazzo P.,
RA   Panico M.R., Crescenzo R., Carratore V., Zennaro D., Liso M., Santoro M.,
RA   Zuzzi S., Tamburrini M., Ciardiello M.A., Mari A.;
RT   "Allergenic lipid transfer proteins from plant-derived foods do not
RT   immunologically and clinically behave homogeneously: the kiwifruit LTP as a
RT   model.";
RL   PLoS ONE 6:E27856-E27856(2011).
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).
CC       {ECO:0000250|UniProtKB:Q42952}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds and, at very low levels, in pulp
CC       of fruit (at protein level). {ECO:0000269|PubMed:22114713}.
CC   -!- MASS SPECTROMETRY: Mass=9484; Mass_error=20; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22114713};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:22114713}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85206; -.
DR   SMR; P85206; -.
DR   Allergome; 5737; Act d 10.
DR   Allergome; 5739; Act d 10.0201.
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.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW   Transport.
FT   CHAIN           1..92
FT                   /note="Non-specific lipid-transfer protein 2"
FT                   /id="PRO_0000415603"
FT   DISULFID        4..52
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        29..74
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
SQ   SEQUENCE   92 AA;  9488 MW;  B82E8B0137FBB0C3 CRC64;
     TVSCGQVDTA LTPCLTYLTK GGTPSTQCCS GVRSLKSMTG TKVPDRQAAC NCLKQAAARY
     QGIKDAAAAL SQKCGVQLSV PISRSTDCSK IS