ID   NLTP3_VITSX             Reviewed;          91 AA.
AC   P80273; P85104;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Non-specific lipid-transfer protein P3;
DE            Short=LTP P3;
OS   Vitis sp. (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis; unclassified Vitis.
OX   NCBI_TaxID=3604;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=V.berlandieri X V.vinifera cv. 41B;
RA   Girault T., Francois J., Rogniaux H., Delrot S., Lemoine R.,
RA   Coutos-Thevenot P., Gomes E.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-37.
RC   STRAIN=V.vinifera X Berlanchen cv. Rootstock 41B;
RX   PubMed=8223644; DOI=10.1111/j.1432-1033.1993.tb18317.x;
RA   Coutos-Thevenot P., Jouenne T., Maes O., Guerbette F., Grosbois M.,
RA   Le Caer J.-P., Boulay M., Deloire A., Kader J.-C., Guern J.;
RT   "Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms
RT   of lipid-transfer proteins.";
RL   Eur. J. Biochem. 217:885-889(1993).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=9274.5; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   PIR; S39036; S39036.
DR   AlphaFoldDB; P80273; -.
DR   SMR; P80273; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Direct protein sequencing; Disulfide bond; Lipid-binding; Secreted;
KW   Transport.
FT   CHAIN           1..91
FT                   /note="Non-specific lipid-transfer protein P3"
FT                   /id="PRO_0000153886"
FT   DISULFID        3..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..27
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..87
FT                   /evidence="ECO:0000250"
FT   CONFLICT        33
FT                   /note="N -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="N -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   91 AA;  9283 MW;  4189595343A79BE0 CRC64;
     LSCGDVATQM ASCINYLRGA GPLPAACCNG VKNLKNSATT TQDRRTACKC LISASKTISG
     VNFGLAAGLP AKCGVSIPYK ISPSTNCDQV N