ID A0A251QP67_PRUPE Unreviewed; 122 AA.
AC A0A251QP67;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain-containing protein {ECO:0000259|Pfam:PF14368};
GN ORFNames=PRUPE_2G242700 {ECO:0000313|EMBL:ONI24485.1};
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 {ECO:0000313|EMBL:ONI24485.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI24485.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(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.
CC {ECO:0000256|ARBA:ARBA00003211}.
CC -!- SIMILARITY: Belongs to the plant LTP family.
CC {ECO:0000256|ARBA:ARBA00009748}.
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DR EMBL; CM007652; ONI24485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251QP67; -.
DR STRING; 3760.A0A251QP67; -.
DR EnsemblPlants; ONI24485; ONI24485; PRUPE_2G242700.
DR Gramene; ONI24485; ONI24485; PRUPE_2G242700.
DR OrthoDB; 802948at2759; -.
DR Proteomes; UP000006882; Chromosome g2.
DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
DR GO; GO:0009627; P:systemic acquired resistance; IEA:InterPro.
DR CDD; cd00010; AAI_LTSS; 1.
DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR039265; DIR1-like.
DR PANTHER; PTHR33122; LIPID BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33122:SF4; OS04G0415800 PROTEIN; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..122
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013168594"
FT DOMAIN 45..111
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|Pfam:PF14368"
SQ SEQUENCE 122 AA; 12976 MW; 79BDD0B4DA2AEDD6 CRC64;
MGGGLILRYM WMVGLFAIVG NNWGFEIEGV EGDGECGQLD PEVLIYKLAS CAPSGQDENV
EVPPKCCGLI QKVRTSCLCA IILSKEAKSL GINPVVAATI PKRCKIAGRP KGYKCGAYVV
QA
//
