NLTP1_HELAN
ID NLTP1_HELAN Reviewed; 116 AA.
AC P82007; Q7M1P2; Q7X9Q5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Non-specific lipid-transfer protein AP10;
DE Short=Ha-AP10;
DE Short=LTP;
DE Short=NsLTP;
DE Flags: Precursor;
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=AR10018; TISSUE=Seed;
RX PubMed=12685036; DOI=10.1078/0176-1617-00799;
RA Regente M., de la Canal L.;
RT "A cDNA encoding a putative lipid transfer protein expressed in sunflower
RT seeds.";
RL J. Plant Physiol. 160:201-203(2003).
RN [2]
RP PROTEIN SEQUENCE OF 27-50, AND FUNCTION.
RC STRAIN=cv. Rodeo; TISSUE=Seed;
RX PubMed=2266969; DOI=10.1007/bf00231367;
RA Arondel V., Vergnolle C., Tchang F., Kader J.-C.;
RT "Bifunctional lipid-transfer: fatty acid-binding proteins in plants.";
RL Mol. Cell. Biochem. 98:49-56(1990).
RN [3]
RP PROTEIN SEQUENCE OF 27-46, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AR10018; TISSUE=Seed;
RA Regente M.C., de la Canal L.;
RT "Purification, characterization and antifungal properties of a lipid-
RT transfer protein from sunflower (Helianthus annuus) seeds.";
RL Physiol. Plantarum 110:158-163(2000).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16008084; DOI=10.1016/j.jplph.2004.10.006;
RA Gonorazky A.G., Regente M.C., de la Canal L.;
RT "Stress induction and antimicrobial properties of a lipid transfer protein
RT in germinating sunflower seeds.";
RL J. Plant Physiol. 162:618-624(2005).
RN [5]
RP FUNCTION.
RX PubMed=15715642; DOI=10.1111/j.1472-765x.2004.01647.x;
RA Regente M.C., Giudici A.M., Villalain J., de la Canal L.;
RT "The cytotoxic properties of a plant lipid transfer protein involve
RT membrane permeabilization of target cells.";
RL Lett. Appl. Microbiol. 40:183-189(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19117640; DOI=10.1016/j.jplph.2008.11.005;
RA Pagnussat L.A., Lombardo C., Regente M., Pinedo M., Martin M.,
RA de la Canal L.;
RT "Unexpected localization of a lipid transfer protein in germinating
RT sunflower seeds.";
RL J. Plant Physiol. 166:797-806(2009).
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. Permeabilizes the
CC membrane of fungal spores, inhibits germination of the spores of the
CC fungus F.solani at a concentration of 40 ug/ml. Inhibits the growth of
CC F.solani with an IC(50) of 6.5 ug/ml, weakly inhibits the growth of the
CC fungus A.alternata. Binds oleoyl-CoA. {ECO:0000269|PubMed:15715642,
CC ECO:0000269|PubMed:16008084, ECO:0000269|PubMed:2266969,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Membrane.
CC Note=Present intracellularly, associated with unidentified structures.
CC -!- TISSUE SPECIFICITY: In germinating seeds, detected in the entire
CC surface of the cotyledons, shoot meristem, inter-cotyledon space,
CC primary xylem and immature vascular elements (at protein level).
CC Expressed in seeds, but not the aerial parts of the plant.
CC {ECO:0000269|PubMed:12685036, ECO:0000269|PubMed:16008084,
CC ECO:0000269|PubMed:19117640}.
CC -!- DEVELOPMENTAL STAGE: Present during at least the first 5 days of
CC germination. {ECO:0000269|PubMed:16008084}.
CC -!- INDUCTION: By salt stress, abscisic acid (ABA) and fungal infection.
CC {ECO:0000269|PubMed:16008084}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AF529201; AAP47226.1; -; mRNA.
DR PIR; PH0084; PH0084.
DR AlphaFoldDB; P82007; -.
DR SMR; P82007; -.
DR Allergome; 2862; Hel a 3.
DR Allergome; 3308; Hel a 3.0101.
DR EnsemblPlants; mRNA:HanXRQr2_Chr15g0684801; mRNA:HanXRQr2_Chr15g0684801; HanXRQr2_Chr15g0684801.
DR Gramene; mRNA:HanXRQr2_Chr15g0684801; mRNA:HanXRQr2_Chr15g0684801; HanXRQr2_Chr15g0684801.
DR OMA; RTACKCA; -.
DR OrthoDB; 1606522at2759; -.
DR PhylomeDB; P82007; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; 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; PF14368; LTP_2; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW Lipid-binding; Membrane; Plant defense; Secreted; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2266969, ECO:0000269|Ref.3"
FT CHAIN 27..116
FT /note="Non-specific lipid-transfer protein AP10"
FT /id="PRO_0000153873"
FT DISULFID 29..76
FT /evidence="ECO:0000250"
FT DISULFID 39..53
FT /evidence="ECO:0000250"
FT DISULFID 54..98
FT /evidence="ECO:0000250"
FT DISULFID 74..112
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="G -> S (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 11954 MW; AC64611183234FC3 CRC64;
MKGTSMGVAI LAMIVMAQLM VHPSVAITCN DVTGNLTPCL PYLRSGGKPT PACCAGAKKL
LGATRTQADR RTACKCAKTA APQLKVRPDM ASSLPGKCGI STSIPINPNV NCNTIP
