ID A0A0D3HL57_9ORYZ Unreviewed; 117 AA.
AC A0A0D3HL57;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART11G11440.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART11G11440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G11440.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART11G11440.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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|RuleBase:RU000628}.
CC -!- SIMILARITY: Belongs to the plant LTP family.
CC {ECO:0000256|ARBA:ARBA00009748, ECO:0000256|RuleBase:RU000628}.
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DR AlphaFoldDB; A0A0D3HL57; -.
DR SMR; A0A0D3HL57; -.
DR STRING; 65489.A0A0D3HL57; -.
DR PaxDb; 65489-OBART11G11420-1; -.
DR EnsemblPlants; OBART11G11420.1; OBART11G11420.1; OBART11G11420.
DR EnsemblPlants; OBART11G11440.1; OBART11G11440.1; OBART11G11440.
DR Gramene; OBART11G11420.1; OBART11G11420.1; OBART11G11420.
DR Gramene; OBART11G11440.1; OBART11G11440.1; OBART11G11440.
DR eggNOG; ENOG502S4CI; Eukaryota.
DR HOGENOM; CLU_128423_0_0_1; -.
DR Proteomes; UP000026960; Chromosome 11.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR CDD; cd01960; nsLTP1; 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; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076:SF161; NON-SPECIFIC LIPID-TRANSFER PROTEIN 1; 1.
DR PANTHER; PTHR33076; NON-SPECIFIC LIPID-TRANSFER PROTEIN 2-RELATED; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
DR PROSITE; PS00597; PLANT_LTP; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU000628}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..117
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010907800"
FT DOMAIN 28..113
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
SQ SEQUENCE 117 AA; 11569 MW; 7A4632F5B6F1C17D CRC64;
MARAQLVLVA VVAALLLAAP HAAVAITCGQ VNSAVGPCLT YARGGGAGPS AACCNGVRSL
KSAARTTADR RTACNCLKNA ARGIKGLNAG NAASIPSKCG VSVPYTISAS IDCSRVR
//
