ID I1Q2V8_ORYGL Unreviewed; 147 AA.
AC I1Q2V8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA06G0147100.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA06G0147100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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|RuleBase:RU000628}.
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DR AlphaFoldDB; I1Q2V8; -.
DR STRING; 4538.I1Q2V8; -.
DR EnsemblPlants; ORGLA06G0147100.1; ORGLA06G0147100.1; ORGLA06G0147100.
DR Gramene; ORGLA06G0147100.1; ORGLA06G0147100.1; ORGLA06G0147100.
DR eggNOG; ENOG502S6F2; Eukaryota.
DR HOGENOM; CLU_128423_2_3_1; -.
DR OMA; SECCAGV; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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:SF181; NON-SPECIFIC LIPID-TRANSFER PROTEIN; 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.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU000628}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..147
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003650762"
FT DOMAIN 35..121
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 147 AA; 15112 MW; 54637F071128C6DD CRC64;
MGKNASRLAV AAVVVFALLL SLRQLEAADD VSVSCSDVVA DVTPCLGFLQ GDDDHPSGEC
CDGLSGLVAA AATTEDRQAA CECLKSAVSG QFTAVEAAPA RDLPADCGLS LPYTFSPDVD
CSQSQGHNQA FKQPNNSSTG PQLPPRN
//
