ID A0A0S3RKD5_PHAAN Unreviewed; 112 AA.
AC A0A0S3RKD5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
GN Name=Vigan.03G067300 {ECO:0000313|EMBL:BAT81028.1};
GN ORFNames=VIGAN_03067300 {ECO:0000313|EMBL:BAT81028.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT81028.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT81028.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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 EMBL; AP015036; BAT81028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RKD5; -.
DR Proteomes; UP000291084; Chromosome 3.
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; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|RuleBase:RU000628}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..112
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006617112"
FT DOMAIN 35..108
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
SQ SEQUENCE 112 AA; 12348 MW; DF9D211893CE7436 CRC64;
MMFVSFFTIL FVSVIATEAS NGLTCEQEKA LVMPCSDFVT KKTVEPSTLC CKGLNQIISL
TPEEKSSACT CLKEAASHIP NLDKDRINHL PKACKLNLDY PISNDFDCTL IL
//
