ID A0A314XT13_PRUYE Unreviewed; 206 AA.
AC A0A314XT13;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Protein YLS3-like {ECO:0000313|EMBL:PQP95769.1};
GN ORFNames=Pyn_16220 {ECO:0000313|EMBL:PQP95769.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQP95769.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQP95769.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQP95769.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the plant LTP family.
CC {ECO:0000256|ARBA:ARBA00009748}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PQP95769.1}.
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DR EMBL; PJQY01002190; PQP95769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314XT13; -.
DR STRING; 2094558.A0A314XT13; -.
DR Proteomes; UP000250321; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; IPR043325; LTSS.
DR PANTHER; PTHR33044; BIFUNCTIONAL INHIBITOR/LIPID-TRANSFER PROTEIN/SEED STORAGE 2S ALBUMIN SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR33044:SF144; PROTEIN YLS3-LIKE; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Reference proteome {ECO:0000313|Proteomes:UP000250321};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..206
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016424964"
FT DOMAIN 31..108
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
FT REGION 119..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 206 AA; 21444 MW; F16A47177C00B2C6 CRC64;
MRNKKLKVFC IVVASLAMAS MATMEDDENE CAEQMATLAA CIPFVSGTAK KPTPECCENT
KKVKATKPKC LCALIKESAD PSMGLPVNTT LALQMPSACN IDGKISDCPS ILKLPPNSPD
AKIFKEADSN STTSPTTDGH DHQSTPSSAS TSSSSSVSTS PSSSSSGSDS KPSDSKANPS
SGATLMKLTG TTYLLMMMVS MALMLN
//