ID A0A498HWJ1_MALDO Unreviewed; 204 AA.
AC A0A498HWJ1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain-containing protein {ECO:0000259|SMART:SM00499};
GN ORFNames=DVH24_042613 {ECO:0000313|EMBL:RXH75826.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH75826.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH75826.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH75826.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-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:RXH75826.1}.
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DR EMBL; RDQH01000341; RXH75826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498HWJ1; -.
DR SMR; A0A498HWJ1; -.
DR STRING; 3750.A0A498HWJ1; -.
DR EnsemblPlants; mRNA:MD15G0311700; mRNA:MD15G0311700; MD15G0311700.
DR Gramene; mRNA:MD15G0311700; mRNA:MD15G0311700; MD15G0311700.
DR OrthoDB; 1127351at2759; -.
DR Proteomes; UP000290289; Chromosome 15.
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 GO; GO:0006869; P:lipid transport; IEA:InterPro.
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 InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33044; BIFUNCTIONAL INHIBITOR/LIPID-TRANSFER PROTEIN/SEED STORAGE 2S ALBUMIN SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR33044:SF27; NON-SPECIFIC LIPID TRANSFER PROTEIN GPI-ANCHORED 29-RELATED; 1.
DR Pfam; PF14368; LTP_2; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000290289};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..204
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019778554"
FT DOMAIN 51..130
FT /note="Bifunctional inhibitor/plant lipid transfer
FT protein/seed storage helical"
FT /evidence="ECO:0000259|SMART:SM00499"
FT REGION 138..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 21076 MW; F4115F410460D959 CRC64;
MERLIFILTT CFMLANCARI PDVDPLSYAA SPEPSSPDVP KTAGSPSADG CNDVIFEIAD
CIPFLSDGNT NTKPEGSCCP GLEMVLKASD GCICEAIESS ADLGVHINMT KAMTLPSACG
ISAPSFLSEC NIPLPPGASA QVPHTHAPKS SPKSQSPKPS QAPRSSVNVV PSPVTAPHAG
TYSVSASLVL TLSMLSASFY CISF
//
