GenomeNet

Database: UniProt
Entry: M5WD29_PRUPE
LinkDB: M5WD29_PRUPE
Original site: M5WD29_PRUPE 
ID   M5WD29_PRUPE            Unreviewed;       179 AA.
AC   M5WD29;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain-containing protein {ECO:0000259|SMART:SM00499};
GN   ORFNames=PRUPE_6G152000 {ECO:0000313|EMBL:ONI01668.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI01668.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI01668.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM007656; ONI01668.1; -; Genomic_DNA.
DR   RefSeq; XP_007205989.1; XM_007205927.1.
DR   AlphaFoldDB; M5WD29; -.
DR   STRING; 3760.M5WD29; -.
DR   EnsemblPlants; ONI01668; ONI01668; PRUPE_6G152000.
DR   GeneID; 18773852; -.
DR   Gramene; ONI01668; ONI01668; PRUPE_6G152000.
DR   KEGG; pper:18773852; -.
DR   eggNOG; ENOG502S59X; Eukaryota.
DR   HOGENOM; CLU_089796_5_2_1; -.
DR   OMA; FSKMNIV; -.
DR   OrthoDB; 472989at2759; -.
DR   Proteomes; UP000006882; Chromosome g6.
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:SF104; NON-SPECIFIC LIPID TRANSFER PROTEIN GPI-ANCHORED 2; 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:UP000006882};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          37..118
FT                   /note="Bifunctional inhibitor/plant lipid transfer
FT                   protein/seed storage helical"
FT                   /evidence="ECO:0000259|SMART:SM00499"
SQ   SEQUENCE   179 AA;  18065 MW;  40321AA6CA02A3FB CRC64;
     MGRAIMLLMM MTTTTMLHAV LGQEAPAPAP GPASPDCQTA VLGLADCLSY VMPGSNLTKP
     DKPCCPELAE LVKDNPICLC SLLANSNSSN SVGLEIDVNR ALKLPTVCKV STPPPSTCEL
     LGIPVGAPTA SEAPANSPGS GLTPQGPSAA TSPKSGASKT ANSVMAFLAG LVIAVLPIW
//
DBGET integrated database retrieval system