ID   OLEO1_PRUDU             Reviewed;         148 AA.
AC   Q43804;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Oleosin 1;
GN   Name=OLE1;
OS   Prunus dulcis (Almond) (Amygdalus dulcis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Texas; TISSUE=Immature seed;
RX   PubMed=7865791; DOI=10.1007/bf00019192;
RA   Garcia-Mas J., Messeguer R., Arus P., Puigdomenech P.;
RT   "Molecular characterization of cDNAs corresponding to genes expressed
RT   during almond (Prunus amygdalus Batsch) seed development.";
RL   Plant Mol. Biol. 27:205-210(1995).
CC   -!- FUNCTION: May have a structural role to stabilize the lipid body during
CC       desiccation of the seed by preventing coalescence of the oil. Probably
CC       interacts with both lipid and phospholipid moieties of lipid bodies.
CC       May also provide recognition signals for specific lipase anchorage in
CC       lipolysis during seedling growth (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet. Membrane; Multi-pass membrane
CC       protein. Note=Surface of oil bodies. Oleosins exist at a monolayer
CC       lipid/water interface.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; X78118; CAA55008.1; -; mRNA.
DR   PIR; S51940; S51940.
DR   AlphaFoldDB; Q43804; -.
DR   EnsemblPlants; VVA10868; VVA10868; Prudul26B006731.
DR   Gramene; VVA10868; VVA10868; Prudul26B006731.
DR   OMA; FGQQHIT; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IEA:InterPro.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   InterPro; IPR000136; Oleosin.
DR   PANTHER; PTHR33203; PTHR33203; 1.
DR   Pfam; PF01277; Oleosin; 1.
DR   PROSITE; PS00811; OLEOSINS; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Lipid droplet; Membrane; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..148
FT                   /note="Oleosin 1"
FT                   /id="PRO_0000108141"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          2..28
FT                   /note="Polar"
FT   REGION          29..148
FT                   /note="Hydrophobic"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   148 AA;  15612 MW;  0530F205082DCC7C CRC64;
     MADQHFQQPL HFQGSYGQQQ PRSYQVAKAA TAVTAGGSLL VLSGLVLAGT VIALTIATPL
     LVIFSPVLVP ALITVALITM GFLTSGGFGV AAVTVLSWIY KYVTGKQPPG ADQLDQARHK
     LAGKARDIKD RAEQFGQQHV PSGQQQSS