ID   OLES1_BRANA             Reviewed;         193 AA.
AC   C3S7F0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Oleosin S1-2;
GN   Name=S1;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19562800; DOI=10.1002/pmic.200800449;
RA   Jolivet P., Boulard C., Bellamy A., Larre C., Barre M., Rogniaux H.,
RA   d'Andrea S., Chardot T., Nesi N.;
RT   "Protein composition of oil bodies from mature Brassica napus seeds.";
RL   Proteomics 9:3268-3284(2009).
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 {ECO:0000269|PubMed:19562800}.
CC       Membrane {ECO:0000269|PubMed:19562800}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:19562800}. Note=Surface of oil bodies. Oleosins
CC       exist at a monolayer lipid/water interface.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; EU678257; ACG69505.1; -; mRNA.
DR   AlphaFoldDB; C3S7F0; -.
DR   SMR; C3S7F0; -.
DR   iPTMnet; C3S7F0; -.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Lipid droplet; Membrane; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:19562800"
FT   CHAIN           2..193
FT                   /note="Oleosin S1-2"
FT                   /id="PRO_0000381927"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          2..39
FT                   /note="Polar"
FT                   /evidence="ECO:0000250"
FT   REGION          40..113
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000250"
FT   REGION          139..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:19562800"
SQ   SEQUENCE   193 AA;  20722 MW;  19BBFFB127651C2F CRC64;
     MADVRTHAHQ VQVHPLRQHE GGIKVVYPQS GPSSTQVLAV VAGVPVGGTL LTLAGLTLAV
     SVIGLILAFP LFLIFSPVIV PAAFVIGLAM TGFMASGAIG LTGLSSMSWV LNHIRRVRER
     IPDELDEAKQ RLADMAEYAG QRTKDAGQTI EDKAHDVRES KTYDVRDRDT KGHTASGGDR
     DTKTTREVRV ATT