ID   OLES2_BRANA             Reviewed;         188 AA.
AC   C3S7F1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Oleosin S2-2;
GN   Name=S2;
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; EU678258; ACG69506.1; -; mRNA.
DR   RefSeq; XP_013725019.1; XM_013869565.1.
DR   AlphaFoldDB; C3S7F1; -.
DR   SMR; C3S7F1; -.
DR   iPTMnet; C3S7F1; -.
DR   EnsemblPlants; CDY20040; CDY20040; GSBRNA2T00009878001.
DR   GeneID; 106428814; -.
DR   Gramene; CDY20040; CDY20040; GSBRNA2T00009878001.
DR   KEGG; bna:106428814; -.
DR   OMA; YFRQGKS; -.
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..188
FT                   /note="Oleosin S2-2"
FT                   /id="PRO_0000381928"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          2..51
FT                   /note="Polar"
FT                   /evidence="ECO:0000250"
FT   REGION          52..125
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000250"
FT   REGION          164..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:19562800"
SQ   SEQUENCE   188 AA;  19880 MW;  BB99F43234633EE3 CRC64;
     MATVERRVQV DPTDKRIHLQ PQYEGDVGYG YGYGGRADYK SSGPSSNQIV ALIVGVPVGG
     SLLALAGLTL AGSVIGLMLS VPLFLLFSPV IVPAAITIGL AVTAILASGL FGLTGLSSVS
     WVLNYLRGTS DTVPEQLDYA KRRMADAVGY AGQKGKEMGQ YVQDKAHEAH DTSLTTETTE
     PGKTRRHT