ID   OLEO2_BRANA             Reviewed;         175 AA.
AC   P29111;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Major oleosin NAP-II;
DE   Flags: Fragment;
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], AND PROTEIN SEQUENCE OF 43-77.
RC   TISSUE=Seed;
RX   PubMed=1989697; DOI=10.1016/0167-4781(91)90156-g;
RA   Murphy D.J., Keen J.N., O'Sullivan J.N., Au D.M.Y., Edwards E.-W.,
RA   Jackson P.J., Cummins I., Gibbons T., Shaw C.H., Ryan A.J.;
RT   "A class of amphipathic proteins associated with lipid storage bodies in
RT   plants. Possible similarities with animal serum apolipoproteins.";
RL   Biochim. Biophys. Acta 1088:86-94(1991).
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.
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   -!- DEVELOPMENTAL STAGE: Accumulates during the desiccation phase of embryo
CC       development.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; X58000; CAA41064.1; -; mRNA.
DR   PIR; S70915; S70915.
DR   AlphaFoldDB; P29111; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Lipid droplet; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..175
FT                   /note="Major oleosin NAP-II"
FT                   /id="PRO_0000108134"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          17..26
FT   REPEAT          27..36
FT   REGION          <1..47
FT                   /note="Polar"
FT   REGION          48..119
FT                   /note="Hydrophobic"
FT   REGION          151..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        49
FT                   /note="V -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="L -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="A -> L (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   175 AA;  19349 MW;  E166698E285ABC38 CRC64;
     RRDQYPRDRD QYSMIGRDRD KYSMIGRDRD QYNMYGRDYS KSRQIAKAVT AVTAGGSLLV
     LSSLTLVGTV IALTVATPLL VIFSPILVPA LITVALLITG FLSSGGFGIA AITVFSWIYK
     YATGEHPQGS DKLDSARMKL GGKVQDMKDR AQYYGQQQTG GEDDRDRTRG TQHTT