ID   OLEO3_MAIZE             Reviewed;         187 AA.
AC   P21641;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Oleosin Zm-II;
DE   AltName: Full=Lipid body-associated protein L2;
DE   AltName: Full=Oleosin 18 kDa;
GN   Name=OLE18; Synonyms=OLE3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-56.
RC   STRAIN=cv. Missouri 17;
RX   PubMed=2298748; DOI=10.1016/s0021-9258(19)39967-3;
RA   Qu R., Huang A.H.C.;
RT   "Oleosin KD 18 on the surface of oil bodies in maize. Genomic and cDNA
RT   sequences and the deduced protein structure.";
RL   J. Biol. Chem. 265:2238-2243(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. B73, and cv. Missouri 17;
RX   PubMed=7858232; DOI=10.1007/bf00019508;
RA   Lee K., Huang A.H.C.;
RT   "Genes encoding oleosins in maize kernel of inbreds Mo17 and B73.";
RL   Plant Mol. Biol. 26:1981-1987(1994).
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   -!- TISSUE SPECIFICITY: Found in embryonic axis, scutellum, and aleurone
CC       layer. {ECO:0000269|PubMed:7858232}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during seed maturation.
CC       {ECO:0000269|PubMed:7858232}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; J05212; AAA67699.1; -; Genomic_DNA.
DR   PIR; A35040; A35040.
DR   AlphaFoldDB; P21641; -.
DR   STRING; 4577.AC206941.2_FGP002; -.
DR   PaxDb; P21641; -.
DR   PRIDE; P21641; -.
DR   MaizeGDB; 65606; -.
DR   eggNOG; ENOG502S1R0; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P21641; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IBA:GO_Central.
DR   GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR   GO; GO:0050826; P:response to freezing; IBA:GO_Central.
DR   GO; GO:0010344; P:seed oilbody biogenesis; IBA:GO_Central.
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   Acetylation; Direct protein sequencing; Lipid droplet; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..187
FT                   /note="Oleosin Zm-II"
FT                   /id="PRO_0000108145"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          2..51
FT                   /note="Polar"
FT   REGION          17..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..123
FT                   /note="Hydrophobic"
FT   REGION          155..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  18501 MW;  22D694B8B1697351 CRC64;
     MADRDRSGIY GGAHATYGQQ QQQGGGGRPM GEQVKKGMLH DKGPTASQAL TVATLFPLGG
     LLLVLSGLAL TASVVGLAVA TPVFLIFSPV LVPAALLIGT AVMGFLTSGA LGLGGLSSLT
     CLANTARQAF QRTPDYVEEA RRRMAEAAAQ AGHKTAQAGQ AIQGRAQEAG TGGGAGAGAG
     GGGRASS