ID   OLE_PINEL               Reviewed;         146 AA.
AC   A0A1I9R3Y6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Oleosin {ECO:0000303|PubMed:27889638, ECO:0000312|EMBL:AOZ15521.1};
OS   Pinus elliottii (Slash pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=42064 {ECO:0000312|EMBL:AOZ15521.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Pollen {ECO:0000303|PubMed:27889638};
RX   PubMed=27889638; DOI=10.1016/j.plaphy.2016.11.010;
RA   Pasaribu B., Chen C.S., Liao Y.K., Jiang P.L., Tzen J.T.C.;
RT   "Identification of caleosin and oleosin in oil bodies of pine pollen.";
RL   Plant Physiol. Biochem. 111:20-29(2017).
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:27889638}.
CC       Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC       Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water
CC       interface. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC       {ECO:0000269|PubMed:27889638}.
CC   -!- DOMAIN: The proline-knot motif may be involved in targeting to lipid
CC       bodies. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KX688796; AOZ15521.1; -; mRNA.
DR   AlphaFoldDB; A0A1I9R3Y6; -.
DR   SMR; A0A1I9R3Y6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:UniProtKB.
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:0000250|UniProtKB:C3S7F0"
FT   CHAIN           2..146
FT                   /note="Oleosin"
FT                   /id="PRO_0000449968"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           55..66
FT                   /note="Proline-knot"
FT                   /evidence="ECO:0000305|PubMed:27889638"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:C3S7F0"
SQ   SEQUENCE   146 AA;  15585 MW;  308DA485FD32A0B7 CRC64;
     MADQYHGVMQ KIHDHTPNPT QILGFITLFV SGAILLLLTG LTLTGTVIGL VVLTPVLIFF
     SPILIPVATV LFVAVAGFLS AGGFGLAALS AISWLYNYIK GRHPPGADQI DYARMRIADT
     ASHVKDYARE YGGYLQSKIQ DAAPGA