OLEL_SESIN
ID OLEL_SESIN Reviewed; 145 AA.
AC Q9XHP2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Oleosin L {ECO:0000303|PubMed:12450125};
DE AltName: Full=Allergen Ses i 5 {ECO:0000303|PubMed:16436145};
DE AltName: Full=Oleosin 15 kDa {ECO:0000303|PubMed:12450125, ECO:0000303|PubMed:16436145};
DE AltName: Allergen=Ses i 5.0101 {ECO:0000305};
OS Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=4182 {ECO:0000312|EMBL:AAD42942.1};
RN [1] {ECO:0000312|EMBL:AAD42942.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Tainan 1 {ECO:0000312|EMBL:AAD42942.1};
RC TISSUE=Seed {ECO:0000303|PubMed:12450125};
RX PubMed=12450125; DOI=10.1271/bbb.66.2146;
RA Tai S.S., Chen M.C., Peng C.C., Tzen J.T.;
RT "Gene family of oleosin isoforms and their structural stabilization in
RT sesame seed oil bodies.";
RL Biosci. Biotechnol. Biochem. 66:2146-2153(2002).
RN [2] {ECO:0000312|EMBL:ACH85187.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA He F., Wu Y., Liu Z.;
RT "Molecular cloning, expression and identification of the main allergen 15
RT kda oleosin in white sesame.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=16436145; DOI=10.1111/j.1398-9995.2006.01013.x;
RA Leduc V., Moneret-Vautrin D.A., Tzen J.T., Morisset M., Guerin L.,
RA Kanny G.;
RT "Identification of oleosins as major allergens in sesame seed allergic
RT patients.";
RL Allergy 61:349-356(2006).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000255|RuleBase:RU000540,
CC ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:16436145}. Membrane
CC {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein
CC {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins
CC exist at a monolayer lipid/water interface. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC {ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:16436145}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation. Expressed in
CC maturing seeds about 1 and half weeks after flowering. Expression
CC continues steadily thereafter until it decreases in the seed-drying
CC stage, reaching undetectable levels in mature seeds.
CC {ECO:0000269|PubMed:12450125}.
CC -!- DOMAIN: The proline-knot motif may be involved in the targeting to oil
CC bodies. {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in all of
CC the 32 patients tested allergic to sesame seeds.
CC {ECO:0000269|PubMed:16436145}.
CC -!- SIMILARITY: Belongs to the oleosin family.
CC {ECO:0000255|RuleBase:RU000540}.
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DR EMBL; AF091840; AAD42942.1; -; mRNA.
DR EMBL; EU999158; ACH85187.1; -; mRNA.
DR AlphaFoldDB; Q9XHP2; -.
DR Allergome; 1441; Ses i 5.
DR Allergome; 3475; Ses i 5.0101.
DR EnsemblPlants; SIN_1016733.t; SIN_1016733.t.cds1; SIN_1016733.
DR Gramene; SIN_1016733.t; SIN_1016733.t.cds1; SIN_1016733.
DR Proteomes; UP000504604; Genome assembly.
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 GO; GO:0034389; P:lipid droplet organization; IC:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IC:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
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; Allergen; Lipid droplet; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:C3S7F0"
FT CHAIN 2..145
FT /note="Oleosin L"
FT /id="PRO_0000449966"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 123..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..69
FT /note="Proline-knot"
FT /evidence="ECO:0000305|PubMed:12450125"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:C3S7F0"
SQ SEQUENCE 145 AA; 15194 MW; 489F7DEA029E7A3D CRC64;
MAEHYGQQQQ TRAPHLQLQP RAQRVVKAAT AVTAGGSLLV LSGLTLAGTV IALTIATPLL
VIFSPVLVPA VITIFLLGAG FLASGGFGVA ALSVLSWIYR YLTGKHPPGA DQLESAKTKL
ASKAREMKDR AEQFSQQPVA GSQTS
