ID   OL102_ARAHY             Reviewed;         150 AA.
AC   Q647G4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Oleosin Ara h 10.0102 {ECO:0000305};
DE   AltName: Allergen=Ara h 10.0102 {ECO:0000303|PubMed:25860789};
DE   Flags: Fragment;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000312|EMBL:AAU21500.1};
RN   [1] {ECO:0000312|EMBL:AAU21500.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yan Y., Wang L., Huang S.;
RT   "cDNA clone of peanut seed storage protein gene.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 19-28; 118-131 AND 134-144, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RC   TISSUE=Seed {ECO:0000303|PubMed:25860789};
RX   PubMed=25860789; DOI=10.1371/journal.pone.0123419;
RA   Schwager C., Kull S., Krause S., Schocker F., Petersen A., Becker W.M.,
RA   Jappe U.;
RT   "Development of a novel strategy to isolate lipophilic allergens (oleosins)
RT   from peanuts.";
RL   PLoS ONE 10:E0123419-E0123419(2015).
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:0000269|PubMed:25860789}.
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 seeds (at protein level).
CC       {ECO:0000269|PubMed:25860789}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Pooled with Ara h 11
CC       binds to IgE in 75% of the 4 peanut-allergic patients tested.
CC       {ECO:0000269|PubMed:25860789}.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; AY722695; AAU21500.1; -; mRNA.
DR   AlphaFoldDB; Q647G4; -.
DR   Allergome; 5758; Ara h 10.
DR   Allergome; 5872; Ara h 10.0102.
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   Allergen; Direct protein sequencing; Lipid droplet; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..>150
FT                   /note="Oleosin Ara h 10.0102"
FT                   /id="PRO_0000449840"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         150
FT                   /evidence="ECO:0000312|EMBL:AAU21500.1"
SQ   SEQUENCE   150 AA;  15527 MW;  D3051FFA53CC7158 CRC64;
     MTDRTQPHAV QVHTTAGRFG DTAAGTNRYA DRGPSTSKVI AVITGLPIGG TLLLFAGLAL
     AGTLLGLAVT TPLFILFSPV IVPATIVVGL SVAGFLTSGA CGLTGLSSFS WVMNYIRQTH
     GSVPEQLEMA KHRMADVAGY VGQKTKDVGQ