OLE15_ARAHY
ID OLE15_ARAHY Reviewed; 166 AA.
AC Q647G3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Oleosin Ara h 15.0101 {ECO:0000305};
DE AltName: Full=Oleosin 3 {ECO:0000303|PubMed:22790944, ECO:0000303|PubMed:25860789, ECO:0000312|EMBL:AAU21501.1};
DE AltName: Allergen=Ara h 15.0101 {ECO:0000305};
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:AAU21501.1};
RN [1] {ECO:0000312|EMBL:AAU21501.1}
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 2-10; 7-42; 125-136 AND 145-158, 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).
RN [3]
RP PROTEIN SEQUENCE OF 2-9, TISSUE SPECIFICITY, ALLERGEN, REGION, AND
RP ACETYLATION AT SER-2.
RC TISSUE=Seed {ECO:0000303|PubMed:22790944};
RX PubMed=22790944; DOI=10.1271/bbb.120063;
RA Kobayashi S., Katsuyama S., Wagatsuma T., Okada S., Tanabe S.;
RT "Identification of a new IgE-binding epitope of peanut oleosin that cross-
RT reacts with buckwheat.";
RL Biosci. Biotechnol. Biochem. 76:1182-1188(2012).
RN [4]
RP TISSUE SPECIFICITY, ALLERGEN, AND REGION.
RX PubMed=28342912; DOI=10.1016/j.jaci.2017.02.020;
RA Schwager C., Kull S., Behrends J., Roeckendorf N., Schocker F., Frey A.,
RA Homann A., Becker W.M., Jappe U.;
RT "Peanut oleosins associated with severe peanut allergy-importance of
RT lipophilic allergens for comprehensive allergy diagnostics.";
RL J. Allergy Clin. Immunol. 140:1331-1338(2017).
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:25860789}. Membrane {ECO:0000255|RuleBase:RU000540};
CC Multi-pass membrane protein {ECO:0000255|RuleBase:RU000540}.
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:22790944, ECO:0000269|PubMed:25860789,
CC ECO:0000269|PubMed:28342912}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:25860789,
CC PubMed:22790944, PubMed:28342912). Pooled with Ara h 14 binds to IgE in
CC 75% of the 4 peanut-allergic patients tested (PubMed:25860789). Binds
CC to IgE in all of the 8 peanut-allergic patients tested
CC (PubMed:22790944). Protein obtained from roasted peanuts pooled with
CC Ara h 14 binds to IgE in 97% of the 35 patients with severe peanut-
CC allergy tested, but does not bind to IgE from patients with only mild
CC allergy to peanuts. IgE-binding to this protein obtained from raw
CC peanuts is notably decreased or almost undetectable in patients with
CC severe peanut-allergy. Induces degranulation of human basophils
CC (PubMed:28342912). {ECO:0000269|PubMed:22790944,
CC ECO:0000269|PubMed:25860789, ECO:0000269|PubMed:28342912}.
CC -!- SIMILARITY: Belongs to the oleosin family.
CC {ECO:0000255|RuleBase:RU000540}.
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DR EMBL; AY722696; AAU21501.1; -; mRNA.
DR AlphaFoldDB; Q647G3; -.
DR Allergome; 11757; Ara h 15.0101.
DR Allergome; 913; Ara h 15.
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:0019863; F:IgE binding; IEA:UniProtKB-KW.
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 Acetylation; Allergen; Direct protein sequencing; IgE-binding protein;
KW Lipid droplet; Membrane; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22790944,
FT ECO:0000269|PubMed:25860789"
FT CHAIN 2..166
FT /note="Oleosin Ara h 15.0101"
FT /id="PRO_0000449846"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 2..9
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:22790944"
FT REGION 141..155
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:28342912"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:22790944"
SQ SEQUENCE 166 AA; 16875 MW; 2AFE873BCCB2F18B CRC64;
MSDQTRTGYG GGGSYGSSYG GGGTYGSSYG TSYDPSTNQP IRQAIKFMTA STIGVSFLIL
SGLILTGTVI GLIIATPLLV IFSPILVPAA ITLALAAGGF LFSGGCGVAA IAALSWLYSY
VTGKHPAGSD RLDYAKGVIA DKARDVKDRA KDYAGAGRAQ EGTPGY
