OL142_ARAHY
ID OL142_ARAHY Reviewed; 176 AA.
AC Q9AXI0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Oleosin Ara h 14.0102 {ECO:0000305};
DE AltName: Full=Oleosin 5 variant B {ECO:0000303|PubMed:25860789};
DE AltName: Allergen=Ara h 14.0102 {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:AAK13450.1};
RN [1] {ECO:0000312|EMBL:AAK13450.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 147-156, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND CIRCULAR
RP DICHROISM ANALYSIS.
RC STRAIN=cv. Valencia {ECO:0000303|PubMed:16095908};
RC TISSUE=Seed {ECO:0000303|PubMed:16095908};
RX PubMed=16095908; DOI=10.1016/j.plaphy.2005.06.002;
RA Pons L., Chery C., Mrabet N., Schohn H., Lapicque F., Gueant J.L.;
RT "Purification and cloning of two high molecular mass isoforms of peanut
RT seed oleosin encoded by cDNAs of equal sizes.";
RL Plant Physiol. Biochem. 43:659-668(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-21; 27-43; 129-143 AND 146-156, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT
RP ALA-2, 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 SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALLERGEN.
RX PubMed=12144563; DOI=10.1034/j.1398-9995.57.s72.16.x;
RA Pons L., Chery C., Romano A., Namour F., Artesani M.C., Gueant J.L.;
RT "The 18 kDa peanut oleosin is a candidate allergen for IgE-mediated
RT reactions to peanuts.";
RL Allergy 57:88-93(2002).
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 -!- SUBUNIT: Homodimer. Forms oligomers. {ECO:0000269|PubMed:12144563,
CC ECO:0000269|PubMed:16095908}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:12144563,
CC ECO:0000269|PubMed:16095908, ECO:0000269|PubMed:25860789}. Membrane
CC {ECO:0000255, ECO:0000269|PubMed:12144563}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a
CC monolayer lipid/water interface. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level)
CC (PubMed:16095908, PubMed:25860789, PubMed:12144563). Not expressed in
CC leaves (PubMed:16095908). {ECO:0000269|PubMed:12144563,
CC ECO:0000269|PubMed:16095908, ECO:0000269|PubMed:25860789}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature (78 days post-seedling) and
CC mature seeds. {ECO:0000269|PubMed:16095908}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:25860789,
CC PubMed:12144563). Pooled with Ara h 15 binds to IgE in 75% of the 4
CC peanut-allergic patients tested (PubMed:25860789). Binds to IgE in 36%
CC of the 14 peanut allergic-patients tested. IgE-binding is increased in
CC roasted peanuts compared to fresh peanuts (PubMed:12144563).
CC {ECO:0000269|PubMed:12144563, ECO:0000269|PubMed:25860789}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; AF325918; AAK13450.1; -; mRNA.
DR AlphaFoldDB; Q9AXI0; -.
DR SMR; Q9AXI0; -.
DR Allergome; 11753; Ara h 14.
DR Allergome; 11755; Ara h 14.0102.
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 Acetylation; Allergen; Direct protein sequencing; Lipid droplet; Membrane;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25860789"
FT CHAIN 2..176
FT /note="Oleosin Ara h 14.0102"
FT /id="PRO_0000449844"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 156..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine; alternate"
FT /evidence="ECO:0000269|PubMed:25860789"
FT CONFLICT 149
FT /note="M -> V (in Ref. 1; AAK13450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 18457 MW; EAF6BDC606A82DC7 CRC64;
MATATDRAPH QVQVHTPTTQ RVDVQRRGYD VSGGGVKTFL PDRGPSTSQI IAVLVGVPTG
GTLLLLSGLS LLGTIIGLAI ATPVFTFFSP VIVPAVVTIG LAVIGILTAG ACGLTGLMSL
SWMINFIRQV HGTTVPDQLD SAKRRMADMA DYVGQKTKDA GQEIQTKAQD VKRSSS
