OL141_ARAHY
ID OL141_ARAHY Reviewed; 176 AA.
AC Q9AXI1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Oleosin Ara h 14.0101 {ECO:0000305};
DE AltName: Full=Oleosin 5 variant A {ECO:0000303|PubMed:25860789};
DE AltName: Allergen=Ara h 14.0101 {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:AAK13449.1};
RN [1] {ECO:0000312|EMBL:AAK13449.1}
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, however two of these
CC patients IgE bind only weakly. IgE-binding is increased in roasted
CC 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; AF325917; AAK13449.1; -; mRNA.
DR AlphaFoldDB; Q9AXI1; -.
DR SMR; Q9AXI1; -.
DR Allergome; 11753; Ara h 14.
DR Allergome; 11754; Ara h 14.0101.
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 14.0101"
FT /id="PRO_0000449843"
FT TRANSMEM 50..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..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; AAK13449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 18435 MW; A7EFF329A60BB188 CRC64;
MATATDRAPH QVQVHTPTTQ RVDVPRRGYD VSGGGIKTLL PERGPSTSQI IAVLVGVPTG
GTLLLLSGLS LLGTIIGLAI ATPVFTFFSP VIVPAVVTIG LAVTGILTAG ACGLTGLMSL
SWMINFIRQV HGTTVPDQLD SVKRRMADMA DYVGQKTKDA GQQIQTKAQD VKRSSS
