ID   OL111_ARAHY             Reviewed;         137 AA.
AC   Q45W87;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Oleosin Ara h 11.0101 {ECO:0000305};
DE   AltName: Allergen=Ara h 11.0101 {ECO:0000303|PubMed:25860789};
GN   ORFNames=Ahy_B10g105758 {ECO:0000312|EMBL:RYQ86093.1};
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:AAZ20276.1};
RN   [1] {ECO:0000312|EMBL:AAZ20276.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed {ECO:0000312|EMBL:AAZ20276.1};
RA   Yan Y.S., Wang L., Huang S.Z.;
RT   "Isolation of genes encoding peanut seed protein.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:RYQ86093.1, ECO:0000312|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000312|Proteomes:UP000289738};
RC   TISSUE=Leaf {ECO:0000312|EMBL:RYQ86093.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-10; 102-113 AND 122-137, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT ALA-2, AND
RP   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 10
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; DQ097716; AAZ20276.1; -; mRNA.
DR   EMBL; SDMP01000020; RYQ86093.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q45W87; -.
DR   SMR; Q45W87; -.
DR   STRING; 3818.Q45W87; -.
DR   Allergome; 5760; Ara h 11.
DR   Allergome; 5761; Ara h 11.0101.
DR   Proteomes; UP000289738; Chromosome b10.
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   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25860789"
FT   CHAIN           2..137
FT                   /note="Oleosin Ara h 11.0101"
FT                   /id="PRO_0000449841"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; alternate"
FT                   /evidence="ECO:0000269|PubMed:25860789"
SQ   SEQUENCE   137 AA;  14308 MW;  8C470857182A3372 CRC64;
     MAEALYYGGR QRQEQPRSTQ LVKATTAVVA GGSLLILAGL VLAGTVIGLT TITPLFVIFS
     PVLVPAVITV ALLGLGFLAS GGFGVAAITV LTWIYRYVTG KHPPGANQLD TARHKLMGKA
     REIKDFGQQQ TSGAQAS