OL101_ARAHY
ID OL101_ARAHY Reviewed; 169 AA.
AC Q647G5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Oleosin Ara h 10.0101 {ECO:0000305};
DE AltName: Allergen=Ara h 10.0101 {ECO:0000303|PubMed:25860789};
GN ORFNames=Ahy_A06g029932 {ECO:0000312|EMBL:RYR54624.1};
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:AAU21499.2};
RN [1] {ECO:0000312|EMBL:AAU21499.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yan Y., Wang L., Huang S.;
RT "cDNA clone of peanut seed storage protein gene.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABS28870.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li C., Fu G., Zhong Y., Yan Y., Wang L., Huang S.;
RT "Cloning and characterization of four genes encoding peanut seed
RT oleosins.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:RYR54624.1, 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:RYR54624.1};
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 [4]
RP PROTEIN SEQUENCE OF 5-38; 118-131; 134-144 AND 154-168, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, 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 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; AY722694; AAU21499.2; -; mRNA.
DR EMBL; EF695400; ABS28870.1; -; Genomic_DNA.
DR EMBL; SDMP01000006; RYR54624.1; -; Genomic_DNA.
DR AlphaFoldDB; Q647G5; -.
DR SMR; Q647G5; -.
DR STRING; 3818.Q647G5; -.
DR Allergome; 5758; Ara h 10.
DR Allergome; 5759; Ara h 10.0101.
DR Proteomes; UP000289738; Chromosome a06.
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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..169
FT /note="Oleosin Ara h 10.0101"
FT /id="PRO_0000449839"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 146..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 169 AA; 17753 MW; 03F6FC7D9327824F CRC64;
MTDRTQPHTV QVHTTAGRFG DTAAGTNRYP DRGPSTSKVI AVITGLPIGG TLLLFAGLAL
AGTLLGLAVT TPLFILFSPV IVPAIIVVGL SVAGFLTSGA CGLTGLSSFS WVMNYIRQTH
GSVPEQLEMA KHRMADVAGY VGQKTKDVGQ KTKEVGQEIQ TKAQDSKRT