OL143_ARAHY
ID OL143_ARAHY Reviewed; 176 AA.
AC Q6J1J8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Oleosin Ara h 14.0103 {ECO:0000305};
DE AltName: Full=Oleosin 5 {ECO:0000303|PubMed:25860789, ECO:0000312|EMBL:ABC96763.1};
DE AltName: Allergen=Ara h 14.0103 {ECO:0000305};
GN ORFNames=Ahy_A05g023475 {ECO:0000312|EMBL:RYR57768.1};
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:AAT11925.1};
RN [1] {ECO:0000312|EMBL:AAT11925.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schocker F., Poeppelmann M., Becker W.M.;
RT "Clinical characterization of a peanut oleosin isoform.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABC96763.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhong Y.J., Yan Y.S., Wang L., Lin X.D., Zhang Y.S., Fu G.H., Huang S.Z.;
RT "Isolation of genes encoding peanut seed protein.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:ABS28871.1}
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 [4] {ECO:0000312|EMBL:RYR57768.1, 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:RYR57768.1};
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 [5]
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).
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:25860789}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Pooled with Ara h 15
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.
CC {ECO:0000255|RuleBase:RU000540}.
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DR EMBL; AY605694; AAT11925.1; -; Genomic_DNA.
DR EMBL; DQ368496; ABC96763.1; -; mRNA.
DR EMBL; EF695401; ABS28871.1; -; Genomic_DNA.
DR EMBL; SDMP01000005; RYR57768.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6J1J8; -.
DR SMR; Q6J1J8; -.
DR STRING; 3818.Q6J1J8; -.
DR Allergome; 11753; Ara h 14.
DR Allergome; 11756; Ara h 14.0103.
DR Proteomes; UP000289738; Chromosome a05.
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.
DR PROSITE; PS00811; OLEOSINS; 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..176
FT /note="Oleosin Ara h 14.0103"
FT /id="PRO_0000449845"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
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"
SQ SEQUENCE 176 AA; 18448 MW; 191FEFE4BACB3894 CRC64;
MATATDRAPH QVQVHTPTTQ RVDVPRRGYD VSGGGIKTLL PERGPSTSQI IAVLVGVPTG
GTLLLLSGLS LLGTIIGLAI ATPVFIFFSP VIVPAVVTIG LAVTGILTAG ACGLTGLMSL
SWMINFIRQV HGTTVPDQLD SVKRRMADMA DYVGQKTKDA GQEIQTKAQD VKRSSS