ID   OLE12_CORAV             Reviewed;         159 AA.
AC   Q84T21;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Oleosin Cor a 12 {ECO:0000303|PubMed:34146442};
DE   AltName: Allergen=Cor a 12 {ECO:0000303|PubMed:34146442};
OS   Corylus avellana (European hazel) (Corylus maxima).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Corylus.
OX   NCBI_TaxID=13451 {ECO:0000312|EMBL:AAO67349.2};
RN   [1] {ECO:0000312|EMBL:AAO67349.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16288502; DOI=10.1002/mnfr.200500147;
RA   Akkerdaas J.H., Schocker F., Vieths S., Versteeg S., Zuidmeer L.,
RA   Hefle S.L., Aalberse R.C., Richter K., Ferreira F., van Ree R.;
RT   "Cloning of oleosin, a putative new hazelnut allergen, using a hazelnut
RT   cDNA library.";
RL   Mol. Nutr. Food Res. 50:18-23(2006).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=34146442; DOI=10.1111/pai.13579;
RA   Nebbia S., Lamberti C., Cirrincione S., Acquadro A., Abba S., Ciuffo M.,
RA   Torello Marinoni D., Manfredi M., Marengo E., Calzedda R., Monti G.,
RA   Cavallarin L., Giuffrida M.G.;
RT   "Oleosin Cor a 15 is a novel allergen for Italian hazelnut allergic
RT   children.";
RL   Pediatr. Allergy Immunol. 32:1743-1755(2021).
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:0000250|UniProtKB:O04925}.
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. {ECO:0000269|PubMed:16288502}.
CC   -!- MASS SPECTROMETRY: Mass=14000; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:34146442};
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:34146442). Binds
CC       to IgE of patients allergic to hazelnuts (PubMed:34146442).
CC       {ECO:0000269|PubMed:34146442}.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; AY224679; AAO67349.2; -; mRNA.
DR   Allergome; 2819; Cor a 12.
DR   Allergome; 5764; Cor a 12.0101.
DR   EnsemblPlants; Cav05g23730.t1; Cav05g23730.t1.cds1; Cav05g23730.
DR   Gramene; Cav05g23730.t1; Cav05g23730.t1.cds1; Cav05g23730.
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; Lipid droplet; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..159
FT                   /note="Oleosin Cor a 12"
FT                   /id="PRO_0000456211"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   159 AA;  16698 MW;  9D2224B496584A27 CRC64;
     MADRPQQLQV HPQRGHGHYE GGIKNQRGGG PSAVKVMAVL AALPVGGTLL ALAGLTLAGS
     VIGLLVTSPL FIIFSPVLVP AAIVVGLAVA SFLSSGALGL TGLSSLSWVL NYLRCASQSL
     PREMDQAKRR MQDMAAFVGQ KTREVGQEIQ SRAQEGRRT