ID   PROAQ_OLEEU             Reviewed;         134 AA.
AC   P0DKF8; A4GDQ9;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Profilin-2;
DE   AltName: Full=Pollen allergen Ole e 2;
DE   AltName: Allergen=Ole e 2;
OS   Olea europaea (Common olive).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Oleaceae; Oleeae; Olea.
OX   NCBI_TaxID=4146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zard;
RA   Soleimani A., Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.;
RT   "Isoforms of pollen allergens in two widespread olive cultivars from
RT   Iran.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC       At high concentrations, profilin prevents the polymerization of actin,
CC       whereas it enhances it at low concentrations (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- PTM: Phosphorylated by MAP kinases. {ECO:0000250}.
CC   -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC       polymorphism.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF541374; ABP58620.1; -; mRNA.
DR   EMBL; EF541376; ABP58622.1; -; mRNA.
DR   AlphaFoldDB; P0DKF8; -.
DR   SMR; P0DKF8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd00148; PROF; 1.
DR   InterPro; IPR005455; PFN.
DR   InterPro; IPR036140; PFN_sf.
DR   InterPro; IPR027310; Profilin_CS.
DR   PANTHER; PTHR11604; PTHR11604; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   PRINTS; PR00392; PROFILIN.
DR   PRINTS; PR01640; PROFILINPLNT.
DR   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
DR   PROSITE; PS00414; PROFILIN; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Allergen; Cytoplasm; Cytoskeleton; Disulfide bond;
KW   Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..134
FT                   /note="Profilin-2"
FT                   /id="PRO_0000425008"
FT   MOTIF           84..100
FT                   /note="Involved in PIP2 interaction"
FT   MOD_RES         114
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..118
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   134 AA;  14413 MW;  8CC7FD84E42D97C6 CRC64;
     MSWQTYVDDH LMCDIEGHEG HRLTAAAIVG HDGSVWAQSA TFPQFKPEEM NGIMTDFNEP
     GHLAPTGLHL GGTKYMVIQG EAGAVIRGKK GSGGITIKKT GQALVCGIYE EPVTPGQCNM
     VVERLGDYLL EQGL