ID   PROFE_OLEEU             Reviewed;         134 AA.
AC   A4GCR5;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
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], AND POLYMORPHISM.
RC   STRAIN=cv. Lechin de Sevilla; TISSUE=Pollen;
RX   PubMed=22348028; DOI=10.1371/journal.pone.0030878;
RA   Jimenez-Lopez J.C., Morales S., Castro A.J., Volkmann D.,
RA   Rodriguez-Garcia M.I., Alche Jde D.;
RT   "Characterization of profilin polymorphism in pollen with a focus on
RT   multifunctionality.";
RL   PLoS ONE 7:E30878-E30878(2012).
RN   [2]
RP   3D-STRUCTURE MODELING, AND DISULFIDE BOND.
RX   PubMed=24146818; DOI=10.1371/journal.pone.0076066;
RA   Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.D.;
RT   "Analysis of the effects of polymorphism on pollen profilin structural
RT   functionality and the generation of conformational, T- and B-cell
RT   epitopes.";
RL   PLoS ONE 8:E76066-E76066(2013).
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   -!- MISCELLANEOUS: The variability of the residues taking part of IgE-
CC       binding epitopes might be responsible of the difference in cross-
CC       reactivity among olive pollen cultivars, and between distantly related
CC       pollen species, leading to a variable range of allergy reactions among
CC       atopic patients. {ECO:0000305|PubMed:24146818}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; DQ061976; AAZ08564.1; -; mRNA.
DR   AlphaFoldDB; A4GCR5; -.
DR   SMR; A4GCR5; -.
DR   Allergome; 490; Ole e 2.
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   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.
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_0000424970"
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|PubMed:24146818"
SQ   SEQUENCE   134 AA;  14453 MW;  CDCB943B9B4ED04A CRC64;
     MLWQAYVDDH LMCDIEGHEG HRLTAAAIVG HDGSVWAQSA TFPQFKPEEM NGIMTDFNEP
     GHLAPTGLHL GGTKYMVIQG EAGAVIRGKK GSGGITIKKT GQALVFGIYE EPVTPGQCNM
     VVERLGDYLL EQGL