ID   PROFA_OLEEU             Reviewed;         134 AA.
AC   O24169;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Profilin-1;
DE   AltName: Full=Pollen allergen Ole e 2;
DE   AltName: Allergen=Ole e 2;
GN   Name=PRO1;
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 ALLERGEN.
RC   TISSUE=Pollen;
RX   PubMed=9314349; DOI=10.1016/s0091-6749(97)70250-1;
RA   Asturias J.A., Arilla M.C., Gomez-Bayon N., Martinez J., Martinez A.,
RA   Palacios R.;
RT   "Cloning and expression of the panallergen profilin and the major allergen
RT   (Ole e 1) from olive tree pollen.";
RL   J. Allergy Clin. Immunol. 100:365-372(1997).
RN   [2]
RP   POLYMORPHISM.
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   [3]
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).
RN   [4]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=22385802; DOI=10.1016/j.talanta.2012.01.016;
RA   Esteve C., Montealegre C., Marina M.L., Garcia M.C.;
RT   "Analysis of olive allergens.";
RL   Talanta 92:1-14(2012).
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 binding to PIP2, it
CC       inhibits the formation of IP3 and DG (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio.
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       {ECO:0000269|PubMed:9314349}.
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; Y12425; CAA73035.1; -; mRNA.
DR   AlphaFoldDB; O24169; -.
DR   SMR; O24169; -.
DR   Allergome; 3383; Ole e 2.0101.
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   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-1"
FT                   /id="PRO_0000199656"
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;  14489 MW;  6F7B8DD1A246AF6C CRC64;
     MSWQAYVDDH LMCDIEGHED HRLTAAAIVG HDGSVWAQSA TFPQFKPEEM NGIMTDFNEP
     GHLAPTGLHL GGTKYMVIQG EAGAVIRGKK GSGGITIKKT GQALVFGIYE EPVTPGQCNM
     VVERLGDYLV EQGM