ID   PROF3_PHLPR             Reviewed;         131 AA.
AC   O24282;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Profilin-3;
DE   AltName: Full=Allergen Phl p 11;
DE   AltName: Full=Pollen allergen Phl p 12;
DE   AltName: Allergen=Phl p 12;
GN   Name=PRO3;
OS   Phleum pratense (Common timothy).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poinae;
OC   Phleum.
OX   NCBI_TaxID=15957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pollen;
RX   PubMed=9224949; DOI=10.1016/s0167-4781(97)00061-4;
RA   Asturias J.A., Arilla M.C., Bartolome B., Martinez J., Martinez A.,
RA   Palacios R.;
RT   "Sequence polymorphism and structural analysis of timothy grass pollen
RT   profilin allergen (Phl p 11).";
RL   Biochim. Biophys. Acta 1352:253-257(1997).
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   -!- 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.
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.
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. Binds to IgE.
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; Y09457; CAA70609.1; -; mRNA.
DR   AlphaFoldDB; O24282; -.
DR   SMR; O24282; -.
DR   Allergome; 3417; Phl p 12.0103.
DR   Allergome; 553; Phl p 12.
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..131
FT                   /note="Profilin-3"
FT                   /id="PRO_0000199665"
FT   MOTIF           81..97
FT                   /note="Involved in PIP2 interaction"
FT   MOD_RES         111
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..115
FT                   /evidence="ECO:0000305|PubMed:24146818"
SQ   SEQUENCE   131 AA;  14164 MW;  CD9A319020E0C7C8 CRC64;
     MSWQTYVDEH LMCEIEGHHL ASAAIFGHDG TVWAQSADFP QFKPEEITGI MKDLDEPGHL
     APTGMFVAAA KYMVIQGEPG AVIRGKKGAG GITIKKTGQA LVVGIYDEPM TPGQCNMVVE
     RLGDYLVEQG M