ID PROFB_OLEEU Reviewed; 134 AA. AC O24170; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 79. DE RecName: Full=Profilin-2; DE AltName: Full=Pollen allergen Ole e 2; DE AltName: Allergen=Ole e 2; GN Name=PRO2; 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 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 -!- 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}. 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; Y12429; CAA73039.1; -; mRNA. DR AlphaFoldDB; O24170; -. DR SMR; O24170; -. 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 Gene3D; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 1. DR InterPro; IPR048278; PFN. DR InterPro; IPR005455; PFN_euk. DR InterPro; IPR036140; PFN_sf. DR InterPro; IPR027310; Profilin_CS. DR PANTHER; PTHR11604; PROFILIN; 1. DR PANTHER; PTHR11604:SF25; PROFILIN-5; 1. DR Pfam; PF00235; Profilin; 1. DR PRINTS; PR00392; PROFILIN. DR PRINTS; PR01640; PROFILINPLNT. DR SMART; SM00392; PROF; 1. DR SUPFAM; SSF55770; Profilin (actin-binding protein); 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_0000199657" 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; 14427 MW; CDCB8C98917DC2DA CRC64; MSWQAYVDDH LMCDIEGHEG HRLTAAAIVG HDGSVWAQSA TFPQFKPEEM NGIMTDFNEP GHLAPTGLHL GGTKYMVIQG EAGAVIRGKK GSGGITIKKT GQALVFGIYE EPVTPGQCNM VVERLGDYLL EQGL //