PROFP_OLEEU
ID PROFP_OLEEU Reviewed; 134 AA.
AC A4GCR7;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Profilin-4;
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 -!- 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 -!- 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; DQ061978; AAZ08566.1; -; mRNA.
DR AlphaFoldDB; A4GCR7; -.
DR SMR; A4GCR7; -.
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-4"
FT /id="PRO_0000424981"
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; 14455 MW; 0CFAAEC393D6B0A9 CRC64;
MSWQAYVDDH LMCDIEGHED HRLTAAAIVG HDGSVWAQSA TFPQFKPVEM NGIMTDFNEP
GHLAPTGLHL GGTKYMVIQG EAGAVIRGKK GSGGITIKKT GQALVFGIYE EPVTPGQCNM
VVERLGDYLI EQGL