ID   PROF1_CORAV             Reviewed;         133 AA.
AC   A4KA39;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Profilin-1;
DE   AltName: Full=Allergen Cor a 2;
DE   AltName: Full=Pollen allergen Cor a 2;
DE   AltName: Allergen=Cor a 2;
OS   Corylus avellana (European hazel) (Corylus maxima).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Corylus.
OX   NCBI_TaxID=13451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RC   STRAIN=cv. Avellana;
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}.
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DR   EMBL; DQ663543; ABG81296.1; -; mRNA.
DR   EMBL; DQ663546; ABG81299.1; -; mRNA.
DR   AlphaFoldDB; A4KA39; -.
DR   SMR; A4KA39; -.
DR   Allergome; 244; Cor a 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..133
FT                   /note="Profilin-1"
FT                   /id="PRO_0000424963"
FT   MOTIF           83..99
FT                   /note="Involved in PIP2 interaction"
FT   MOD_RES         113
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..117
FT                   /evidence="ECO:0000305|PubMed:24146818"
SQ   SEQUENCE   133 AA;  14203 MW;  3293C2841219C67A CRC64;
     MSWQAYVDEH LMCDIDGQGQ QLAASAIVGH DGSVWAQSSS FPQLKPEEIT GIMKDFDEPG
     HLAPTGLHLG GTKYMVIQGE AGAVIRGKKG SGGITIKKTG QALVFGIYEE PVTPGQCNMV
     VERLGDYLLE QGL