ID   PROF2_BETPN             Reviewed;         133 AA.
AC   A4K9Z8;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Profilin-2;
DE   AltName: Full=Allergen Bet v II;
DE   AltName: Full=Pollen allergen Bet v 2;
DE   AltName: Allergen=Bet v 2;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RC   STRAIN=cv. Laciniata;
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-133, AND DISULFIDE BOND.
RX   PubMed=29035299; DOI=10.3390/ijms18102156;
RA   Soh W.T., Briza P., Dall E., Asam C., Schubert M., Huber S., Aglas L.,
RA   Bohle B., Ferreira F., Brandstetter H.;
RT   "Two distinct conformations in Bet v 2 determine its proteolytic resistance
RT   to cathepsin S.";
RL   Int. J. Mol. Sci. 18:0-0(2017).
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. {ECO:0000269|PubMed:22348028}.
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; DQ650633; ABG48509.1; -; mRNA.
DR   PDB; 5NZB; X-ray; 1.70 A; A=2-133.
DR   PDB; 5NZC; X-ray; 2.00 A; A/B=2-133.
DR   PDBsum; 5NZB; -.
DR   PDBsum; 5NZC; -.
DR   AlphaFoldDB; A4K9Z8; -.
DR   SMR; A4K9Z8; -.
DR   Allergome; 127; Bet v 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   3D-structure; Actin-binding; Allergen; Cytoplasm; Cytoskeleton;
KW   Disulfide bond; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..133
FT                   /note="Profilin-2"
FT                   /id="PRO_0000424962"
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:0000269|PubMed:29035299,
FT                   ECO:0000305|PubMed:24146818, ECO:0007744|PDB:5NZB"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          23..29
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   TURN            59..65
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          72..80
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   STRAND          100..108
FT                   /evidence="ECO:0007829|PDB:5NZB"
FT   HELIX           114..130
FT                   /evidence="ECO:0007829|PDB:5NZB"
SQ   SEQUENCE   133 AA;  14278 MW;  50E3A0EA509A9261 CRC64;
     MSWQTYVDEH LMCDIDGQGQ QLAASAIVGH DGSVWAQSSS FPQFKPQEIT GIMKDFEEPG
     HLAPTGLHLG GIKYMVIQGE AGAVIRGKKG SGGITIKKTG QALVFGIYEE PVTPGQCNMV
     VERLGDYLID QGL