PROF1_BETPN
ID PROF1_BETPN Reviewed; 133 AA.
AC P25816;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Profilin-1;
DE AltName: Full=Allergen Bet v II;
DE AltName: Full=Pollen allergen Bet v 2;
DE AltName: Allergen=Bet v 2;
GN Name=BETVII;
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].
RC TISSUE=Pollen;
RX PubMed=1857985; DOI=10.1126/science.1857985;
RA Valenta R., Duchene M., Pettenburger K., Sillaber C., Valent P.,
RA Bettelheim P., Breitenbach M., Rumpold H., Kraft D., Scheiner O.;
RT "Identification of profilin as a novel pollen allergen; IgE autoreactivity
RT in sensitized individuals.";
RL Science 253:557-560(1991).
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 (2.4 ANGSTROMS).
RX PubMed=9016715; DOI=10.1016/s0969-2126(97)00164-0;
RA Fedorov A.A., Ball T., Mahoney N.M., Valenta R., Almo S.C.;
RT "The molecular basis for allergen cross-reactivity: crystal structure and
RT IgE-epitope mapping of birch pollen profilin.";
RL Structure 5:33-45(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9130496; DOI=10.1159/000237520;
RA Fedorov A.A., Ball T., Valenta R., Almo S.C.;
RT "X-ray crystal structures of birch pollen profilin and Phl p 2.";
RL Int. Arch. Allergy Immunol. 113:109-113(1997).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=9271223; DOI=10.1016/s0014-5793(97)00719-9;
RA Domke T., Federau T., Schlueter K., Giehl K., Valenta R., Schomburg D.,
RA Jockusch B.M.;
RT "Birch pollen profilin: structural organization and interaction with poly-
RT (L-proline) peptides as revealed by NMR.";
RL FEBS Lett. 411:291-295(1997).
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 -!- 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; M65179; AAA16522.1; -; mRNA.
DR PIR; JC2082; JC2082.
DR PDB; 1CQA; X-ray; 2.40 A; A=1-133.
DR PDBsum; 1CQA; -.
DR AlphaFoldDB; P25816; -.
DR SMR; P25816; -.
DR Allergome; 127; Bet v 2.
DR Allergome; 3136; Bet v 2.0101.
DR ABCD; P25816; 1 sequenced antibody.
DR EvolutionaryTrace; P25816; -.
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-1"
FT /id="PRO_0000199622"
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"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1CQA"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1CQA"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1CQA"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1CQA"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:1CQA"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:1CQA"
SQ SEQUENCE 133 AA; 14253 MW; 9443FC43786E114A CRC64;
MSWQTYVDEH LMCDIDGQAS NSLASAIVGH DGSVWAQSSS FPQFKPQEIT GIMKDFEEPG
HLAPTGLHLG GIKYMVIQGE AGAVIRGKKG SGGITIKKTG QALVFGIYEE PVTPGQCNMV
VERLGDYLID QGL
