PROF2_HEVBR
ID PROF2_HEVBR Reviewed; 131 AA.
AC Q9STB6;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Profilin-2 {ECO:0000303|PubMed:10955696};
DE AltName: Full=Pollen allergen Hev b 8.0102 {ECO:0000303|PubMed:10955696};
DE AltName: Allergen=Hev b 8.0102 {ECO:0000303|PubMed:10955696};
GN Name=PRO2 {ECO:0000303|PubMed:10955696};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC STRAIN=cv. RRIM 600; TISSUE=Leaf;
RX PubMed=10955696; DOI=10.1034/j.1398-9995.2000.00553.x;
RA Rihs H.-P., Chen Z., Rozynek P., Baur X., Lundberg M., Cremer R.;
RT "PCR-based cloning, isolation, and IgE-binding properties of recombinant
RT latex profilin (rHev b 8).";
RL Allergy 55:712-717(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), DISULFIDE BONDS, AND ALLERGEN.
RX PubMed=27586352; DOI=10.1038/srep32552;
RA Mares-Mejia I., Martinez-Caballero S., Garay-Canales C., Cano-Sanchez P.,
RA Torres-Larios A., Lara-Gonzalez S., Ortega E., Rodriguez-Romero A.;
RT "Structural insights into the IgE mediated responses induced by the
RT allergens Hev b 8 and Zea m 12 in their dimeric forms.";
RL Sci. Rep. 6:32552-32552(2016).
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. {ECO:0000250|UniProtKB:Q9FR39}.
CC -!- SUBUNIT: Multimer (PubMed:27586352). Occurs in many kinds of cells as a
CC complex with monomeric actin in a 1:1 ratio (By similarity).
CC {ECO:0000250|UniProtKB:P35081, ECO:0000269|PubMed:27586352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P35081}.
CC -!- PTM: Phosphorylated by MAP kinases. {ECO:0000250|UniProtKB:P35081}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Involved in latex
CC allergic reactions (PubMed:10955696). Dimerization considerably
CC increases the IgE-mediated degranulation in rat basophilic leukemia
CC cells (PubMed:27586352). {ECO:0000269|PubMed:10955696,
CC ECO:0000269|PubMed:27586352}.
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; AJ132397; CAB51914.1; -; mRNA.
DR PDB; 5FDS; X-ray; 1.90 A; A=1-131.
DR PDB; 5FEG; X-ray; 2.80 A; A/B=1-131.
DR PDBsum; 5FDS; -.
DR PDBsum; 5FEG; -.
DR AlphaFoldDB; Q9STB6; -.
DR SMR; Q9STB6; -.
DR Allergome; 397; Hev b 8.
DR Allergome; 399; Hev b 8.0102.
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 GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
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..131
FT /note="Profilin-2"
FT /id="PRO_0000199634"
FT MOTIF 81..97
FT /note="Involved in PIP2 interaction"
FT /evidence="ECO:0000250|UniProtKB:P35081"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ST99"
FT DISULFID 13..115
FT /evidence="ECO:0000250|UniProtKB:A4GDU3"
FT DISULFID 13
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:27586352,
FT ECO:0007744|PDB:5FEG"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5FDS"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5FDS"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5FEG"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:5FDS"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5FDS"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:5FDS"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:5FDS"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5FDS"
SQ SEQUENCE 131 AA; 14151 MW; 4AC33760CFEDC87D CRC64;
MSWQAYVDDH LMCEIEGNHL SAAAIIGQDG SVWAQSANFP QFKSEEITGI MSDFHEPGTL
APTGLYIGGT KYMVIQGEPG AVIRGKKGPG GVTVKKTNQA LIIGIYDEPM TPGQCNMIVE
RLGDYLIDQG Y
