PROF2_SOLLC
ID PROF2_SOLLC Reviewed; 131 AA.
AC Q93YG7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Profilin-2;
DE AltName: Full=Minor food allergen Lyc e 1;
DE AltName: Allergen=Lyc e 1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Fruit;
RX PubMed=12915767; DOI=10.1159/000072136;
RA Willerroider M., Fuchs H., Ballmer-Weber B., Focke M., Susani M.,
RA Thalhamer J., Ferreira F., Wuethrich B., Scheiner O., Breiteneder H.,
RA Hoffman-Sommergruber K.;
RT "Cloning and molecular and immunological characterization of two new food
RT allergens, Cap a 2 and Lyc e 1, profilins from bell pepper (Capsicum
RT annuum) and Tomato (Lycopersicon esculentum).";
RL Int. Arch. Allergy Immunol. 131:245-255(2003).
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. This is a
CC food allergen. {ECO:0000269|PubMed:12915767}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AJ417553; CAD10377.1; -; mRNA.
DR RefSeq; NP_001233973.1; NM_001247044.3.
DR AlphaFoldDB; Q93YG7; -.
DR SMR; Q93YG7; -.
DR STRING; 4081.Solyc08g066110.2.1; -.
DR Allergome; 3358; Sola l 1.0101.
DR Allergome; 703; Sola l 1.
DR PaxDb; Q93YG7; -.
DR PRIDE; Q93YG7; -.
DR EnsemblPlants; Solyc08g066110.3.1; Solyc08g066110.3.1; Solyc08g066110.3.
DR GeneID; 543782; -.
DR Gramene; Solyc08g066110.3.1; Solyc08g066110.3.1; Solyc08g066110.3.
DR KEGG; sly:543782; -.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR InParanoid; Q93YG7; -.
DR OMA; WAQSSGF; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q93YG7; -.
DR Proteomes; UP000004994; Chromosome 8.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..131
FT /note="Profilin-2"
FT /id="PRO_0000199645"
SQ SEQUENCE 131 AA; 14257 MW; E55E464A0E1168D2 CRC64;
MSWQTYVDEH LLCENEGNHL TSAAIIGQDG TVWAQSANFP QFKPEEITGI MNDFAVPGTL
APTGLYLGGT KYMVIQGEPE AVIRGKKGPG GITIKKTNQA LIIGIYDEPM TPGQCNMIVE
RLGDYLIEQS L