ID   PROF2_SOYBN             Reviewed;         131 AA.
AC   O65810;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Profilin-2;
DE   AltName: Full=GmPRO2;
DE   AltName: Allergen=Gly m 3.0102;
GN   Name=PRO2;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=10589015; DOI=10.1016/s0091-6749(99)70027-8;
RA   Rihs H.-P., Chen Z., Rueff F., Petersen A., Rozynek P., Heimann H.,
RA   Baur X.;
RT   "IgE binding of the recombinant allergen soybean profilin (rGly m 3) is
RT   mediated by conformational epitopes.";
RL   J. Allergy Clin. Immunol. 104:1293-1301(1999).
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.
CC       {ECO:0000269|PubMed:10589015}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AJ223981; CAA11755.1; -; mRNA.
DR   PIR; T07773; T07773.
DR   RefSeq; NP_001236192.1; NM_001249263.1.
DR   AlphaFoldDB; O65810; -.
DR   SMR; O65810; -.
DR   STRING; 3847.O65810; -.
DR   Allergome; 372; Gly m 3.
DR   Allergome; 374; Gly m 3.0102.
DR   GeneID; 547670; -.
DR   KEGG; gmx:547670; -.
DR   InParanoid; O65810; -.
DR   OrthoDB; 2965090at2759; -.
DR   Proteomes; UP000008827; Unplaced.
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   Gene3D; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 1.
DR   InterPro; IPR048278; PFN.
DR   InterPro; IPR005455; PFN_euk.
DR   InterPro; IPR036140; PFN_sf.
DR   InterPro; IPR027310; Profilin_CS.
DR   PANTHER; PTHR11604; PROFILIN; 1.
DR   PANTHER; PTHR11604:SF78; PROFILIN LP04; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   PRINTS; PR00392; PROFILIN.
DR   PRINTS; PR01640; PROFILINPLNT.
DR   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; Profilin (actin-binding protein); 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_0000199673"
SQ   SEQUENCE   131 AA;  14100 MW;  AE9B9517AE9166BE CRC64;
     MSWQAYVDDH LLCGIEGNHL THAAIIGQDG SVWLQSTDFP QFKPEEITAI MNDFNEPGSL
     APTGLYLGGT KYMVIQGEPG AVIRGKKGPG GVTVKKTGAA LIIGIYDEPM TPGQCNMVVE
     RLGDYLIDQG Y
//