ID   PROF2_TOBAC             Reviewed;         134 AA.
AC   Q9ST99;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Profilin-2;
DE   AltName: Full=Pollen allergen Nic t 8;
DE   AltName: Allergen=Nic t 8;
GN   Name=PRO2;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Petit Havana; TISSUE=Pollen;
RX   AGRICOLA=IND20526767;
RA   Mittermann I., Heiss S., Dietrich K., Valenta R., Heberle-Bors E.;
RT   "Molecular characterisation of profilin isoforms from tobacco (Nicotiana
RT   tabacum) pollen.";
RL   Sex. Plant Reprod. 9:133-139(1996).
RN   [2]
RP   PHOSPHORYLATION AT THR-114, AND MUTAGENESIS OF THR-114.
RX   PubMed=15465030; DOI=10.1016/j.bbrc.2004.09.071;
RA   Limmongkon A., Giuliani C., Valenta R., Mittermann I., Heberle-Bors E.,
RA   Wilson C.;
RT   "MAP kinase phosphorylation of plant profilin.";
RL   Biochem. Biophys. Res. Commun. 324:382-386(2004).
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   -!- PTM: Phosphorylated by MAP kinases. {ECO:0000269|PubMed:15465030}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; X93465; CAA63751.1; -; mRNA.
DR   AlphaFoldDB; Q9ST99; -.
DR   SMR; Q9ST99; -.
DR   Allergome; 1407; Nic t 8.
DR   iPTMnet; Q9ST99; -.
DR   Proteomes; UP000084051; 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   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; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..134
FT                   /note="Profilin-2"
FT                   /id="PRO_0000199675"
FT   MOD_RES         114
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:15465030"
FT   MUTAGEN         114
FT                   /note="T->A: Loss of phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:15465030"
SQ   SEQUENCE   134 AA;  14489 MW;  B05615420DBDF21E CRC64;
     MSWQTYVDDH LMADIEGQQG NHLAAAAILG NDGSVWAQST TFPKFKPEEI TNIMKDFDEP
     GHLAPTGLFL GGAKYMVIQG EPGAVIRGKK GSGGITIKKT NQALIFGIYE EPVTPGQCNM
     VVEKIGDYLV DQGY