ID   PROF3_MAIZE             Reviewed;         131 AA.
AC   P35083;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Profilin-3;
DE   AltName: Full=Pollen allergen Zea m 12;
DE   AltName: Full=ZmPRO3;
DE   AltName: Allergen=Zea m 12;
GN   Name=PRO3; Synonyms=PRF3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A188; TISSUE=Pollen;
RX   PubMed=8252067; DOI=10.1046/j.1365-313x.1993.04040631.x;
RA   Staiger C.J., Goodbody K.C., Hussey P.J., Valenta R., Droebak B.K.,
RA   Lloyd C.W.;
RT   "The profilin multigene family of maize: differential expression of three
RT   isoforms.";
RL   Plant J. 4:631-641(1993).
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).
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   -!- TISSUE SPECIFICITY: Pollen specific.
CC   -!- PTM: Phosphorylated by MAP kinases. {ECO:0000250}.
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; X73281; CAA51720.1; -; mRNA.
DR   PIR; S35798; S35798.
DR   RefSeq; NP_001105452.1; NM_001111982.1.
DR   AlphaFoldDB; P35083; -.
DR   SMR; P35083; -.
DR   STRING; 4577.GRMZM5G876285_P01; -.
DR   Allergome; 3532; Zea m 12.0103.
DR   Allergome; 682; Zea m 12.
DR   PaxDb; P35083; -.
DR   EnsemblPlants; Zm00001eb371230_T001; Zm00001eb371230_P001; Zm00001eb371230.
DR   GeneID; 542411; -.
DR   Gramene; Zm00001eb371230_T001; Zm00001eb371230_P001; Zm00001eb371230.
DR   KEGG; zma:542411; -.
DR   MaizeGDB; 78604; -.
DR   eggNOG; KOG1755; Eukaryota.
DR   OMA; KPAEMAN; -.
DR   OrthoDB; 1428600at2759; -.
DR   Proteomes; UP000007305; Chromosome 8.
DR   ExpressionAtlas; P35083; baseline and differential.
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; IDA:AgBase.
DR   GO; GO:0070064; F:proline-rich region binding; IDA:AgBase.
DR   GO; GO:0007097; P:nuclear migration; IDA:AgBase.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:AgBase.
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; Disulfide bond;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Profilin-3"
FT                   /id="PRO_0000199648"
FT   MOTIF           81..97
FT                   /note="Involved in PIP2 interaction"
FT   MOD_RES         111
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..115
FT                   /evidence="ECO:0000305|PubMed:24146818"
SQ   SEQUENCE   131 AA;  14237 MW;  A746F90BFA9B8386 CRC64;
     MSWQTYVDEH LMCEIEGHHL SSAAIVGHDG AVWAQSTAFP QFKPEEMTNI IKDFDEPGFL
     APIGLFLGPT KYMVIQGEPG AVIRGKKGSG GITVKKTGQA LVIGIYDEPM TPGQCNMVVE
     RLGDYLVEQG L