ID   PROF1_MAIZE             Reviewed;         131 AA.
AC   P35081;
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-1;
DE   AltName: Full=Pollen allergen Zea m 12;
DE   AltName: Full=ZmPRO1;
DE   AltName: Allergen=Zea m 12;
GN   Name=PRO1; Synonyms=PRF1;
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   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. B73; TISSUE=Pollen {ECO:0000303|PubMed:8252067};
RX   PubMed=10760246; DOI=10.2307/3871071;
RA   Kovar D.R., Droebak B.K., Staiger C.J.;
RT   "Maize profilin isoforms are functionally distinct.";
RL   Plant Cell 12:583-598(2000).
RN   [3]
RP   ALLERGEN, AND SUBUNIT.
RX   DOI=10.1046/j.1440-1592.2000.00155.x;
RA   Psaradellis T., Kao N.L., Babich M.;
RT   "Recombinant Zea mays profilin forms multimers with pan-allergenic
RT   potential.";
RL   Allergol. Int. 49:27-35(2000).
RN   [4]
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. {ECO:0000269|PubMed:10760246}.
CC   -!- SUBUNIT: Multimer. Occurs in many kinds of cells as a complex with
CC       monomeric actin in a 1:1 ratio. {ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:10760246}.
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. {ECO:0000269|Ref.3}.
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; X73279; CAA51718.1; -; mRNA.
DR   PIR; S35796; S35796.
DR   RefSeq; NP_001105450.1; NM_001111980.1.
DR   AlphaFoldDB; P35081; -.
DR   SMR; P35081; -.
DR   STRING; 4577.GRMZM2G074361_P01; -.
DR   Allergome; 3530; Zea m 12.0101.
DR   Allergome; 682; Zea m 12.
DR   PaxDb; P35081; -.
DR   GeneID; 542409; -.
DR   KEGG; zma:542409; -.
DR   MaizeGDB; 51451; -.
DR   eggNOG; KOG1755; Eukaryota.
DR   OrthoDB; 1428600at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P35081; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0003785; F:actin monomer binding; IDA:AgBase.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; TAS:AgBase.
DR   GO; GO:0070064; F:proline-rich region binding; IDA:AgBase.
DR   GO; GO:0007097; P:nuclear migration; IDA:AgBase.
DR   GO; GO:0030845; P:phospholipase C-inhibiting G protein-coupled receptor signaling pathway; IDA:AgBase.
DR   GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:AgBase.
DR   GO; GO:0042989; P:sequestering of actin monomers; IDA:AgBase.
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-1"
FT                   /id="PRO_0000199646"
FT   MOTIF           81..97
FT                   /note="Involved in PIP2 interaction"
FT                   /evidence="ECO:0000305|PubMed:10760246"
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;  14147 MW;  3AA320DD721BEBB8 CRC64;
     MSWQTYVDEH LMCEIEGHHL TSAAIVGHDG ATWAQSTAFP EFKPEEMAAI MKDFDEPGHL
     APTGLILGGT KYMVIQGEPG AVIRGKKGSG GITVKKTGQS LIIGIYDEPM TPGQCNLVVE
     RLGDYLLEQG M