ID   PRO11_MAIZE             Reviewed;         131 AA.
AC   A4KA60;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Profilin-11;
DE   AltName: Full=Pollen allergen Zea m 12;
DE   AltName: Full=Pollen profilin variant 6;
DE   AltName: Allergen=Zea m 12;
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], AND POLYMORPHISM.
RC   STRAIN=cv. Birko;
RX   PubMed=22348028; DOI=10.1371/journal.pone.0030878;
RA   Jimenez-Lopez J.C., Morales S., Castro A.J., Volkmann D.,
RA   Rodriguez-Garcia M.I., Alche Jde D.;
RT   "Characterization of profilin polymorphism in pollen with a focus on
RT   multifunctionality.";
RL   PLoS ONE 7:E30878-E30878(2012).
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 similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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; DQ663564; ABG81317.1; -; mRNA.
DR   AlphaFoldDB; A4KA60; -.
DR   SMR; A4KA60; -.
DR   Allergome; 682; Zea m 12.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; A4KA60; 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; IBA:GO_Central.
DR   GO; GO:0070064; F:proline-rich region binding; IEA:UniProt.
DR   GO; GO:0007097; P:nuclear migration; IEA:UniProt.
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-11"
FT                   /id="PRO_0000425070"
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;  14189 MW;  21D5519CC6E21605 CRC64;
     MSWQAYVDEH LMCEIEGHHL TSAAIVGHDG AVWAQSTAFP QSKTEEMTNI MKDFDEPGFL
     APTGLFLGPT KYMVIQGEPG AVIRGKKGSG GITVKKTGQA MVVGIYDEPM TPGQCNMVVE
     RLGDYLLEQG L