ID   PROF4_MAIZE             Reviewed;         131 AA.
AC   O22655;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Profilin-4;
DE   AltName: Full=Pollen allergen Zea m 12;
DE   AltName: Full=ZmPRO4;
DE   AltName: Allergen=Zea m 12;
GN   Name=PRO4;
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 CHARACTERIZATION.
RC   STRAIN=cv. Wisconsin 64A2;
RX   PubMed=9634586; DOI=10.2307/3870684;
RA   Gibbon B.C., Zonia L.E., Kovar D.R., Hussey P.J., Staiger C.J.;
RT   "Pollen profilin function depends on interaction with proline-rich
RT   motifs.";
RL   Plant Cell 10:981-993(1998).
RN   [2]
RP   ERRATUM OF PUBMED:9634586.
RA   Gibbon B.C., Zonia L.E., Kovar D.R., Hussey P.J., Staiger C.J.;
RL   Plant Cell 11:1603-1603(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. Has a high affinity for poly-
CC       proline.
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: Expressed predominantly in endosperm but is also
CC       found at low levels in all tissues examined, including mature and
CC       germinated pollen.
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   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AF032370; AAB86960.1; -; mRNA.
DR   PIR; T01328; T01328.
DR   RefSeq; NP_001104885.1; NM_001111415.1.
DR   AlphaFoldDB; O22655; -.
DR   SMR; O22655; -.
DR   STRING; 4577.GRMZM2G108780_P01; -.
DR   Allergome; 3538; Zea m 12.0104.
DR   Allergome; 682; Zea m 12.
DR   PaxDb; O22655; -.
DR   PRIDE; O22655; -.
DR   GeneID; 541662; -.
DR   KEGG; zma:541662; -.
DR   eggNOG; KOG1755; Eukaryota.
DR   HOGENOM; CLU_120772_0_1_1; -.
DR   OMA; CEVEGNH; -.
DR   OrthoDB; 1428600at2759; -.
DR   Proteomes; UP000007305; Chromosome 6.
DR   ExpressionAtlas; O22655; baseline and differential.
DR   Genevisible; O22655; ZM.
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:0009555; P:pollen development; TAS:AgBase.
DR   GO; GO:0009860; P:pollen tube growth; TAS:AgBase.
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-4"
FT                   /id="PRO_0000199649"
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"
SQ   SEQUENCE   131 AA;  14101 MW;  E0744573FAADBE85 CRC64;
     MSWQAYVDEH LMCEIEGQHL SAAAIVGHDG SVWAQSESFP ELKPEEVAGI IKDFDEPGTL
     APTGLFVGGT KYMVIQGEPG VVIRGKKGTG GITIKKTGMS LIIGVYDEPM TPGQCNMVVE
     RLGDYLIEQG F