ID   PROF_PYRCO              Reviewed;         131 AA.
AC   Q9XF38;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Profilin;
DE   AltName: Full=Allergen Pyr c 3;
DE   AltName: Allergen=Pyr c 4;
OS   Pyrus communis (Pear) (Pyrus domestica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=23211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC   STRAIN=cv. Williams;
RX   PubMed=11419723; DOI=10.1016/s0378-4347(01)00090-1;
RA   Scheurer S., Wangorsch A., Nerkamp J., Skov P.S., Ballmer-Weber B.,
RA   Wuthrich B., Haustein D., Vieths S.;
RT   "Cross-reactivity within the profilin panallergen family investigated by
RT   comparison of recombinant profilins from pear (Pyr c 4), cherry (Pru av 4)
RT   and celery (Api g 4) with birch pollen profilin Bet v 2.";
RL   J. Chromatogr. B 756:315-325(2001).
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   -!- ALLERGEN: Causes an allergic reaction in human. Food allergen.
CC       {ECO:0000269|PubMed:11419723}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AF129424; AAD29410.1; -; mRNA.
DR   AlphaFoldDB; Q9XF38; -.
DR   SMR; Q9XF38; -.
DR   Allergome; 3459; Pyr c 4.0101.
DR   Allergome; 608; Pyr c 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Profilin"
FT                   /id="PRO_0000199670"
SQ   SEQUENCE   131 AA;  14064 MW;  B51211E2DB6C0938 CRC64;
     MSWQAYVDDH LMCDIDGHHL TAAAILGHDG SVWAQSSTFP KFKPEEITAI MKDFDEPGSL
     APTGLHLGGT KYMVIQGEGG AVIRGKKGSG GVTVKKTSQA LVFGIYEEPL TPGQCNMIVE
     RLGDYLIDQG L