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PROF_CYNDA
ID   PROF_CYNDA              Reviewed;         131 AA.
AC   O04725;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Profilin;
DE   AltName: Full=Pollen allergen Cyn d 12;
DE   AltName: Allergen=Cyn d 12;
GN   Name=PRO1;
GN   and
GN   Name=PRO2;
OS   Cynodon dactylon (Bermuda grass) (Panicum dactylon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Cynodonteae; Eleusininae; Cynodon.
OX   NCBI_TaxID=28909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC   TISSUE=Pollen;
RX   PubMed=9420135; DOI=10.1111/j.1365-2222.1997.tb01176.x;
RA   Asturias J.A., Arilla M.C., Gomez-Bayon N., Martinez J., Martinez A.,
RA   Palacios R.;
RT   "Cloning and high level expression of Cynodon dactylon (Bermuda grass)
RT   pollen profilin (Cyn d 12) in Escherichia coli: purification and
RT   characterization of the allergen.";
RL   Clin. Exp. Allergy 27:1307-1313(1997).
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.
CC       {ECO:0000269|PubMed:9420135}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; Y08390; CAA69670.1; -; mRNA.
DR   EMBL; Y08389; CAA69669.1; -; mRNA.
DR   AlphaFoldDB; O04725; -.
DR   SMR; O04725; -.
DR   Allergome; 279; Cyn d 12.
DR   Allergome; 3233; Cyn d 12.0101.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003785; F:actin monomer binding; IEA:UniProt.
DR   GO; GO:0070064; F:proline-rich region binding; IEA:UniProt.
DR   GO; GO:0007097; P:nuclear migration; IEA:UniProt.
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_0000199629"
SQ   SEQUENCE   131 AA;  14144 MW;  04ED32BC0608A48D CRC64;
     MSWQAYVDDH LMCEIEGHHL TSAAIIGHDG TVWAQSAAFP AFKPEEMANI MKDFDEPGFL
     APTGLFLGPT KYMVIQGEPG AVIRGKKGSG GVTVKKTGQA LVIGIYDEPM TPGQCNMVIE
     KLGDYLIEQG M
 
 
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