ID   PROF6_HEVBR             Reviewed;         131 AA.
AC   Q9LEI8;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Profilin-6;
DE   AltName: Full=Pollen allergen Hev b 8.0204;
DE   AltName: Allergen=Hev b 8.0204;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ganglberger E., Scheiner O., Breiteneder H.;
RT   "Molecular and immunological characterisation of profilin from Hevea
RT   brasiliensis.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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. Involved in latex
CC       allergic reactions.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AJ243325; CAB96215.1; -; mRNA.
DR   PDB; 1G5U; X-ray; 3.10 A; A/B=1-131.
DR   PDBsum; 1G5U; -.
DR   AlphaFoldDB; Q9LEI8; -.
DR   SMR; Q9LEI8; -.
DR   Allergome; 397; Hev b 8.
DR   Allergome; 403; Hev b 8.0204.
DR   OrthoDB; 1428600at2759; -.
DR   EvolutionaryTrace; Q9LEI8; -.
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   3D-structure; Actin-binding; Allergen; Cytoplasm; Cytoskeleton.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..131
FT                   /note="Profilin-6"
FT                   /id="PRO_0000199638"
FT   TURN            3..9
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   HELIX           44..55
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   HELIX           112..127
FT                   /evidence="ECO:0007829|PDB:1G5U"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:1G5U"
SQ   SEQUENCE   131 AA;  14007 MW;  B24428AA0AA73DB2 CRC64;
     MSWQTYVDDH LMCDIDGHRL TAAAIIGHDG SVWAQSSSFP QFKSDEVAAV MKDFDEPGSL
     APTGLHLGGT KYMVIQGEPG AVIRGKKGSG GITVKKTGQA LIIGIYDEPL TPGQCNMIVE
     RLGDYLLDQG L