ID   PROF1_ARTVU             Reviewed;         133 AA.
AC   Q8H2C9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Profilin-1 {ECO:0000305};
DE   AltName: Full=Pollen allergen Art v 4.01 {ECO:0000303|PubMed:12530543};
DE   AltName: Allergen=Art v 4.01 {ECO:0000303|PubMed:12530543};
OS   Artemisia vulgaris (Mugwort).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=4220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, MASS SPECTROMETRY, AND CLEAVAGE OF
RP   INITIATOR METHIONINE.
RC   TISSUE=Pollen;
RX   PubMed=12530543; DOI=10.1515/bc.2002.199;
RA   Wopfner N., Willeroidee M., Hebenstreit D., van Ree R., Aalbers M.,
RA   Briza P., Thalhamer J., Ebner C., Richter K., Ferreira F.;
RT   "Molecular and immunological characterization of profilin from mugwort
RT   pollen.";
RL   Biol. Chem. 383:1779-1789(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-133, FUNCTION, ALLERGEN, AND
RP   DISULFIDE BONDS.
RX   PubMed=27231348; DOI=10.1074/jbc.m116.733659;
RA   Offermann L.R., Schlachter C.R., Perdue M.L., Majorek K.A., He J.Z.,
RA   Booth W.T., Garrett J., Kowal K., Chruszcz M.;
RT   "Structural, functional, and immunological characterization of profilin
RT   panallergens Amb a 8, Art v 4, and Bet v 2.";
RL   J. Biol. Chem. 291:15447-15459(2016).
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). Possesses high
CC       binding affinity for poly(L-proline) (PubMed:27231348).
CC       {ECO:0000250|UniProtKB:Q9FR39, ECO:0000269|PubMed:27231348}.
CC   -!- SUBUNIT: Dimer and tetramer (PubMed:12530543). Occurs in many kinds of
CC       cells as a complex with monomeric actin in a 1:1 ratio.
CC       {ECO:0000269|PubMed:12530543}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9FR39}.
CC   -!- MASS SPECTROMETRY: Mass=14077; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12530543};
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12530543). Binds
CC       to IgE of mugwort pollen-sensitized patients (PubMed:12530543).
CC       {ECO:0000269|PubMed:12530543}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AJ421030; CAD12861.1; -; mRNA.
DR   PDB; 5EM0; X-ray; 1.10 A; A=2-133.
DR   PDB; 6B6J; X-ray; 1.90 A; A=2-133.
DR   PDBsum; 5EM0; -.
DR   PDBsum; 6B6J; -.
DR   AlphaFoldDB; Q8H2C9; -.
DR   SMR; Q8H2C9; -.
DR   Allergome; 1652; Art v 4.0101.
DR   Allergome; 60; Art v 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   GO; GO:1900750; F:oligopeptide binding; IDA:UniProtKB.
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;
KW   Disulfide bond.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12530543"
FT   CHAIN           2..133
FT                   /note="Profilin-1"
FT                   /id="PRO_0000199620"
FT   DISULFID        95..117
FT                   /evidence="ECO:0000269|PubMed:27231348,
FT                   ECO:0007744|PDB:5EM0, ECO:0007744|PDB:6B6J"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          23..29
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          72..80
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   STRAND          100..108
FT                   /evidence="ECO:0007829|PDB:5EM0"
FT   HELIX           114..130
FT                   /evidence="ECO:0007829|PDB:5EM0"
SQ   SEQUENCE   133 AA;  14207 MW;  96FA8A3D7CA54E3D CRC64;
     MSWQTYVDDH LMCDIEGTGQ HLTSAAIFGT DGTVWAKSAS FPEFKPNEID AIIKEFNEAG
     QLAPTGLFLG GAKYMVIQGE AGAVIRGKKG AGGICIKKTG QAMVFGIYDE PVAPGQCNMV
     VERLGDYLLD QGM