PRO10_PHLPR
ID PRO10_PHLPR Reviewed; 131 AA.
AC A4KA38;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Profilin-10;
DE AltName: Full=Pollen allergen Phl p 12;
DE AltName: Full=pollen profilin variant 8;
DE AltName: Allergen=Phl p 12;
OS Phleum pratense (Common timothy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poinae;
OC Phleum.
OX NCBI_TaxID=15957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
RC STRAIN=cv. Pratense;
RX PubMed=22348028; DOI=10.1371/journal.pone.0030878;
RA Jimenez-Lopez J.C., Morales S., Castro A.J., Volkmann D.,
RA Rodriguez-Garcia M.I., Alche Jde D.;
RT "Characterization of profilin polymorphism in pollen with a focus on
RT multifunctionality.";
RL PLoS ONE 7:E30878-E30878(2012).
RN [2]
RP 3D-STRUCTURE MODELING, AND DISULFIDE BOND.
RX PubMed=24146818; DOI=10.1371/journal.pone.0076066;
RA Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.D.;
RT "Analysis of the effects of polymorphism on pollen profilin structural
RT functionality and the generation of conformational, T- and B-cell
RT epitopes.";
RL PLoS ONE 8:E76066-E76066(2013).
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 similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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 -!- MISCELLANEOUS: The variability of the residues taking part of IgE-
CC binding epitopes might be responsible of the difference in cross-
CC reactivity among olive pollen cultivars, and between distantly related
CC pollen species, leading to a variable range of allergy reactions among
CC atopic patients. {ECO:0000305|PubMed:24146818}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; DQ663542; ABG81295.1; -; mRNA.
DR AlphaFoldDB; A4KA38; -.
DR SMR; A4KA38; -.
DR Allergome; 553; Phl p 12.
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; Disulfide bond;
KW Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..131
FT /note="Profilin-10"
FT /id="PRO_0000425064"
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|PubMed:24146818"
SQ SEQUENCE 131 AA; 14118 MW; 3C7E7002343AFB35 CRC64;
MSWQAYVDEH LMCEIEGHHL ASAAILGHDG TVWAQSADFP QFKPEEITGI MKDFDEPGHL
APTGMFVATA KYMVIQGEPG AVIRGKKGAG GITIKKTGQA LVVGIYDEPM TPGQCSMVVE
RLGDYLVKQG L
