PROF_PHODC
ID PROF_PHODC Reviewed; 131 AA.
AC Q8L5D8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Profilin {ECO:0000255|RuleBase:RU003909, ECO:0000303|PubMed:15784118};
DE AltName: Allergen=Pho d 2 {ECO:0000303|PubMed:15784118};
OS Phoenix dactylifera (Date palm).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Coryphoideae;
OC Phoeniceae; Phoenix.
OX NCBI_TaxID=42345 {ECO:0000312|EMBL:CAD10390.1};
RN [1] {ECO:0000312|EMBL:CAD10390.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000312|EMBL:CAD10390.1};
RX PubMed=15784118; DOI=10.1111/j.1365-2222.2005.02179.x;
RA Asturias J.A., Ibarrola I., Fernandez J., Arilla M.C., Gonzalez-Rioja R.,
RA Martinez A.;
RT "Pho d 2, a major allergen from date palm pollen, is a profilin: cloning,
RT sequencing, and immunoglobulin E cross-reactivity with other profilins.";
RL Clin. Exp. Allergy 35:374-381(2005).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-84 AND 97-121, ALLERGEN, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Pollen {ECO:0000303|PubMed:28126622};
RX PubMed=28126622; DOI=10.1016/j.molimm.2017.01.017;
RA Moya R., Rubio V., Beitia J.M., Carnes J., Lopez-Matas M.A.;
RT "Purification and immunochemical characterization of Pla l 2, the profilin
RT from Plantago lanceolata.";
RL Mol. Immunol. 83:100-106(2017).
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.
CC {ECO:0000255|RuleBase:RU003908}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio. {ECO:0000255|RuleBase:RU003908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P35081}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:15784118, ECO:0000269|PubMed:28126622}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU003909}.
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DR EMBL; AJ417566; CAD10390.1; -; mRNA.
DR RefSeq; NP_001288607.1; NM_001301678.1.
DR AlphaFoldDB; Q8L5D8; -.
DR SMR; Q8L5D8; -.
DR STRING; 42345.XP_008795502.1; -.
DR Allergome; 3423; Pho d 2.0101.
DR Allergome; 571; Pho d 2.
DR GeneID; 103711216; -.
DR KEGG; pda:103711216; -.
DR Proteomes; UP000228380; Chromosome 11.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
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;
KW Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..131
FT /note="Profilin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439275"
FT MOTIF 81..97
FT /note="Involved in PIP2 interaction"
FT /evidence="ECO:0000250|UniProtKB:P35081"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ST99"
FT DISULFID 13..115
FT /evidence="ECO:0000250|UniProtKB:P35081"
SQ SEQUENCE 131 AA; 14269 MW; E4A86A9094A8EA75 CRC64;
MSWQAYVDEH LMCEIDGHHL TAAAILGHDG SVWAQSSSFP QFKSEEITNI MNDFNEPGSL
APTGLYLGST KYMVIQGEPG AVIRGKKGSG GVTVKKTNQA LIFGIYEEPM TPGQCNMVVE
RLGDYLIEQG M