POLC7_PHLPR
ID POLC7_PHLPR Reviewed; 78 AA.
AC O82040;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Polcalcin Phl p 7 {ECO:0000305};
DE AltName: Full=Calcium-binding pollen allergen Phl p 7 {ECO:0000303|PubMed:10224228};
DE Short=Protein P7 {ECO:0000312|EMBL:CAA76887.1};
DE AltName: Allergen=Phl p 7 {ECO:0000303|PubMed:10224228};
GN Name=P7 {ECO:0000312|EMBL:CAA76887.1};
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], ALLERGEN, AND TISSUE SPECIFICITY.
RC TISSUE=Pollen;
RX PubMed=10224228; DOI=10.1096/fasebj.13.8.843;
RA Niederberger V., Hayek B., Vrtala S., Laffer S., Twardosz A.,
RA Vangelista L., Sperr W.R., Valent P., Rumpold H., Kraft D., Ehrenberger K.,
RA Valenta R., Spitzauer S.;
RT "Calcium-dependent immunoglobulin E recognition of the apo- and calcium-
RT bound form of a cross-reactive two EF-hand timothy grass pollen allergen,
RT Phl p 7.";
RL FASEB J. 13:843-856(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RX PubMed=12356717; DOI=10.1093/emboj/cdf526;
RA Verdino P., Westritschnig K., Valenta R., Keller W.;
RT "The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a
RT novel dimer assembly.";
RL EMBO J. 21:5007-5016(2002).
RN [3]
RP STRUCTURE BY NMR OF 2-78 IN COMPLEX WITH CALCIUM, AND SUBUNIT.
RX PubMed=23011803; DOI=10.1002/prot.24186;
RA Henzl M.T., Sirianni A.G., Wycoff W.G., Tan A., Tanner J.J.;
RT "Solution structures of polcalcin Phl p 7 in three ligation states: Apo-,
RT hemi-Mg2+-bound, and fully Ca2+-bound.";
RL Proteins 81:300-315(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CALCIUM, SUBUNIT,
RP AND ALLERGEN.
RX PubMed=30150373; DOI=10.1073/pnas.1806840115;
RA Mitropoulou A.N., Bowen H., Dodev T.S., Davies A.M., Bax H.J., Beavil R.L.,
RA Beavil A.J., Gould H.J., James L.K., Sutton B.J.;
RT "Structure of a patient-derived antibody in complex with allergen reveals
RT simultaneous conventional and superantigen-like recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E8707-E8716(2018).
CC -!- FUNCTION: May be involved in the regulation of pollen-tube growth.
CC {ECO:0000305|PubMed:23011803}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23011803,
CC ECO:0000269|PubMed:30150373}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in pollen.
CC {ECO:0000269|PubMed:10224228}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:10224228,
CC PubMed:30150373). Binds to IgE of sensitized grass pollen allergic
CC patients (PubMed:10224228, PubMed:30150373). Triggers immediate
CC hypersensitivity reactions by cross-linking receptor-bound IgE
CC molecules on effector cells, and induces degranulation of basophils
CC sensitized with IgE (PubMed:30150373). Recombinant protein induces
CC basophil histamine release and immediate type skin reactions in
CC sensitized allergic patients (PubMed:10224228).
CC {ECO:0000269|PubMed:10224228, ECO:0000269|PubMed:30150373}.
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DR EMBL; Y17835; CAA76887.1; -; mRNA.
DR PDB; 1K9U; X-ray; 1.75 A; A/B=1-78.
DR PDB; 2LVI; NMR; -; A=2-78.
DR PDB; 2LVJ; NMR; -; A=2-78.
DR PDB; 2LVK; NMR; -; A=2-78.
DR PDB; 5OTJ; X-ray; 2.35 A; C/D=1-78.
DR PDBsum; 1K9U; -.
DR PDBsum; 2LVI; -.
DR PDBsum; 2LVJ; -.
DR PDBsum; 2LVK; -.
DR PDBsum; 5OTJ; -.
DR AlphaFoldDB; O82040; -.
DR BMRB; O82040; -.
DR SASBDB; O82040; -.
DR SMR; O82040; -.
DR MINT; O82040; -.
DR Allergome; 3422; Phl p 7.0101.
DR Allergome; 570; Phl p 7.
DR ABCD; O82040; 1 sequenced antibody.
DR EvolutionaryTrace; O82040; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Metal-binding; Repeat.
FT CHAIN 1..78
FT /note="Polcalcin Phl p 7"
FT /id="PRO_0000073675"
FT DOMAIN 1..35
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 35..70
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:12356717, ECO:0000269|PubMed:23011803,
FT ECO:0000269|PubMed:30150373, ECO:0007744|PDB:1K9U,
FT ECO:0007744|PDB:2LVK, ECO:0007744|PDB:5OTJ"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:1K9U"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1K9U"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1K9U"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:1K9U"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1K9U"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:1K9U"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:1K9U"
SQ SEQUENCE 78 AA; 8677 MW; 1469370AAEAE2244 CRC64;
MADDMERIFK RFDTNGDGKI SLSELTDALR TLGSTSADEV QRMMAEIDTD GDGFIDFNEF
ISFCNANPGL MKDVAKVF
