POLC3_CHEAL
ID POLC3_CHEAL Reviewed; 86 AA.
AC Q84V36;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Polcalcin Che a 3 {ECO:0000303|PubMed:15208604};
DE AltName: Full=Calcium-binding pollen allergen Che a 3 {ECO:0000303|PubMed:15208604};
DE AltName: Allergen=Che a 3 {ECO:0000303|PubMed:15208604};
OS Chenopodium album (Fat-hen).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Chenopodium.
OX NCBI_TaxID=3559;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=15208604; DOI=10.1016/j.jaci.2003.12.587;
RA Barderas R., Villalba M., Pascual C.Y., Batanero E., Rodriguez R.;
RT "Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of
RT Chenopodium album pollen: isolation, amino acid sequences, and immunologic
RT properties.";
RL J. Allergy Clin. Immunol. 113:1192-1198(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND
RP ALLERGEN.
RX PubMed=18250440; DOI=10.4049/jimmunol.180.4.2313;
RA Verdino P., Barderas R., Villalba M., Westritschnig K., Valenta R.,
RA Rodriguez R., Keller W.;
RT "Three-dimensional structure of the cross-reactive pollen allergen Che a 3:
RT visualizing cross-reactivity on the molecular surfaces of weed, grass, and
RT tree pollen allergens.";
RL J. Immunol. 180:2313-2321(2008).
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE
CC (PubMed:15208604). Exhibits a cross-reactivity with IgE from allergic
CC patient to the Phleum pratense Phl p 7 allergen (PubMed:18250440).
CC {ECO:0000269|PubMed:15208604, ECO:0000269|PubMed:18250440}.
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DR EMBL; AY082338; AAL92871.1; -; mRNA.
DR PDB; 2OPO; X-ray; 1.75 A; A/B/C/D=1-86.
DR PDBsum; 2OPO; -.
DR AlphaFoldDB; Q84V36; -.
DR SMR; Q84V36; -.
DR Allergome; 1069; Che a 3.
DR Allergome; 3190; Che a 3.0101.
DR EvolutionaryTrace; Q84V36; -.
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..86
FT /note="Polcalcin Che a 3"
FT /id="PRO_0000073671"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 43..78
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 23
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 25
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 27
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 32
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 56
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 58
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 60
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:18250440, ECO:0007744|PDB:2OPO"
FT BINDING 67
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:18250440, ECO:0007744|PDB:2OPO"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:2OPO"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2OPO"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:2OPO"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2OPO"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2OPO"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2OPO"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2OPO"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2OPO"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:2OPO"
SQ SEQUENCE 86 AA; 9552 MW; D950CE65546181BB CRC64;
MAAEDTPQDI ADRERIFKRF DTNGDGKISS SELGDALKTL GSVTPDEVRR MMAEIDTDGD
GFISFDEFTD FARANRGLVK DVSKIF
