ID POLC4_BETPN Reviewed; 85 AA. AC Q39419; O04131; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-FEB-2023, entry version 100. DE RecName: Full=Polcalcin Bet v 4; DE AltName: Full=Calcium-binding pollen allergen Bet v 4; DE AltName: Allergen=Bet v 4; GN Name=BETV4; OS Betula pendula (European white birch) (Betula verrucosa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fagales; Betulaceae; Betula. OX NCBI_TaxID=3505; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pollen; RX PubMed=9353329; DOI=10.1074/jbc.272.45.28630; RA Engel E., Richter K., Obermeyer G., Briza P., Kungl A.J., Simon B., RA Auer M., Ebner C., Rheinberger H.J., Breitenbach M., Ferreira F.; RT "Immunological and biological properties of Bet v 4, a novel birch pollen RT allergen with two EF-hand calcium-binding domains."; RL J. Biol. Chem. 272:28630-28637(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pollen; RX PubMed=9345295; DOI=10.1006/bbrc.1997.6860; RA Twardosz A., Hayek B., Seiberler S., Pastore A., Vangelista L., RA Groenlund H., Kraft D., Valenta R.; RT "Molecular characterization, expression in Escherichia coli, and epitope RT analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4."; RL Biochem. Biophys. Res. Commun. 239:197-204(1997). RN [3] RP STRUCTURE BY NMR OF 2-85, AND SUBUNIT. RX PubMed=15037075; DOI=10.1016/j.jmb.2003.12.070; RA Neudecker P., Nerkamp J., Eisenmann A., Nourse A., Lauber T., Schweimer K., RA Lehmann K., Schwarzinger S., Ferreira F., Rosch P.; RT "Solution structure, dynamics, and hydrodynamics of the calcium-bound RT cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric RT two EF-hand assembly with a regulatory function."; RL J. Mol. Biol. 336:1141-1157(2004). CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15037075}. CC -!- ALLERGEN: Causes an allergic reaction in human. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X87153; CAA60628.1; -; mRNA. DR EMBL; Y12560; CAA73147.1; -; mRNA. DR PIR; JC5711; JC5711. DR PIR; S54819; S54819. DR PDB; 1H4B; NMR; -; A=2-85. DR PDBsum; 1H4B; -. DR AlphaFoldDB; Q39419; -. DR SMR; Q39419; -. DR MINT; Q39419; -. DR Allergome; 129; Bet v 4. DR Allergome; 3138; Bet v 4.0101. DR EvolutionaryTrace; Q39419; -. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR10891:SF892; CALCIUM-BINDING PROTEIN CML29-RELATED; 1. DR PANTHER; PTHR10891; EF-HAND CALCIUM-BINDING DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47473; EF-hand; 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..85 FT /note="Polcalcin Bet v 4" FT /id="PRO_0000073666" FT DOMAIN 7..42 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 42..77 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 20 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 22 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 31 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 57 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CONFLICT 71 FT /note="G -> A (in Ref. 2; CAA73147)" FT /evidence="ECO:0000305" FT HELIX 6..19 FT /evidence="ECO:0007829|PDB:1H4B" FT STRAND 24..27 FT /evidence="ECO:0007829|PDB:1H4B" FT HELIX 29..36 FT /evidence="ECO:0007829|PDB:1H4B" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:1H4B" FT HELIX 44..54 FT /evidence="ECO:0007829|PDB:1H4B" FT HELIX 64..73 FT /evidence="ECO:0007829|PDB:1H4B" FT HELIX 75..84 FT /evidence="ECO:0007829|PDB:1H4B" SQ SEQUENCE 85 AA; 9448 MW; E2FC882E5BB8ADFF CRC64; MADDHPQDKA ERERIFKRFD ANGDGKISAA ELGEALKTLG SITPDEVKHM MAEIDTDGDG FISFQEFTDF GRANRGLLKD VAKIF //