ID PLAL1_PLALA Reviewed; 131 AA. AC P82242; Q93X26; Q949A3; Q949A4; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 12-FEB-2003, sequence version 2. DT 27-MAR-2024, entry version 69. DE RecName: Full=Major pollen allergen Pla l 1; DE AltName: Allergen=Pla l 1; OS Plantago lanceolata (English plantain) (Ribwort plantain). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Plantaginaceae; Plantagineae; Plantago. OX NCBI_TaxID=39414; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pollen; RX PubMed=12646046; DOI=10.1042/bj20021491; RA Calabozo B., Diaz-Perales A., Salcedo G., Barber D., Polo F.; RT "Cloning and expression of biologically active Plantago lanceolata pollen RT allergen Pla l 1 in the yeast Pichia pastoris."; RL Biochem. J. 372:889-896(2003). RN [2] RP PROTEIN SEQUENCE OF 1-18. RC TISSUE=Pollen; RX PubMed=11251634; DOI=10.1046/j.1365-2222.2001.00985.x; RA Calabozo B., Barber D., Polo F.; RT "Purification and characterization of the main allergen of Plantago RT lanceolata pollen, Pla l 1."; RL Clin. Exp. Allergy 31:322-330(2001). RN [3] RP STRUCTURE OF CARBOHYDRATE. RX PubMed=12569985; DOI=10.1046/j.1365-2222.2002.01530.x; RA Calabozo B., Barber D., Polo F.; RT "Studies on the carbohydrate moiety of Pla l 1 allergen. Identification of RT a major N-glycan and significance for the immunoglobulin E-binding RT activity."; RL Clin. Exp. Allergy 32:1628-1634(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH ZINC, AND DISULFIDE RP BONDS. RX PubMed=27965108; DOI=10.1016/j.jaci.2016.10.035; RA Stemeseder T., Freier R., Wildner S., Fuchs J.E., Briza P., Lang R., RA Batanero E., Lidholm J., Liedl K.R., Campo P., Hawranek T., Villalba M., RA Brandstetter H., Ferreira F., Gadermaier G.; RT "Crystal structure of Pla l 1 reveals both structural similarity and RT allergenic divergence within the Ole e 1-like protein family."; RL J. Allergy Clin. Immunol. 140:277-280(2017). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Exists in two variants: glycosylated and non-glycosylated. Carries CC a complex, major N-linked glycan, with a alpha-1,3-fucose residue in CC its structure and probably also a beta-1,2-xylose. The average CC modification of molecular mass due to glycosylation is approximately CC 969 Da. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. The CC English plantain pollen is an important cause of pollinosis in the CC temperate regions of North America, Australia and Europe. The glycan CC moiety does not seem to constitute a relevant allergenic epitope. CC -!- SIMILARITY: Belongs to the Ole e I family. {ECO:0000305}. 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; AJ313166; CAC41633.1; -; mRNA. DR EMBL; AJ313167; CAC41634.1; -; mRNA. DR EMBL; AJ313168; CAC41635.1; -; mRNA. DR PDB; 4Z8W; X-ray; 1.98 A; A=1-131. DR PDBsum; 4Z8W; -. DR AlphaFoldDB; P82242; -. DR SMR; P82242; -. DR Allergome; 1323; Pla l 1.0101. DR Allergome; 1324; Pla l 1.0102. DR Allergome; 1325; Pla l 1.0103. DR Allergome; 574; Pla l 1. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR InterPro; IPR006041; Pollen_Ole_e1_allergen. DR PANTHER; PTHR31614:SF20; ANTHER-SPECIFIC PROTEIN LAT52; 1. DR PANTHER; PTHR31614; PROTEIN DOWNSTREAM OF FLC-RELATED; 1. DR Pfam; PF01190; Pollen_Ole_e_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Metal-binding; Secreted; Zinc. FT CHAIN 1..131 FT /note="Major pollen allergen Pla l 1" FT /id="PRO_0000215117" FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305" FT DISULFID 17..86 FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT DISULFID 20..131 FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT DISULFID 42..74 FT /evidence="ECO:0000269|PubMed:27965108, FT ECO:0007744|PDB:4Z8W" FT VARIANT 58 FT /note="D -> G (in Pla l 1.0102 and 1.0103)" FT VARIANT 82 FT /note="S -> G (in Pla l 1.0103)" FT STRAND 8..18 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 61..69 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:4Z8W" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:4Z8W" SQ SEQUENCE 131 AA; 14521 MW; 62F9B279ED3A4BC6 CRC64; TQTSHPAKFH VEGEVYCNVC HSRNLINELS ERMAGAQVQL DCKDDSKKVI YSIGGETDQD GVYRLPVVGY HEDCEIKLVK SSRPDCSEIP KLAKGTIQTS KVDLSKNTTI TEKTRHVKPL SFRAKTDAPG C //