PLAL1_PLALA
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 03-AUG-2022, entry version 66.
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}.
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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; PTHR31614; 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
