PLY1_JUNAS
ID PLY1_JUNAS Reviewed; 367 AA.
AC P81294; Q9ZNU7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Pectate lyase 1;
DE EC=4.2.2.2;
DE AltName: Full=Major pollen allergen Jun a 1 {ECO:0000303|PubMed:10482835, ECO:0000303|PubMed:10482836};
DE AltName: Allergen=Jun a 1 {ECO:0000303|PubMed:10482835, ECO:0000303|PubMed:10482836, ECO:0000303|PubMed:14563374, ECO:0000303|PubMed:15665478, ECO:0000303|PubMed:16423400};
DE Flags: Precursor;
OS Juniperus ashei (Ozark white cedar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Juniperus.
OX NCBI_TaxID=13101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-38; 42-50; 58-80; 88-94;
RP 117-124; 134-140; 160-164; 256-263 AND 322-325, TISSUE SPECIFICITY, AND
RP ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=10482836; DOI=10.1016/s0091-6749(99)70332-5;
RA Midoro-Horiuti T.M., Goldblum R.M., Kurosky A., Wood T.G., Brooks E.G.;
RT "Molecular cloning of the mountain cedar (Juniperus ashei) pollen major
RT allergen, Jun a 1.";
RL J. Allergy Clin. Immunol. 104:613-617(1999).
RN [2]
RP PROTEIN SEQUENCE OF 22-50, TISSUE SPECIFICITY, AND ALLERGEN.
RC TISSUE=Pollen;
RX PubMed=10482835; DOI=10.1016/s0091-6749(99)70331-3;
RA Midoro-Horiuti T., Goldblum R.M., Kurosky A., Goetz D.W., Brooks E.G.;
RT "Isolation and characterization of the mountain cedar (Juniperus ashei)
RT pollen major allergen, Jun a 1.";
RL J. Allergy Clin. Immunol. 104:608-612(1999).
RN [3]
RP TISSUE SPECIFICITY, ALLERGEN, REGIONS, AND 3D-STRUCTURE MODELING.
RX PubMed=14563374; DOI=10.1016/s0161-5890(03)00168-8;
RA Midoro-Horiuti T., Mathura V., Schein C.H., Braun W., Yu S., Watanabe M.,
RA Lee J.C., Brooks E.G., Goldblum R.M.;
RT "Major linear IgE epitopes of mountain cedar pollen allergen Jun a 1 map to
RT the pectate lyase catalytic site.";
RL Mol. Immunol. 40:555-562(2003).
RN [4]
RP GLYCOSYLATION.
RX PubMed=15665478; DOI=10.1271/bbb.69.137;
RA Kimura Y., Kamamoto M., Maeda M., Okano M., Yokoyama M., Kino K.;
RT "Occurrence of Lewis a epitope in N-glycans of a glycoallergen, Jun a 1,
RT from mountain cedar (Juniperus ashei) pollen.";
RL Biosci. Biotechnol. Biochem. 69:137-144(2005).
RN [5]
RP TISSUE SPECIFICITY, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=16423400; DOI=10.1016/j.molimm.2005.12.001;
RA Varshney S., Goldblum R.M., Kearney C., Watanabe M., Midoro-Horiuti T.;
RT "Major mountain cedar allergen, Jun a 1, contains conformational as well as
RT linear IgE epitopes.";
RL Mol. Immunol. 44:2781-2785(2007).
RN [6]
RP FUNCTION AS A PECTATE LYASE, CATALYTIC ACTIVITY, IGE-BINDING, AND
RP MUTAGENESIS OF HIS-224.
RX PubMed=20559000; DOI=10.1159/000316345;
RA Liu Z., Bhattacharyya S., Ning B., Midoro-Horiuti T., Czerwinski E.W.,
RA Goldblum R.M., Mort A., Kearney C.M.;
RT "Plant-expressed recombinant mountain cedar allergen Jun a 1 is allergenic
RT and has limited pectate lyase activity.";
RL Int. Arch. Allergy Immunol. 153:347-358(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-367, AND DISULFIDE BONDS.
RX PubMed=15539389; DOI=10.1074/jbc.m409655200;
RA Czerwinski E.W., Midoro-Horiuti T., White M.A., Brooks E.G., Goldblum R.M.;
RT "Crystal structure of Jun a 1, the major cedar pollen allergen from
RT Juniperus ashei, reveals a parallel beta-helical core.";
RL J. Biol. Chem. 280:3740-3746(2005).
CC -!- FUNCTION: Has low pectate lyase activity.
CC {ECO:0000269|PubMed:20559000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC Evidence={ECO:0000269|PubMed:20559000};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level).
CC {ECO:0000269|PubMed:10482835, ECO:0000269|PubMed:10482836,
CC ECO:0000269|PubMed:14563374, ECO:0000269|PubMed:16423400}.
CC -!- PTM: N-glycosylated; consists of complex-type N-glycans containing the
CC Lewis a antigen (Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-).
CC {ECO:0000269|PubMed:15665478}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to mountain cedar (PubMed:10482836, PubMed:10482835,
CC PubMed:14563374, PubMed:16423400). Binds to IgE in 71% of the 14
CC patients tested allergic to mountain cedar. Binds to IgE in 40% of the
CC 35 patients tested allergic to Japanese cedar (PubMed:10482835). IgE-
CC binding is significantly reduced by heat denaturation (75 degrees
CC Celsius), chemical denaturation (guanidine treatment) and reductive
CC alkylation in guanidine, but not by reductive alkylation alone,
CC indicating the presence of conformational epitopes. On the other hand,
CC heat and guanidine-induced denaturation increases binding to a mouse
CC monoclonal antibody KW-S91, indicative of enhanced display of the
CC linear epitope by these treatments (PubMed:16423400). Causes
CC proliferation of the peripheral blood mononuclear cells (PBMCs) in
CC patients allergic to mountain cedar (PubMed:10482835). Causes seasonal
CC allergic rhinitis in North America (PubMed:10482836, PubMed:10482835,
CC PubMed:14563374, PubMed:16423400). {ECO:0000269|PubMed:10482835,
CC ECO:0000269|PubMed:10482836, ECO:0000269|PubMed:14563374,
CC ECO:0000269|PubMed:16423400}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC subfamily. {ECO:0000305}.
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DR EMBL; AF106663; AAD03609.1; -; mRNA.
DR EMBL; AF106662; AAD03608.1; -; mRNA.
DR PDB; 1PXZ; X-ray; 1.70 A; A/B=22-367.
DR PDBsum; 1PXZ; -.
DR AlphaFoldDB; P81294; -.
DR SMR; P81294; -.
DR Allergome; 3337; Jun a 1.0101.
DR Allergome; 3338; Jun a 1.0102.
DR Allergome; 427; Jun a 1.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR UniPathway; UPA00545; UER00824.
DR EvolutionaryTrace; P81294; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IDA:UniProtKB.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR018082; AmbAllergen.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR PRINTS; PR00807; AMBALLERGEN.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lyase; Metal-binding; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10482835"
FT CHAIN 22..367
FT /note="Pectate lyase 1"
FT /id="PRO_0000024908"
FT REGION 38..305
FT /note="Beta-helix"
FT REGION 92..104
FT /note="IgE-binding. Binds to IgE in 5 out of 7 patients
FT tested"
FT /evidence="ECO:0000269|PubMed:14563374"
FT REGION 239..250
FT /note="IgE-binding. Binds to IgE in 6 out of 7 patients
FT tested"
FT /evidence="ECO:0000269|PubMed:14563374"
FT REGION 251..258
FT /note="IgE-binding. Binds to IgE in 5 out of 7 patients
FT tested"
FT /evidence="ECO:0000269|PubMed:14563374"
FT REGION 317..327
FT /note="IgE-binding. Binds to IgE in 3 out of 7 patients
FT tested"
FT /evidence="ECO:0000269|PubMed:14563374"
FT ACT_SITE 250
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..45
FT /evidence="ECO:0000269|PubMed:15539389"
FT DISULFID 128..147
FT /evidence="ECO:0000269|PubMed:15539389"
FT DISULFID 306..312
FT /evidence="ECO:0000269|PubMed:15539389"
FT MUTAGEN 224
FT /note="H->A: Reduced pectate lyase activity."
FT /evidence="ECO:0000269|PubMed:20559000"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1PXZ"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1PXZ"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1PXZ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:1PXZ"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1PXZ"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1PXZ"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:1PXZ"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:1PXZ"
SQ SEQUENCE 367 AA; 39825 MW; FC9B81E675662E49 CRC64;
MASPCLIAVL VFLCAIVSCY SDNPIDSCWR GDSNWDQNRM KLADCAVGFG SSTMGGKGGD
FYTVTSTDDN PVNPTPGTLR YGATREKALW IIFSQNMNIK LKMPLYVAGH KTIDGRGADV
HLGNGGPCLF MRKVSHVILH SLHIHGCNTS VLGDVLVSES IGVEPVHAQD GDAITMRNVT
NAWIDHNSLS DCSDGLIDVT LGSTGITISN NHFFNHHKVM LLGHDDTYDD DKSMKVTVAF
NQFGPNAGQR MPRARYGLVH VANNNYDPWN IYAIGGSSNP TILSEGNSFT APSESYKKEV
TKRIGCESPS ACANWVWRST RDAFINGAYF VSSGKTEETN IYNSNEAFKV ENGNAAPQLT
KNAGVVT
