ID   PLY1_JUNVI              Reviewed;         367 AA.
AC   Q9LLT1; P81825; Q9LLT2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Pectate lyase 1;
DE            EC=4.2.2.2;
DE   AltName: Full=Major pollen allergen Jun v 1;
DE   AltName: Allergen=Jun v 1;
DE   Flags: Precursor;
OS   Juniperus virginiana (Eastern redcedar) (Sabina virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Juniperus.
OX   NCBI_TaxID=39584;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF80166.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-26, VARIANT PHE-209, AND
RP   ALLERGEN.
RC   TISSUE=Pollen {ECO:0000269|PubMed:11422137};
RX   PubMed=11422137; DOI=10.1046/j.1365-2222.2001.01079.x;
RA   Midoro-Horiuti T., Goldblum R.M., Brooks E.G.;
RT   "Identification of mutations in the genes for the pollen allergens of
RT   eastern red cedar (Juniperus virginiana).";
RL   Clin. Exp. Allergy 31:771-778(2001).
CC   -!- FUNCTION: Has pectate lyase activity. {ECO:0000250}.
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   -!- 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   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       patients who are allergic to J.ashei. {ECO:0000269|PubMed:11422137}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF151427; AAF80164.1; -; mRNA.
DR   EMBL; AF151429; AAF80166.1; -; mRNA.
DR   AlphaFoldDB; Q9LLT1; -.
DR   SMR; Q9LLT1; -.
DR   Allergome; 3342; Jun v 1.0101.
DR   Allergome; 3343; Jun v 1.0102.
DR   Allergome; 431; Jun v 1.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   UniPathway; UPA00545; UER00824.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
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   Allergen; Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lyase; Metal-binding; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:11422137"
FT   CHAIN           22..367
FT                   /note="Pectate lyase 1"
FT                   /id="PRO_0000024909"
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:0000250"
FT   DISULFID        128..147
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..312
FT                   /evidence="ECO:0000250"
FT   VARIANT         209
FT                   /note="S -> F"
FT                   /evidence="ECO:0000269|PubMed:11422137"
SQ   SEQUENCE   367 AA;  39709 MW;  DCBD1981A74E4711 CRC64;
     MASPCLIAFL VFLCAIVSCC SDNPIDSCWR GDSNWGQNRM KLADCAVGFG SSTMGGKGGD
     FYTVTSADDN PVNPTPGTLR YGATREKTLW IIFSQNMNIK LKMPLYVAGH KTIDGRGADV
     HLGNGGPCLF MRKVSHVILH GLHIHGCNTS VLGDVLVSES IGVVPVHAQD GDAITMRNVT
     NAWIDHNSLS DCSDGLIDVT LGSTGITISN NHFFNHHKVM LLGHDDTYDD DKSMKVTVAF
     NQFGPNAGQR MPRARYGLVH VANNNYDPWN IYAIGGSSNP TILSEGNSFT APNENYKKEV
     TKRIGCESTS ACANWVWRST RDAFSNGAYF VSSGKIEETN IYNSNEAFKV ENGNAAPQLT
     KNAGVVA