PGLR2_PLAAC
ID PGLR2_PLAAC Reviewed; 377 AA.
AC Q6H9K0; P82967;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Exopolygalacturonase;
DE EC=3.2.1.67 {ECO:0000269|PubMed:15208603};
DE AltName: Full=Pollen allergen Pla a 2 {ECO:0000303|PubMed:15208603, ECO:0000303|PubMed:17177673, ECO:0000303|Ref.2};
DE AltName: Allergen=Pla a 2.0101 {ECO:0000305};
DE Flags: Precursor; Fragment;
GN Name=plaa2 {ECO:0000312|EMBL:CAE52833.1};
OS Platanus acerifolia (London plane tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Platanaceae; Platanus.
OX NCBI_TaxID=140101;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAE52833.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-25; 130-137; 340-347 AND
RP 349-358, GLYCOSYLATION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY,
RP AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000312|EMBL:CAE52833.1};
RX PubMed=15208603; DOI=10.1016/j.jaci.2004.02.031;
RA Ibarrola I., Arilla M.C., Martinez A., Asturias J.A.;
RT "Identification of a polygalacturonase as a major allergen (Pla a 2) from
RT Platanus acerifolia pollen.";
RL J. Allergy Clin. Immunol. 113:1185-1191(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1007/s00497-005-0002-4;
RA Suarez-Cervera M., Asturias J.A., Vega-Maray A., Castells T.,
RA Lopez-Iglesias C., Ibarrola I., Arilla M.C., Gabarayeva N.,
RA Seoane-Camba J.A.;
RT "The role of allergenic proteins Pla a 1 and Pla a 2 in the germination of
RT Platanus acerifolia pollen grains.";
RL Sex. Plant Reprod. 18:101-112(2005).
RN [3]
RP TISSUE SPECIFICITY, ALLERGEN, AND BIOTECHNOLOGY.
RX PubMed=17177673; DOI=10.1111/j.1365-2222.2006.02591.x;
RA Asturias J.A., Ibarrola I., Amat P., Tella R., Malet A., Cistero-Bahima A.,
RA Enrique E., Malek T., Martinez A.;
RT "Purified allergens vs. complete extract in the diagnosis of plane tree
RT pollen allergy.";
RL Clin. Exp. Allergy 36:1505-1512(2006).
CC -!- FUNCTION: May function in depolymerizing pectin during pollen
CC development, germination, and tube growth. Acts as an exo-
CC polygalacturonase. {ECO:0000250|UniProtKB:P24548,
CC ECO:0000269|PubMed:15208603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC Evidence={ECO:0000269|PubMed:15208603};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15208603}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. Secreted, cell wall
CC {ECO:0000269|Ref.2}. Golgi apparatus {ECO:0000269|Ref.2}. Endoplasmic
CC reticulum {ECO:0000269|Ref.2}. Vesicle {ECO:0000269|Ref.2}. Note=After
CC 5 min in germination medium, detected as a soluble protein and released
CC from apertural and non-apertural regions of pollen grain wall. After 15
CC and 30 min, abundant in the germinal aperture. After 2 h in germination
CC medium, localization in these regions decreases. In mature, non-
CC hydrated pollen grains, abundant in cisternae and vesicles of Golgi in
CC the apertural region. Sparse in the center of the cytoplasm, associated
CC with cisternae and vesicles of the endoplasmic reticulum (ER) and
CC abundant in the generative cell wall. After 5 min of hydration,
CC localization to these regions decreases. After 15 min of hydration,
CC present around emergent pollen tube and in the center of the vegetative
CC cell, both in the ER and Golgi. After 30 min of hydration, present in
CC juncture between pollen wall and pollen tube. Abundant in the ER
CC cisternae, which show a disorganized and interrupted concentric
CC structure with numerous ER vesicles linked to Golgi vesicles.
CC {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen (at protein level)
CC (PubMed:15208603, Ref.2, PubMed:17177673). Expressed in stem, but not
CC in leaves (at protein level) (PubMed:15208603).
CC {ECO:0000269|PubMed:15208603, ECO:0000269|PubMed:17177673,
CC ECO:0000269|Ref.2}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15208603}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to London plane tree pollen (PubMed:15208603,
CC PubMed:17177673). Binds to IgE in 84% of the 26 patients tested
CC (PubMed:15208603). Binds to IgE in 50% of the 26 patients tested
CC (PubMed:17177673). {ECO:0000269|PubMed:15208603,
CC ECO:0000269|PubMed:17177673}.
CC -!- BIOTECHNOLOGY: Could be used together with allergen Pla a 1 for a
CC reliable diagnosis of London plane tree (P.acerifolia) pollen allergy
CC by skin prick test (SPT) in most patients of the cohort of 47 tested
CC with a sensitivity of over 90% and a specificity of 100%.
CC {ECO:0000269|PubMed:17177673}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AJ586898; CAE52833.1; -; mRNA.
DR AlphaFoldDB; Q6H9K0; -.
DR SMR; Q6H9K0; -.
DR Allergome; 3426; Pla a 2.0101.
DR Allergome; 573; Pla a 2.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043667; C:pollen wall; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IDA:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IEP:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IEP:UniProtKB.
DR GO; GO:0048868; P:pollen tube development; IEP:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Allergen; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Glycosidase; Golgi apparatus; Hydrolase; Repeat; Secreted; Signal.
FT SIGNAL <1..5
FT /evidence="ECO:0000269|PubMed:15208603"
FT CHAIN 6..377
FT /note="Exopolygalacturonase"
FT /evidence="ECO:0000269|PubMed:15208603"
FT /id="PRO_0000024821"
FT REPEAT 159..184
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 186..207
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT REPEAT 209..229
FT /note="PbH1 3"
FT /evidence="ECO:0000255"
FT REPEAT 239..260
FT /note="PbH1 4"
FT /evidence="ECO:0000255"
FT REPEAT 269..290
FT /note="PbH1 5"
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAE52833.1"
SQ SEQUENCE 377 AA; 39765 MW; 10E0F271114BA3D3 CRC64;
RGVQSSGSVF NVNDYGAKGA GDISQAVMKA WKAACASQGP STVLIPKGNY NMGEVAMQGP
CKGSKIGFQI DGVVKAPADP SKFKSDGWVS FYRIDGLTVS GTGTLDGQGQ TAWAKNNCDK
NPNCKHAAMN LRFDFLKHAM VRDITSLNSK MFHINVLECE DITFQHVTVT APGTSINTDG
IHVGISKGVT ITNTKIATGD DCISIGPGSQ NVTITQVNCG PGHGISIGSL GRYNNEKEVR
GITVKGCTFS GTMNGVRVKT WPNSPPGAAT DLTFQDLTMN NVQNPVILDQ EYCPYGQCSR
QAPSRIKLSN INFNNIRGTS TGKVAVVIAC SHGMPCSNMK IGEINLSYRG AGGPATSTCS
NVKPTFSGKQ VPAIKCA
