PGLR2_JUNAS
ID PGLR2_JUNAS Reviewed; 507 AA.
AC Q9FY19;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Major pollen allergen Jun a 2;
DE AltName: Full=Pectinase;
DE AltName: Allergen=Jun a 2;
DE Flags: Precursor;
GN Name=JNA2;
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], AND PROTEIN SEQUENCE OF 55-63.
RC TISSUE=Pollen;
RX PubMed=10944464; DOI=10.1006/bbrc.2000.3273;
RA Yokoyama M., Miyahara M., Shimizu K., Kino K., Tsunoo H.;
RT "Purification, Identification and cDNA cloning of Jun a 2, the second major
RT allergen of mountain cedar pollen.";
RL Biochem. Biophys. Res. Commun. 275:195-202(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-
CC galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
CC -!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AJ404653; CAC05582.1; -; mRNA.
DR PIR; JC7366; JC7366.
DR AlphaFoldDB; Q9FY19; -.
DR SMR; Q9FY19; -.
DR Allergome; 3339; Jun a 2.0101.
DR Allergome; 428; Jun a 2.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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; 6.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
PE 1: Evidence at protein level;
KW Allergen; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Fruit ripening; Glycoprotein; Glycosidase;
KW Hydrolase; Repeat; Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..54
FT /evidence="ECO:0000269|PubMed:10944464"
FT /id="PRO_0000024819"
FT CHAIN 55..507
FT /note="Polygalacturonase"
FT /id="PRO_0000024820"
FT REPEAT 215..241
FT /note="PbH1 1"
FT REPEAT 242..263
FT /note="PbH1 2"
FT REPEAT 265..285
FT /note="PbH1 3"
FT REPEAT 295..316
FT /note="PbH1 4"
FT REPEAT 324..345
FT /note="PbH1 5"
FT REPEAT 358..385
FT /note="PbH1 6"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 55731 MW; 2B2E0AA5E958FE5A CRC64;
MSMKFMAALA FLALQLIVMA AGEDQSAQIM LDSDTKQYHR SSRNLRKRVH HARHDVAIVF
NVEHYGAVGD GKHDSTDAFE KTWNAACNKL SAVFLVPANK KFVVNNLVFY GPCQPHFSFK
VDGTIAAYPD PAKWKNSKIW MHFARLTDFN LMGTGVIDGQ GNRWWSDQCK TINGRTVCND
KGRPTAIKID FSKSVTVKEL TLTNSPEFHL VFGECDGVKI QGIKIKAPRD SPNTDGIDIF
ASKRFEIEKC TIGTGDDCVA VGTGSSNITI KDLTCGPGHG MSIGSLGKGN SRSEVSFVHL
DGAKFIDTQN GLRIKTWQGG SGLASHITYE NVEMINAENP ILINQFYCTS AAACKNQRSA
VKIQDVTFKN IHGTSATTAA IQLMCSDSVP CSNIKLSNVF LKLTSGKVAT CVNKNANGYY
TNPLNPSCKS LHPGRTPKEL ELHQKPTTLL MDEKMGASLN SSPPNCKNKC KGCQPCKPKL
IIVHPNQPED YYPQRWVCSC HNKIYNP
