ID PGLR2_CRYJA Reviewed; 514 AA. AC P43212; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Polygalacturonase; DE Short=PG; DE EC=3.2.1.15; DE AltName: Full=Allergen Cry j II; DE AltName: Full=Major pollen allergen Cry j 2; DE AltName: Full=Pectinase; DE AltName: Allergen=Cry j 2; DE Flags: Precursor; OS Cryptomeria japonica (Japanese cedar) (Cupressus japonica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae; OC Cryptomeria. OX NCBI_TaxID=3369; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Pollen; RX PubMed=7926035; DOI=10.1016/0014-5793(94)01022-6; RA Namba M., Kurose M., Torigoe K., Hino K., Taniguchi Y., Fukuda S., Usui M., RA Kurimoto M.; RT "Molecular cloning of the second major allergen, Cry j II, from Japanese RT cedar pollen."; RL FEBS Lett. 353:124-128(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pollen; RX PubMed=8002972; DOI=10.1006/bbrc.1994.1804; RA Komiyama N., Sone T., Shimizu K., Morikubo K., Kino K.; RT "cDNA cloning and expression of Cry j II the second major allergen of RT Japanese cedar pollen."; RL Biochem. Biophys. Res. Commun. 201:1021-1028(1994). RN [3] RP PROTEIN SEQUENCE OF 55-64. RX PubMed=2382797; DOI=10.1111/j.1398-9995.1990.tb00501.x; RA Sakaguchi M., Inouye S., Taniai M., Ando S., Usui M., Matuhasi T.; RT "Identification of the second major allergen of Japanese cedar pollen."; RL Allergy 45:309-312(1990). 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 {ECO:0000305}. Plastid, amyloplast CC {ECO:0000305}. Secreted, cell wall {ECO:0000305}. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D37765; BAA07021.1; -; mRNA. DR EMBL; D29772; BAA06172.1; -; mRNA. DR PIR; JC2498; JC2498. DR PIR; S48730; S48730. DR AlphaFoldDB; P43212; -. DR SMR; P43212; -. DR Allergome; 249; Cry j 2. DR Allergome; 250; Cry j 2.0101. DR CAZy; GH28; Glycoside Hydrolase Family 28. DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell. 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; Single-stranded right-handed beta-helix, Pectin lyase-like; 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 PANTHER; PTHR31375; -; 1. DR PANTHER; PTHR31375:SF175; POLYGALACTURONASE ADPG2; 1. DR Pfam; PF17181; EPF; 1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 5. DR SUPFAM; SSF51126; Pectin lyase-like; 1. DR PROSITE; PS00502; POLYGALACTURONASE; 1. PE 1: Evidence at protein level; KW Allergen; Amyloplast; Cell wall; Cell wall biogenesis/degradation; KW Direct protein sequencing; Fruit ripening; Glycoprotein; Glycosidase; KW Hydrolase; Plastid; Repeat; Secreted; Signal; Zymogen. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..45 FT /evidence="ECO:0000255" FT /id="PRO_0000024816" FT CHAIN 46..433 FT /note="Polygalacturonase" FT /id="PRO_0000024817" FT PROPEP 434..514 FT /evidence="ECO:0000255" FT /id="PRO_0000024818" FT REPEAT 214..240 FT /note="PbH1 1" FT REPEAT 241..262 FT /note="PbH1 2" FT REPEAT 264..284 FT /note="PbH1 3" FT REPEAT 294..315 FT /note="PbH1 4" FT REPEAT 323..344 FT /note="PbH1 5" FT ACT_SITE 255 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052" FT ACT_SITE 278 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 472 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 5 FT /note="F -> L (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="V -> L (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 34..35 FT /note="DI -> VV (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 37 FT /note="Q -> K (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="K -> N (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="N -> S (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 451 FT /note="K -> E (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 454 FT /note="G -> R (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="M -> I (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" FT CONFLICT 507 FT /note="R -> C (in Ref. 2; BAA06172)" FT /evidence="ECO:0000305" SQ SEQUENCE 514 AA; 56645 MW; 624611C3FA8D6302 CRC64; MAMKFIAPMA FVAMQLIIMA AAEDQSAQIM LDSDIEQYLR SNRSLRKVEH SRHDAINIFN VEKYGAVGDG KHDCTEAFST AWQAACKKPS AMLLVPGNKK FVVNNLFFNG PCQPHFTFKV DGIIAAYQNP ASWKNNRIWL QFAKLTGFTL MGKGVIDGQG KQWWAGQCKW VNGREICNDR DRPTAIKFDF STGLIIQGLK LMNSPEFHLV FGNCEGVKII GISITAPRDS PNTDGIDIFA SKNFHLQKNT IGTGDDCVAI GTGSSNIVIE DLICGPGHGI SIGSLGRENS RAEVSYVHVN GAKFIDTQNG LRIKTWQGGS GMASHIIYEN VEMINSENPI LINQFYCTSA SACQNQRSAV QIQDVTYKNI RGTSATAAAI QLKCSDSMPC KDIKLSDISL KLTSGKIASC LNDNANGYFS GHVIPACKNL SPSAKRKESK SHKHPKTVMV KNMGAYDKGN RTRILLGSRP PNCTNKCHGC SPCKAKLVIV HRIMPQEYYP QRWMCSRHGK IYHP //