PGLR2_CHAOB
ID PGLR2_CHAOB Reviewed; 514 AA.
AC Q7M1E7;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Polygalacturonase;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Major pollen allergen Cha o 2;
DE AltName: Full=Pectinase;
DE AltName: Allergen=Cha o 2;
DE Flags: Precursor;
OS Chamaecyparis obtusa (Hinoki false-cypress) (Retinospora obtusa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Chamaecyparis.
OX NCBI_TaxID=13415;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 51-62.
RC TISSUE=Pollen;
RX PubMed=10486272; DOI=10.1006/bbrc.1999.1261;
RA Mori T., Yokoyama M., Komiyama N., Okano M., Kino K.;
RT "Purification, identification, and cDNA cloning of Cha o 2, the second
RT major allergen of Japanese cypress pollen.";
RL Biochem. Biophys. Res. Commun. 263:166-171(1999).
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. Binds to IgE.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR PIR; JC7100; JC7100.
DR AlphaFoldDB; Q7M1E7; -.
DR SMR; Q7M1E7; -.
DR Allergome; 198; Cha o 2.
DR Allergome; 3187; Cha o 2.0101.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PRIDE; Q7M1E7; -.
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; 5.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..50
FT /evidence="ECO:0000269|PubMed:10486272"
FT /id="PRO_0000024814"
FT CHAIN 51..514
FT /note="Polygalacturonase"
FT /id="PRO_0000024815"
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 REPEAT 357..384
FT /note="PbH1 6"
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 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 514 AA; 56073 MW; 68B62DEBDD59C1EC CRC64;
MGMKFMAAVA FLALQLIVMA AAEDQSAQIM LDSDIEQYLR SNRSLKKLVH SRHDAATVFN
VEQYGAVGDG KHDSTEAFAT TWNAACKKAS AVLLVPANKK FFVNNLVFRG PCQPHLSFKV
DGTIVAQPDP ARWKNSKIWL QFAQLTDFNL MGTGVIDGQG QQWWAGQCKV VNGRTVCNDR
NRPTAIKIDY SKSVTVKELT LMNSPEFHLV FGECEGVKIQ GLKIKAPRDS PNTDGIDIFA
SKRFHIEKCV IGTGDDCIAI GTGSSNITIK DLICGPGHGI SIGSLGRDNS RAEVSHVHVN
RAKFIDTQNG LRIKTWQGGS GLASYITYEN VEMINSENPI LINQFYCTSA SACQNQRSAV
QIQGVTYKNI HGTSATAAAI QLMCSDSVPC TGIQLSNVSL KLTSGKPASC VDKNARGFYS
GRLIPTCKNL RPGPSPKEFE LQQQPTTVMD ENKGACAKGD STCISLSSSP PNCKNKCKGC
QPCKPKLIIV HPNKPQDYYP QKWVCSCHNK IYNP