PGLR2_CRYJA
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 03-AUG-2022, entry version 92.
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}.
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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; -; 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; 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
