ID   PGLR_GOSHI              Reviewed;         407 AA.
AC   Q39786;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Polygalacturonase;
DE            Short=PG;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase;
DE   Flags: Precursor;
GN   Name=G9;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Coker 312; TISSUE=Pollen;
RX   PubMed=7858233; DOI=10.1007/bf00019509;
RA   John M.E., Petersen M.W.;
RT   "Cotton (Gossypium hirsutum L.) pollen-specific polygalacturonase mRNA:
RT   tissue and temporal specificity of its promoter in transgenic tobacco.";
RL   Plant Mol. Biol. 26:1989-1993(1994).
CC   -!- FUNCTION: May function in the depolymerization of the pectin in its
CC       walls during pollen tube elongation, or in that of the pistil during
CC       pollination.
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:0000250}. Secreted, cell wall
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Pollen.
CC   -!- DEVELOPMENTAL STAGE: Appears 12 days before anthesis and maximum levels
CC       are seen in pollen on the day of anthesis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; U09717; AAA82167.1; -; mRNA.
DR   PIR; S52006; S52006.
DR   RefSeq; NP_001314388.1; NM_001327459.1.
DR   AlphaFoldDB; Q39786; -.
DR   SMR; Q39786; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   GeneID; 107942091; -.
DR   KEGG; ghi:107942091; -.
DR   Proteomes; UP000189702; Genome assembly.
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   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   2: Evidence at transcript level;
KW   Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..407
FT                   /note="Polygalacturonase"
FT                   /id="PRO_0000024803"
FT   REPEAT          180..206
FT                   /note="PbH1 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          207..228
FT                   /note="PbH1 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          260..281
FT                   /note="PbH1 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          290..311
FT                   /note="PbH1 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          357..384
FT                   /note="PbH1 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        223..240
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        351..357
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
FT   DISULFID        379..395
FT                   /evidence="ECO:0000250|UniProtKB:O74213"
SQ   SEQUENCE   407 AA;  43921 MW;  B81B2BC4C312D195 CRC64;
     MAPHLNIVPS MFVLLLLFIS ASKVQSDAFD VVAKFGAKAD GKTDLSKPFL DAWKEACASV
     TPSTVVIPKG TYLLSKVNLE GPCKAPIEIN VQGTIQAPAD PSAFKDPNWV RFYSVENFKM
     FGGGIFDGQG SIAYEKNTCE NREFRSKLPV NIRFDFLTNA LIQDITSKDS KLFHINVFAC
     KNITLERLKI EAPDESPNTD GIHMGKSEGV NIIASDIKTG DDCISIGDGT KNMVIKEITC
     GPGHGISIGS LGKFQNEEPV EGIKISNCTI TNTSNGARIK TWPGEHGGAV SEIHFEDITM
     NNVSSPILID QQYCPWNKCK KNEESKVKLS NISFKNIRGT SALPEAIKFI CSGSSPCQNV
     ELADIDIKHN GAEPATSQCL NVKPITSGKL NPIPCSGPVP KTPSATA