ADPG2_ARATH
ID ADPG2_ARATH Reviewed; 433 AA.
AC Q8RY29; O22935; Q8H782;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Polygalacturonase ADPG2;
DE Short=AtADPG2;
DE Short=PG ADPG2;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase ADPG2;
DE AltName: Full=Protein ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 2;
DE Flags: Precursor;
GN Name=ADPG2; Synonyms=PGAZAT; OrderedLocusNames=At2g41850; ORFNames=T11A7.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-185.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11842157; DOI=10.1104/pp.010610;
RA Gonzalez-Carranza Z.H., Whitelaw C.A., Swarup R., Roberts J.A.;
RT "Temporal and spatial expression of a polygalacturonase during leaf and
RT flower abscission in oilseed rape and Arabidopsis.";
RL Plant Physiol. 128:534-543(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17010199; DOI=10.1186/gb-2006-7-9-r87;
RA Kim J., Shiu S.-H., Thoma S., Li W.-H., Patterson S.E.;
RT "Patterns of expansion and expression divergence in the plant
RT polygalacturonase gene family.";
RL Genome Biol. 7:R87.1-R87.14(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17928369; DOI=10.1093/jxb/erm222;
RA Gonzalez-Carranza Z.H., Elliott K.A., Roberts J.A.;
RT "Expression of polygalacturonases and evidence to support their role during
RT cell separation processes in Arabidopsis thaliana.";
RL J. Exp. Bot. 58:3719-3730(2007).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19168715; DOI=10.1105/tpc.108.063768;
RA Ogawa M., Kay P., Wilson S., Swain S.M.;
RT "ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE1 (ADPG1), ADPG2, and
RT QUARTET2 are polygalacturonases required for cell separation during
RT reproductive development in Arabidopsis.";
RL Plant Cell 21:216-233(2009).
CC -!- FUNCTION: Polygalacturonase involved in cell separation in the final
CC stages of pod shatter, in anther dehiscence and in floral organ
CC abscission. {ECO:0000269|PubMed:17928369, ECO:0000269|PubMed:19168715}.
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, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and in the abscission zone of
CC the sepals, petals and stamens of flowers, at the base of cauline
CC leaves and in the basal cell of trichomes from senescing leaves. Found
CC at the site of lateral root emergence, in the dehiscence zone of
CC anthers and maturing siliques. Also expressed early in anther
CC development, at the time of microspore separation. Expressed in
CC germinating seeds, at the point at which the radicle broke through the
CC seed coat. Not expressed at the junction between the seed and the
CC funiculus or in the dehiscence zone of anthers or pods.
CC {ECO:0000269|PubMed:11842157, ECO:0000269|PubMed:17010199,
CC ECO:0000269|PubMed:17928369, ECO:0000269|PubMed:19168715}.
CC -!- INDUCTION: Up-regulated by ethylene. {ECO:0000269|PubMed:11842157,
CC ECO:0000269|PubMed:17928369}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Small delay in floral organ shedding.
CC {ECO:0000269|PubMed:17928369, ECO:0000269|PubMed:19168715}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002339; AAC02763.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10040.1; -; Genomic_DNA.
DR EMBL; AY078936; AAL84942.1; -; mRNA.
DR EMBL; AF083793; AAN60351.1; -; mRNA.
DR PIR; H84846; H84846.
DR RefSeq; NP_850359.1; NM_180028.3.
DR AlphaFoldDB; Q8RY29; -.
DR SMR; Q8RY29; -.
DR STRING; 3702.AT2G41850.1; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; Q8RY29; -.
DR PRIDE; Q8RY29; -.
DR ProteomicsDB; 244832; -.
DR EnsemblPlants; AT2G41850.1; AT2G41850.1; AT2G41850.
DR GeneID; 818785; -.
DR Gramene; AT2G41850.1; AT2G41850.1; AT2G41850.
DR KEGG; ath:AT2G41850; -.
DR Araport; AT2G41850; -.
DR TAIR; locus:2054396; AT2G41850.
DR eggNOG; ENOG502QRJW; Eukaryota.
DR HOGENOM; CLU_016031_2_3_1; -.
DR InParanoid; Q8RY29; -.
DR OMA; DISKWIM; -.
DR OrthoDB; 1028572at2759; -.
DR PhylomeDB; Q8RY29; -.
DR BioCyc; ARA:AT2G41850-MON; -.
DR PRO; PR:Q8RY29; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RY29; baseline and differential.
DR Genevisible; Q8RY29; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:TAIR.
DR GO; GO:0009901; P:anther dehiscence; IMP:TAIR.
DR GO; GO:0009830; P:cell wall modification involved in abscission; TAS:TAIR.
DR GO; GO:0010227; P:floral organ abscission; IMP:TAIR.
DR GO; GO:0010047; P:fruit dehiscence; IMP:TAIR.
DR GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
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; Glycosidase; Hydrolase;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..433
FT /note="Polygalacturonase ADPG2"
FT /id="PRO_0000367914"
FT REPEAT 223..249
FT /note="PbH1 1"
FT REPEAT 250..271
FT /note="PbH1 2"
FT REPEAT 273..293
FT /note="PbH1 3"
FT REPEAT 303..324
FT /note="PbH1 4"
FT REPEAT 332..353
FT /note="PbH1 5"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CONFLICT 5
FT /note="T -> S (in Ref. 4; AAN60351)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="F -> L (in Ref. 3; AAL84942)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> G (in Ref. 4; AAN60351)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="N -> S (in Ref. 4; AAN60351)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Q -> P (in Ref. 4; AAN60351)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="K -> Q (in Ref. 4; AAN60351)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Y -> D (in Ref. 3; AAL84942)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> G (in Ref. 3; AAL84942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 46623 MW; 11311B0DBE3FCD2D CRC64;
MARCTNLVTV FLLWALLMFS WCKASRISPN VYDHSYKRFK SDSLIKRRED ITGLRSFVRA
SLRTPTTVSV SDFGAKGDGK TDDTQAFVNA WKKACSSNGA VNLLVPKGNT YLLKSIQLTG
PCNSILTVQI FGTLSASQKR SDYKDISKWI MFDGVNNLSV DGGDTGVVDG NGETWWQNSC
KRNKAKPCTK APTALTFYNS KSLIVKNLKV RNAQQIQISI EKCSNVQVSN VVVTAPADSP
NTDGIHITNT QNIRVSESII GTGDDCISIE SGSQNVQIND ITCGPGHGIS IGSLGDDNSK
AFVSGVTVDG AKLSGTDNGV RIKTYQGGSG TASNIIFQNI QMDNVKNPII IDQDYCDKSK
CTTEKSAVQV KNVVYRDISG TSASENAITF NCSKNYPCQG IVLDRVNIKG GKATCTNANV
VDKGAVLPQC NST
