ID   QRT2_ARATH              Reviewed;         439 AA.
AC   Q9SFB7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Polygalacturonase QRT2;
DE            Short=AtQRT2;
DE            Short=PG QRT2;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase QRT2;
DE   AltName: Full=Protein QUARTET 2;
DE   Flags: Precursor;
GN   Name=QRT2; OrderedLocusNames=At3g07970; ORFNames=F17A17.31;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   FUNCTION, AND MUTAGENESIS OF VAL-372.
RX   PubMed=8197459; DOI=10.1126/science.8197459;
RA   Preuss D., Rhee S.Y., Davis R.W.;
RT   "Tetrad analysis possible in Arabidopsis with mutation of the QUARTET (QRT)
RT   genes.";
RL   Science 264:1458-1460(1994).
RN   [4]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RA   Kim J., Patterson S.E.;
RT   "Expression divergence and functional redundancy of polygalacturonases in
RT   floral organ abscission.";
RL   Plant Signal. Behav. 1:281-283(2006).
RN   [5]
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   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
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   [7]
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 required for cell type-specific pectin
CC       degradation to separate microspores. Involved in anther dehiscence and
CC       floral organ abscission. {ECO:0000269|PubMed:17928369,
CC       ECO:0000269|PubMed:19168715, ECO:0000269|PubMed:8197459}.
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 predominantly in roots with lower
CC       expression levels in rosette leaves, flower buds and siliques. Bearly
CC       detected in seeds. Found in flowers undergoing floral organ abscission.
CC       Also expressed early in anther development, at the time of microspore
CC       separation. {ECO:0000269|PubMed:17010199, ECO:0000269|PubMed:17928369,
CC       ECO:0000269|PubMed:19168715, ECO:0000269|Ref.4}.
CC   -!- DISRUPTION PHENOTYPE: The mature pollen grains are arranged in a
CC       tetrad. No visible phenotype regarding floral organ abscission.
CC       {ECO:0000269|PubMed:19168715, ECO:0000269|Ref.4}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF21207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC013483; AAF21207.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74626.1; -; Genomic_DNA.
DR   RefSeq; NP_187454.2; NM_111676.4.
DR   AlphaFoldDB; Q9SFB7; -.
DR   SMR; Q9SFB7; -.
DR   STRING; 3702.AT3G07970.1; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PaxDb; Q9SFB7; -.
DR   PRIDE; Q9SFB7; -.
DR   ProteomicsDB; 225934; -.
DR   EnsemblPlants; AT3G07970.1; AT3G07970.1; AT3G07970.
DR   GeneID; 819988; -.
DR   Gramene; AT3G07970.1; AT3G07970.1; AT3G07970.
DR   KEGG; ath:AT3G07970; -.
DR   Araport; AT3G07970; -.
DR   TAIR; locus:2077407; AT3G07970.
DR   eggNOG; ENOG502QRJW; Eukaryota.
DR   HOGENOM; CLU_016031_2_3_1; -.
DR   InParanoid; Q9SFB7; -.
DR   OMA; GKFFPQC; -.
DR   OrthoDB; 1028572at2759; -.
DR   PhylomeDB; Q9SFB7; -.
DR   BioCyc; ARA:AT3G07970-MON; -.
DR   PRO; PR:Q9SFB7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SFB7; baseline and differential.
DR   Genevisible; Q9SFB7; 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:0010047; P:fruit dehiscence; IMP:TAIR.
DR   GO; GO:0045490; P:pectin catabolic process; IMP:TAIR.
DR   GO; GO:0048235; P:pollen sperm cell differentiation; IMP:TAIR.
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; 4.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Glycosidase; Hydrolase;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..439
FT                   /note="Polygalacturonase QRT2"
FT                   /id="PRO_0000367915"
FT   REPEAT          201..250
FT                   /note="PbH1 1"
FT   REPEAT          251..272
FT                   /note="PbH1 2"
FT   REPEAT          304..325
FT                   /note="PbH1 3"
FT   REPEAT          333..354
FT                   /note="PbH1 4"
FT   REGION          43..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT   MUTAGEN         372
FT                   /note="V->A: In qrt2-1; loss of function."
FT                   /evidence="ECO:0000269|PubMed:8197459"
SQ   SEQUENCE   439 AA;  48572 MW;  D52F4691C95633A4 CRC64;
     MYEKIIILSV FLLTFLPSCF SSYPFNHRDD LFMSSNVYYE TNRQHQHGHN TRNSHLKNRH
     GYAPRSSPRS FNVNTFGAKA NGNDDSKAFM KAWEAACSST GIVYIVAPKN RDYMLKAVTF
     SGPCKSSLII FKIYGRIEAW ENPSDYKERR HWIVFENVNN LRVEGGGRID GNGHIWWPKS
     CKINPQLPCL GAPTAVTFVE CNNLRVSNIR LENAQQMHLT FQDCKNVKAL NLMVTSPADS
     PNTDGIHVSG TQNILIQDSI VRTGDDCISI VSGSENVRAT GITCGPGHGI SIGSLGEDNS
     EAYVSNVVVN KATLIGTTNG VRIKTWQGGH GMAKNIIFQD IIMKNVTNPI IINQDYCDRV
     EACPEQKSAV QVSNVLYKNI QGTSSRPIAV KFVCSKNIPC RGISMQNVKL VDQTQQDVSK
     ASCSNVKLDT RGNVSPLCT