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Database: UniProt
Entry: Q9SFB7
LinkDB: Q9SFB7
Original site: Q9SFB7 
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   19-MAR-2014, entry version 83.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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
RT   (QRT) 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
RT   in 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
RT   during 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
CC       and floral organ abscission.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-alpha-D-
CC       galactosiduronic linkages in pectate and other galacturonans.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in roots with lower
CC       expression levels in rosette leaves, flower buds and siliques.
CC       Bearly detected in seeds. Found in flowers undergoing floral organ
CC       abscission. Also expressed early in anther development, at the
CC       time of microspore separation.
CC   -!- DISRUPTION PHENOTYPE: The mature pollen grains are arranged in a
CC       tetrad. No visible phenotype regarding floral organ abscission.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC   -!- SIMILARITY: Contains 4 PbH1 repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF21207.1; Type=Erroneous gene model prediction;
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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_111676.3.
DR   UniGene; At.40276; -.
DR   ProteinModelPortal; Q9SFB7; -.
DR   SMR; Q9SFB7; 83-428.
DR   STRING; 3702.AT3G07970.1-P; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PRIDE; Q9SFB7; -.
DR   EnsemblPlants; AT3G07970.1; AT3G07970.1; AT3G07970.
DR   GeneID; 819988; -.
DR   KEGG; ath:AT3G07970; -.
DR   TAIR; AT3G07970; -.
DR   eggNOG; COG5434; -.
DR   HOGENOM; HOG000237792; -.
DR   InParanoid; Q9SFB7; -.
DR   OMA; KANGNDD; -.
DR   PhylomeDB; Q9SFB7; -.
DR   ProtClustDB; CLSN2690525; -.
DR   BioCyc; ARA:AT3G07970-MONOMER; -.
DR   Genevestigator; Q9SFB7; -.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
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; Complete proteome;
KW   Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    439       Polygalacturonase QRT2.
FT                                /FTId=PRO_0000367915.
FT   REPEAT      201    250       PbH1 1.
FT   REPEAT      251    272       PbH1 2.
FT   REPEAT      304    325       PbH1 3.
FT   REPEAT      333    354       PbH1 4.
FT   ACT_SITE    265    265       Proton donor (By similarity).
FT   ACT_SITE    288    288       By similarity.
FT   MUTAGEN     372    372       V->A: In qrt2-1; loss of function.
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
//
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