PGLR4_ARATH
ID PGLR4_ARATH Reviewed; 475 AA.
AC Q949Z1; Q94EH4; Q9LNG3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Polygalacturonase At1g48100;
DE Short=PG;
DE EC=3.2.1.15;
DE AltName: Full=Pectinase At1g48100;
DE Flags: Precursor;
GN OrderedLocusNames=At1g48100; ORFNames=F21D18.17, F21D18.18;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 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 [5]
RP FUNCTION.
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 not involved in the final stages of pod
CC shatter. {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 flowers and stems.
CC {ECO:0000269|PubMed:17010199}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC023673; AAF79535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32248.1; -; Genomic_DNA.
DR EMBL; AF410319; AAK95305.1; -; mRNA.
DR EMBL; AY050798; AAK92733.1; -; mRNA.
DR EMBL; AY096360; AAM20001.1; -; mRNA.
DR PIR; C96521; C96521.
DR RefSeq; NP_175244.1; NM_103706.4.
DR AlphaFoldDB; Q949Z1; -.
DR SMR; Q949Z1; -.
DR STRING; 3702.AT1G48100.1; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; Q949Z1; -.
DR PRIDE; Q949Z1; -.
DR ProteomicsDB; 236673; -.
DR EnsemblPlants; AT1G48100.1; AT1G48100.1; AT1G48100.
DR GeneID; 841228; -.
DR Gramene; AT1G48100.1; AT1G48100.1; AT1G48100.
DR KEGG; ath:AT1G48100; -.
DR Araport; AT1G48100; -.
DR TAIR; locus:2023817; AT1G48100.
DR eggNOG; ENOG502QPYK; Eukaryota.
DR HOGENOM; CLU_016031_2_1_1; -.
DR InParanoid; Q949Z1; -.
DR OMA; KSNQMYM; -.
DR OrthoDB; 601945at2759; -.
DR PhylomeDB; Q949Z1; -.
DR BioCyc; ARA:AT1G48100-MON; -.
DR PRO; PR:Q949Z1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q949Z1; baseline and differential.
DR Genevisible; Q949Z1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009831; P:plant-type cell wall modification involved in multidimensional cell growth; 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; 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..475
FT /note="Polygalacturonase At1g48100"
FT /id="PRO_0000367916"
FT REPEAT 241..267
FT /note="PbH1 1"
FT REPEAT 268..289
FT /note="PbH1 2"
FT REPEAT 291..311
FT /note="PbH1 3"
FT REPEAT 321..342
FT /note="PbH1 4"
FT REPEAT 350..371
FT /note="PbH1 5"
FT REGION 35..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CONFLICT 123
FT /note="K -> R (in Ref. 3; AAK95305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 51353 MW; ACB066CF725F2C8F CRC64;
MRRLSGILVI YIISTVLFGH FTNVARARYH YHKGRHGVTH PLPPPPPPPL ETANPPDQVP
SDPYPSPDPA PGDSDSGCVF DVTSFGAVGD GSCDDTAAFQ DAWKAACAVE SGVVLAPEGG
VFKITSTIFS GPCKPGLVFQ LDGVLMPPDG PEEWPEKDNK NQWLVFYRLD GFTFSGKGTV
EGNGQKWWDL PCKPHRGPDG SSSSGPCASP TMIRFFMSNN IEVKGLRIQN SPQFHMKFDG
CQGVLINEIQ ISSPKLSPNT DGIHLGNTRS VGIYNSVVSN GDDCISIGTG CSDVDIQGVT
CGPSHGISIG SLGVHNSQAC VSNITVRNTV IRDSDNGLRV KTWQGGTGSV SNLLFENIQM
ENVLNCIIVD QYYCQSKDCR NETSAVKVFD VEYRNIKGTY DVRSPPIHFA CSDTVACTNI
TMSEVELLPE EGELVDDPFC WNAYGKQETL TIPPIDCLLD GSPVVEEAYD SNYGC
