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ADPG1_ARATH
ID   ADPG1_ARATH             Reviewed;         431 AA.
AC   O23147;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Polygalacturonase ADPG1;
DE            Short=AtADPG1;
DE            Short=PG ADPG1;
DE            EC=3.2.1.15;
DE   AltName: Full=Pectinase ADPG1;
DE   AltName: Full=Protein ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 1;
DE   Flags: Precursor;
GN   Name=ADPG1; Synonyms=PGDZAT, SAC70; OrderedLocusNames=At3g57510;
GN   ORFNames=T8H10.110;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   DOI=10.1046/j.1365-3040.1999.00372.x;
RA   Jenkins E.S., Paul W., Craze M., Whitelaw C.A., Weigand A., Roberts J.A.;
RT   "Dehiscence-related expression of an Arabidopsis thaliana gene encoding a
RT   polygalacturonase in transgenic plants of Brassica napus.";
RL   Plant Cell Environ. 22:159-167(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11485203; DOI=10.1023/a:1010619002833;
RA   Sander L., Child R., Ulvskov P., Albrechtsen M., Borkhardt B.;
RT   "Analysis of a dehiscence zone endo-polygalacturonase in oilseed rape
RT   (Brassica napus) and Arabidopsis thaliana: evidence for roles in cell
RT   separation in dehiscence and abscission zones, and in stylar tissues during
RT   pollen tube growth.";
RL   Plant Mol. Biol. 46:469-479(2001).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
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   [7]
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   [8]
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   [9]
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 and in anther dehiscence. Not involved in floral
CC       organ abscission. {ECO:0000269|PubMed:17928369,
CC       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
CC       {ECO:0000269|PubMed:11485203}. Cytoplasm {ECO:0000269|PubMed:11485203}.
CC       Note=Released to the cell wall during maturation of the dehiscence
CC       zone.
CC   -!- TISSUE SPECIFICITY: Expressed in flower buds and siliques, in the
CC       dehiscence zone of anthers (stomium cells) and maturing siliques.
CC       Expressed in stigma during pollen tube growth. Not expressed in seeds
CC       or in the floral part or leaf abscission zone but found at the junction
CC       between the seed and the funiculus at the site of seed abscission.
CC       {ECO:0000269|PubMed:11485203, ECO:0000269|PubMed:17010199,
CC       ECO:0000269|PubMed:17928369, ECO:0000269|PubMed:19168715,
CC       ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: Impaired pod shatter.
CC       {ECO:0000269|PubMed:19168715}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR   EMBL; AF037367; AAC98923.1; -; Genomic_DNA.
DR   EMBL; AJ002532; CAA05525.1; -; Genomic_DNA.
DR   EMBL; AL133248; CAB66108.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79664.1; -; Genomic_DNA.
DR   EMBL; AK117942; BAC42580.1; -; mRNA.
DR   EMBL; BT005376; AAO63440.1; -; mRNA.
DR   PIR; T46187; T46187.
DR   RefSeq; NP_191310.1; NM_115611.2.
DR   AlphaFoldDB; O23147; -.
DR   SMR; O23147; -.
DR   STRING; 3702.AT3G57510.1; -.
DR   CAZy; GH28; Glycoside Hydrolase Family 28.
DR   PaxDb; O23147; -.
DR   PRIDE; O23147; -.
DR   ProteomicsDB; 244799; -.
DR   EnsemblPlants; AT3G57510.1; AT3G57510.1; AT3G57510.
DR   GeneID; 824918; -.
DR   Gramene; AT3G57510.1; AT3G57510.1; AT3G57510.
DR   KEGG; ath:AT3G57510; -.
DR   Araport; AT3G57510; -.
DR   TAIR; locus:2103478; AT3G57510.
DR   eggNOG; ENOG502QRJW; Eukaryota.
DR   HOGENOM; CLU_016031_2_3_1; -.
DR   InParanoid; O23147; -.
DR   OMA; FKPGANY; -.
DR   OrthoDB; 1028572at2759; -.
DR   PhylomeDB; O23147; -.
DR   BioCyc; ARA:AT3G57510-MON; -.
DR   PRO; PR:O23147; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O23147; baseline and differential.
DR   Genevisible; O23147; AT.
DR   GO; GO:0005737; C:cytoplasm; 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; 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; Cytoplasm; Glycosidase;
KW   Hydrolase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..431
FT                   /note="Polygalacturonase ADPG1"
FT                   /id="PRO_0000367913"
FT   REPEAT          223..249
FT                   /note="PbH1 1"
FT   REPEAT          250..271
FT                   /note="PbH1 2"
FT   REPEAT          303..324
FT                   /note="PbH1 3"
FT   REPEAT          332..353
FT                   /note="PbH1 4"
FT   REPEAT          398..420
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"
SQ   SEQUENCE   431 AA;  46572 MW;  0F0F30DF45804FE7 CRC64;
     MARCCRHLAV FLCVLLMLSL CKALSSNVDD GYGHEDGSFE SDSLLKLNND DVLSLISSDE
     TTLEASTVSV SNFGAKGDGK TDDTQAFKKA WKKACSTNGV TTFLVPKGKT YLLKSTRFRG
     PCKSLRNFQI LGTLSASTKR SDYKDKNHWL ILEDVNNLSI DGGSTGIING NGKTWWQNSC
     KIDKSKPCTK APTALTLYNL KNLNVKNLRV KNAQQIQISI EKCNKVEVSN VEITAPGDSP
     NTDGIHITNT QNIRVSNSDI GTGDDCISIE DGTQNLQIFD LTCGPGHGIS IGSLGDDNSK
     AYVSGINVDG AKFSESDNGV RIKTYQGGSG TAKNIKFQNI RMENVKNPII IDQDYCDKDK
     CEDQESAVQV KNVVYKNISG TSATDVAITL NCSEKYPCQG IVLENVKIKG GTASCKNANV
     KNQGTVSPKC S
 
 
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