PGL3_ARATH
ID PGL3_ARATH Reviewed; 626 AA.
AC P92990; O64599; Q0WV83; Q8H7B8; Q93ZQ4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Polygalacturonase 1 beta-like protein 3 {ECO:0000303|PubMed:26106400};
DE Short=AtPGL3 {ECO:0000303|PubMed:26106400};
DE AltName: Full=Aromatic-rich glycoprotein JP650;
DE AltName: Full=PG1beta-like protein 3 {ECO:0000303|PubMed:26106400};
DE AltName: Full=Polygalacturonase 2 {ECO:0000303|PubMed:19639386};
DE AltName: Full=Probable polygalacturonase non-catalytic subunit JP650;
DE Flags: Precursor;
GN Name=PGL3 {ECO:0000303|PubMed:26106400};
GN Synonyms=JP650, PG2 {ECO:0000303|PubMed:19639386};
GN OrderedLocusNames=At1g70370 {ECO:0000312|Araport:AT1G70370};
GN ORFNames=F17O7.9 {ECO:0000312|EMBL:AAC18803.1};
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 [MRNA].
RA Watson C.F., Schuchman B., Liu J., DellaPenna D.;
RT "Arabidopsis aromatic rich glycoprotein JP650.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226.
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 [7]
RP DOMAIN.
RX PubMed=9790599; DOI=10.1007/s004380050832;
RA Hattori J., Boutilier K.A., van Lookeren Campagne M.M., Miki B.L.;
RT "A conserved BURP domain defines a novel group of plant proteins with
RT unusual primary structures.";
RL Mol. Gen. Genet. 259:424-428(1998).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19639386; DOI=10.1007/s11103-009-9526-6;
RA Van Son L., Tiedemann J., Rutten T., Hillmer S., Hinz G., Zank T.,
RA Manteuffel R., Baeumlein H.;
RT "The BURP domain protein AtUSPL1 of Arabidopsis thaliana is destined to the
RT protein storage vacuoles and overexpression of the cognate gene distorts
RT seed development.";
RL Plant Mol. Biol. 71:319-329(2009).
RN [9]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=26106400; DOI=10.3389/fpls.2015.00412;
RA Park J., Cui Y., Kang B.H.;
RT "AtPGL3 is an Arabidopsis BURP domain protein that is localized to the cell
RT wall and promotes cell enlargement.";
RL Front. Plant Sci. 6:412-412(2015).
CC -!- FUNCTION: Involved in cell size determination. May serve as a chaperone
CC for expansins through the secretory pathway.
CC {ECO:0000269|PubMed:26106400}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:26106400}. Secreted, cell wall
CC {ECO:0000269|PubMed:26106400}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and stems. Detected in
CC trichomes, guard cells, root vascular tissue, root hairs, pollen sacs,
CC sepals and styles of pistils. {ECO:0000269|PubMed:26106400}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable in 6 days after-germination
CC (DAG) seedlings, but highly expressed in 14 DAG seedlings.
CC {ECO:0000269|PubMed:26106400}.
CC -!- DOMAIN: The BURP domain located at the C-terminus has not been
CC identified in non-plant proteins (PubMed:9790599). It is critical for
CC PGL3's role in cell growth (PubMed:26106400).
CC {ECO:0000269|PubMed:26106400, ECO:0000269|PubMed:9790599}.
CC -!- DISRUPTION PHENOTYPE: Slightly reduced size of the plant. Atpgl1,
CC atpgl2 and atpgl3 triple mutants produce smaller leaves and petioles.
CC {ECO:0000269|PubMed:26106400}.
CC -!- MISCELLANEOUS: Unlike the tomato GP1, the BURP domain of AtPGL3 is not
CC cleaved when the protein is secreted to the cell wall.
CC {ECO:0000269|PubMed:26106400}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL08244.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAN18083.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U63373; AAB39546.1; -; mRNA.
DR EMBL; AC003671; AAC18803.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35050.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35051.1; -; Genomic_DNA.
DR EMBL; AY056388; AAL08244.1; ALT_FRAME; mRNA.
DR EMBL; BT000514; AAN18083.1; ALT_FRAME; mRNA.
DR EMBL; AK226888; BAE98965.1; -; mRNA.
DR EMBL; AF083752; AAN60310.1; -; mRNA.
DR PIR; T01485; T01485.
DR RefSeq; NP_001185361.1; NM_001198432.1.
DR RefSeq; NP_177194.1; NM_105705.4.
DR AlphaFoldDB; P92990; -.
DR STRING; 3702.AT1G70370.1; -.
DR PaxDb; P92990; -.
DR PRIDE; P92990; -.
DR ProteomicsDB; 236724; -.
DR EnsemblPlants; AT1G70370.1; AT1G70370.1; AT1G70370.
DR EnsemblPlants; AT1G70370.2; AT1G70370.2; AT1G70370.
DR GeneID; 843373; -.
DR Gramene; AT1G70370.1; AT1G70370.1; AT1G70370.
DR Gramene; AT1G70370.2; AT1G70370.2; AT1G70370.
DR KEGG; ath:AT1G70370; -.
DR Araport; AT1G70370; -.
DR TAIR; locus:2016194; AT1G70370.
DR eggNOG; ENOG502QT2V; Eukaryota.
DR HOGENOM; CLU_011822_5_0_1; -.
DR InParanoid; P92990; -.
DR OMA; MSKMEVS; -.
DR OrthoDB; 724379at2759; -.
DR PhylomeDB; P92990; -.
DR PRO; PR:P92990; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92990; baseline and differential.
DR Genevisible; P92990; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0042547; P:cell wall modification involved in multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009827; P:plant-type cell wall modification; IMP:TAIR.
DR InterPro; IPR004873; BURP_dom.
DR Pfam; PF03181; BURP; 1.
DR SMART; SM01045; BURP; 1.
DR PROSITE; PS51277; BURP; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Cell wall; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..626
FT /note="Polygalacturonase 1 beta-like protein 3"
FT /id="PRO_0000042954"
FT REPEAT 117..120
FT /note="FXXY 1"
FT /evidence="ECO:0000305"
FT REPEAT 125..128
FT /note="FXXY 2"
FT /evidence="ECO:0000305"
FT REPEAT 139..142
FT /note="FXXY 3"
FT /evidence="ECO:0000305"
FT REPEAT 153..156
FT /note="FXXY 4"
FT /evidence="ECO:0000305"
FT REPEAT 167..170
FT /note="FXXY 5"
FT /evidence="ECO:0000305"
FT REPEAT 181..184
FT /note="FXXY 6"
FT /evidence="ECO:0000305"
FT REPEAT 195..198
FT /note="FXXY 7"
FT /evidence="ECO:0000305"
FT REPEAT 209..212
FT /note="FXXY 8"
FT /evidence="ECO:0000305"
FT REPEAT 223..226
FT /note="FXXY 9"
FT /evidence="ECO:0000305"
FT REPEAT 238..241
FT /note="FXXY 10"
FT /evidence="ECO:0000305"
FT REPEAT 252..255
FT /note="FXXY 11"
FT /evidence="ECO:0000305"
FT REPEAT 266..269
FT /note="FXXY 12"
FT /evidence="ECO:0000305"
FT REPEAT 280..283
FT /note="FXXY 13"
FT /evidence="ECO:0000305"
FT REPEAT 294..297
FT /note="FXXY 14"
FT /evidence="ECO:0000305"
FT REPEAT 308..311
FT /note="FXXY 15"
FT /evidence="ECO:0000305"
FT REPEAT 322..325
FT /note="FXXY 16"
FT /evidence="ECO:0000305"
FT REPEAT 336..339
FT /note="FXXY 17"
FT /evidence="ECO:0000305"
FT REPEAT 350..353
FT /note="FXXY 18"
FT /evidence="ECO:0000305"
FT REPEAT 364..367
FT /note="FXXY 19"
FT /evidence="ECO:0000305"
FT REPEAT 373..376
FT /note="FXXY 20"
FT /evidence="ECO:0000305"
FT REPEAT 383..386
FT /note="FXXY 21"
FT /evidence="ECO:0000305"
FT DOMAIN 411..625
FT /note="BURP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00604"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 70
FT /note="A -> S (in Ref. 6; AAN60310)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="G -> A (in Ref. 1; AAB39546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 68060 MW; F324231B27D4B710 CRC64;
MLKQFLLLQS FSFFLFNVVI VGGRTFGGGF SAEENPFTPK ASLVRYWNKE IRGQSPRSEF
LISKASPLNA VDSATFSKLA AANSLPTRFP DFCSAANLFC FPDLGASLEK HDDDVKFSVY
DQKNFTNYGN ARAGGADSFK NYSKDGNVVT DSFRRYSRNA AGHDDKFTVY GENSNVVEEG
FNSYGTFGTG GAGDFTNYQN NVNNPTSRFT AYSDGGNGRS QTFKTYTHEA NAGNGQSFTS
YGKNGNGVPN EFTSYGVSSN VIGSGFSNYG ESGNAANDTF TSYGSDGNVP QNNFNNYGAS
GNAAVDTFAN YRDKANVGDD SFSSYAKDSN SEKVNFVNYG QSFNPGSETF TGYGKGAEGS
KLSFKTYTPN STFKDYAKKG VAFAKYNVST TTANTVGDGK TVNKWIEPGK FFRESSLKEG
TVIPMPDIKD KMPKRSFLPR SIITKLPFST SKLGEIKRIF HAVENSTMGG IITDAVTECE
RPPSVGETKR CVGSAEDMID FATSVLGRSV VLRTTENVAG SKEKVVIGKV NGINGGKLTK
AVSCHQSLYP YLLYYCHSVP KVRVYEADLL ELNSKKKINH GIAICHMDTS SWGPSHGAFL
ALGSKPGRIE VCHWIFENDM NWAIAD
