PGL2_ARATH
ID PGL2_ARATH Reviewed; 624 AA.
AC O80760; Q0WTJ0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Polygalacturonase 1 beta-like protein 2 {ECO:0000303|PubMed:26106400};
DE Short=AtPGL2 {ECO:0000303|PubMed:26106400};
DE AltName: Full=Aromatic-rich glycoprotein At1g60390;
DE AltName: Full=PG1beta-like protein 2 {ECO:0000303|PubMed:26106400};
DE AltName: Full=Polygalacturonase 1 {ECO:0000303|PubMed:19639386};
DE AltName: Full=Probable polygalacturonase non-catalytic subunit At1g60390;
DE Flags: Precursor;
GN Name=PGL2 {ECO:0000303|PubMed:26106400};
GN Synonyms=PG1 {ECO:0000303|PubMed:19639386};
GN OrderedLocusNames=At1g60390 {ECO:0000312|Araport:AT1G60390};
GN ORFNames=T13D8.26 {ECO:0000312|EMBL:AAC24065.1};
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 [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;
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 [4]
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 [5]
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 [6]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
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.
CC {ECO:0000250|UniProtKB:P92990}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:P92990}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P92990}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and stems.
CC {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. {ECO:0000269|PubMed:9790599}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Atpgl1, atpgl2 and atpgl3
CC triple mutants produce smaller leaves and petioles.
CC {ECO:0000269|PubMed:26106400}.
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DR EMBL; AC004473; AAC24065.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33681.1; -; Genomic_DNA.
DR EMBL; AK227564; BAE99558.1; -; mRNA.
DR PIR; T02289; T02289.
DR RefSeq; NP_176242.1; NM_104726.3.
DR AlphaFoldDB; O80760; -.
DR STRING; 3702.AT1G60390.1; -.
DR PaxDb; O80760; -.
DR PRIDE; O80760; -.
DR ProteomicsDB; 234903; -.
DR EnsemblPlants; AT1G60390.1; AT1G60390.1; AT1G60390.
DR GeneID; 842334; -.
DR Gramene; AT1G60390.1; AT1G60390.1; AT1G60390.
DR KEGG; ath:AT1G60390; -.
DR Araport; AT1G60390; -.
DR TAIR; locus:2195593; AT1G60390.
DR eggNOG; ENOG502QT2V; Eukaryota.
DR HOGENOM; CLU_011822_5_0_1; -.
DR InParanoid; O80760; -.
DR OMA; LWFPRST; -.
DR OrthoDB; 724379at2759; -.
DR PhylomeDB; O80760; -.
DR PRO; PR:O80760; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80760; baseline and differential.
DR Genevisible; O80760; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..624
FT /note="Polygalacturonase 1 beta-like protein 2"
FT /id="PRO_0000042957"
FT REPEAT 121..124
FT /note="FXXY 1"
FT /evidence="ECO:0000305"
FT REPEAT 129..132
FT /note="FXXY 2"
FT /evidence="ECO:0000305"
FT REPEAT 143..146
FT /note="FXXY 3"
FT /evidence="ECO:0000305"
FT REPEAT 157..160
FT /note="FXXY 4"
FT /evidence="ECO:0000305"
FT REPEAT 171..174
FT /note="FXXY 5"
FT /evidence="ECO:0000305"
FT REPEAT 185..188
FT /note="FXXY 6"
FT /evidence="ECO:0000305"
FT REPEAT 199..202
FT /note="FXXY 7"
FT /evidence="ECO:0000305"
FT REPEAT 213..216
FT /note="FXXY 8"
FT /evidence="ECO:0000305"
FT REPEAT 227..230
FT /note="FXXY 9"
FT /evidence="ECO:0000305"
FT REPEAT 241..244
FT /note="FXXY 10"
FT /evidence="ECO:0000305"
FT REPEAT 255..258
FT /note="FXXY 11"
FT /evidence="ECO:0000305"
FT REPEAT 269..272
FT /note="FXXY 12"
FT /evidence="ECO:0000305"
FT REPEAT 283..286
FT /note="FXXY 13"
FT /evidence="ECO:0000305"
FT REPEAT 297..300
FT /note="FXXY 14"
FT /evidence="ECO:0000305"
FT REPEAT 311..314
FT /note="FXXY 15"
FT /evidence="ECO:0000305"
FT REPEAT 325..328
FT /note="FXXY 16"
FT /evidence="ECO:0000305"
FT REPEAT 339..342
FT /note="FXXY 17"
FT /evidence="ECO:0000305"
FT REPEAT 353..356
FT /note="FXXY 18"
FT /evidence="ECO:0000305"
FT REPEAT 367..370
FT /note="FXXY 19"
FT /evidence="ECO:0000305"
FT REPEAT 376..379
FT /note="FXXY 20"
FT /evidence="ECO:0000305"
FT REPEAT 386..389
FT /note="FXXY 21"
FT /evidence="ECO:0000305"
FT DOMAIN 409..623
FT /note="BURP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00604"
FT REGION 199..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 624 AA; 67762 MW; 4CAAD8858A374F08 CRC64;
MNNIEATLFL CFFCIFSSSN VHFAGAKQTA GNITPSENPF TPKASLIRYW NNHINGDSPK
PSFFLSKASP LTAVDSTRFA SLASNHALNT HHSDFCSAAK LFCFPELAAH SLEKHGDDVN
FAAYSGKNFT NYGSDRLSGA DSFKNYSGGD NIAVDSFRRY SRNSAGHDDG FTNYAGEVNV
ADQSFTTYAT GTTGGSGEFT NYNTDANEPN GRFTSYSDKA NGRSQTFTTY SENGNTGYQS
FTSYSKNGNG APNEFSGYGT GSNVVNTGFT KYGESANGAN DSFTSYGENG NVPVNEFKGY
GDGGNGAVYG FKNYRDQSNI GVDSFSSYAK NSNNEKVNFV NYGKSFNLGS DNFTGYGQDN
VGGNVSFKTY GQGQSFKVYT KDGVVFARYS NNVSSNGKTV NKWVEEGKFF REAMLKEGTL
MQMPDIKDKM PKRTFLPRNI VKNLPFSSST IGEIWRVFGA GENSSMAGII SSAVSECERP
ASHGETKRCV GSAEDMIDFA TSVLGRGVVV RTTENVVGSK KKVVIGKVNG INGGDVTRAV
SCHQSLYPYL LYYCHSVPRV RVYETDLLDP KSLEKINHGV AICHIDTSAW SPSHGAFLAL
GSGPGQIEVC HWIFENDMTW NIID
