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 05-OCT-2016, entry version 92. 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|TAIR:AT1G70370}; GN ORFNames=F17O7.9 {ECO:0000312|EMBL:AAC18803.1}; 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 [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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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., RA Hayashizaki Y., 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 RT leaves 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 RT to the protein storage vacuoles and overexpression of the cognate gene RT distorts 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 RT cell wall and promotes cell enlargement."; RL Front. Plant Sci. 6:412-412(2015). CC -!- FUNCTION: Involved in cell size determination. May serve as a CC chaperone 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 CC sacs, 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 CC for 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 CC petioles. {ECO:0000269|PubMed:26106400}. CC -!- MISCELLANEOUS: Unlike the tomato GP1, the BURP domain of AtPGL3 is CC not cleaved when the protein is secreted to the cell wall. CC {ECO:0000269|PubMed:26106400}. CC -!- SIMILARITY: Contains 1 BURP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00604}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL08244.1; Type=Frameshift; Positions=515; Evidence={ECO:0000305}; CC Sequence=AAN18083.1; Type=Frameshift; Positions=515, 620; 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; 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_105705.3. DR UniGene; At.10202; -. DR UniGene; At.73052; -. DR UniGene; At.75232; -. DR ProteinModelPortal; P92990; -. DR SMR; P92990; 435-493, 439-515. DR STRING; 3702.AT1G70370.1; -. DR PaxDb; P92990; -. DR PRIDE; P92990; -. 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 TAIR; AT1G70370; -. DR eggNOG; ENOG410IK7R; Eukaryota. DR eggNOG; ENOG410YDAC; LUCA. DR HOGENOM; HOG000082581; -. DR InParanoid; P92990; -. DR OMA; NTFKGYA; -. DR OrthoDB; EOG09360493; -. 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:0005618; C:cell wall; 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; Complete proteome; Glycoprotein; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 626 Polygalacturonase 1 beta-like protein 3. FT /FTId=PRO_0000042954. FT REPEAT 117 120 FXXY 1. {ECO:0000305}. FT REPEAT 125 128 FXXY 2. {ECO:0000305}. FT REPEAT 139 142 FXXY 3. {ECO:0000305}. FT REPEAT 153 156 FXXY 4. {ECO:0000305}. FT REPEAT 167 170 FXXY 5. {ECO:0000305}. FT REPEAT 181 184 FXXY 6. {ECO:0000305}. FT REPEAT 195 198 FXXY 7. {ECO:0000305}. FT REPEAT 209 212 FXXY 8. {ECO:0000305}. FT REPEAT 223 226 FXXY 9. {ECO:0000305}. FT REPEAT 238 241 FXXY 10. {ECO:0000305}. FT REPEAT 252 255 FXXY 11. {ECO:0000305}. FT REPEAT 266 269 FXXY 12. {ECO:0000305}. FT REPEAT 280 283 FXXY 13. {ECO:0000305}. FT REPEAT 294 297 FXXY 14. {ECO:0000305}. FT REPEAT 308 311 FXXY 15. {ECO:0000305}. FT REPEAT 322 325 FXXY 16. {ECO:0000305}. FT REPEAT 336 339 FXXY 17. {ECO:0000305}. FT REPEAT 350 353 FXXY 18. {ECO:0000305}. FT REPEAT 364 367 FXXY 19. {ECO:0000305}. FT REPEAT 373 376 FXXY 20. {ECO:0000305}. FT REPEAT 383 386 FXXY 21. {ECO:0000305}. FT DOMAIN 411 625 BURP. {ECO:0000255|PROSITE- FT ProRule:PRU00604}. FT CARBOHYD 124 124 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 141 141 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 277 277 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 370 370 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 387 387 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 465 465 N-linked (GlcNAc...). {ECO:0000255}. FT CONFLICT 70 70 A -> S (in Ref. 6; AAN60310). FT {ECO:0000305}. FT CONFLICT 242 242 G -> A (in Ref. 1; AAB39546). FT {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 //