UGGG_ARATH
ID UGGG_ARATH Reviewed; 1613 AA.
AC Q0WL80; F4I8G1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase;
DE EC=2.4.1.-;
DE AltName: Full=EMS-mutagenized BRI1 suppressor 1;
DE AltName: Full=Protein PRIORITY IN SWEET LIFE 2;
DE Flags: Precursor;
GN Name=UGGT; Synonyms=EBS1, PSL2; OrderedLocusNames=At1g71220;
GN ORFNames=F23N20, F3I17.13;
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] (ISOFORM 1).
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 FUNCTION, MUTAGENESIS OF GLY-1309 AND LEU-1500, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17588517; DOI=10.1016/j.molcel.2007.05.015;
RA Jin H., Yan Z., Nam K.H., Li J.;
RT "Allele-specific suppression of a defective brassinosteroid receptor
RT reveals a physiological role of UGGT in ER quality control.";
RL Mol. Cell 26:821-830(2007).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLU-306 AND ASP-1497, AND DISRUPTION PHENOTYPE.
RX PubMed=19763087; DOI=10.1038/emboj.2009.263;
RA Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H.,
RA Dong X., Robatzek S., Schulze-Lefert P.;
RT "Receptor quality control in the endoplasmic reticulum for plant innate
RT immunity.";
RL EMBO J. 28:3439-3449(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19717464; DOI=10.1073/pnas.0905532106;
RA Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D.,
RA Zipfel C., Jones J.D.;
RT "Specific ER quality control components required for biogenesis of the
RT plant innate immune receptor EFR.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the protein,
CC thus providing quality control for protein folding in the endoplasmic
CC reticulum. Reglucosylated proteins are recognized by calreticulin for
CC recycling to the endoplasmic reticulum and refolding or degradation.
CC Required for elongation factor Tu receptor (EFR), but not flagellin-
CC sensing 2 (FLS2) signaling. {ECO:0000269|PubMed:17588517,
CC ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WL80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WL80-2; Sequence=VSP_041721;
CC -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but activation of the
CC unfolded protein response. Loss of seedling growth inhibition in
CC response to the pathogen-associated molecular pattern (PAMP) elf18.
CC {ECO:0000269|PubMed:17588517, ECO:0000269|PubMed:19717464,
CC ECO:0000269|PubMed:19763087}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AC016162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE35174.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35175.1; -; Genomic_DNA.
DR EMBL; AK230327; BAF02127.1; -; mRNA.
DR RefSeq; NP_001185370.1; NM_001198441.1. [Q0WL80-2]
DR RefSeq; NP_177278.3; NM_105791.5. [Q0WL80-1]
DR AlphaFoldDB; Q0WL80; -.
DR SMR; Q0WL80; -.
DR BioGRID; 28682; 8.
DR STRING; 3702.AT1G71220.2; -.
DR PaxDb; Q0WL80; -.
DR PRIDE; Q0WL80; -.
DR EnsemblPlants; AT1G71220.1; AT1G71220.1; AT1G71220. [Q0WL80-1]
DR EnsemblPlants; AT1G71220.2; AT1G71220.2; AT1G71220. [Q0WL80-2]
DR GeneID; 843462; -.
DR Gramene; AT1G71220.1; AT1G71220.1; AT1G71220. [Q0WL80-1]
DR Gramene; AT1G71220.2; AT1G71220.2; AT1G71220. [Q0WL80-2]
DR KEGG; ath:AT1G71220; -.
DR Araport; AT1G71220; -.
DR TAIR; locus:2032298; AT1G71220.
DR eggNOG; KOG1879; Eukaryota.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; Q0WL80; -.
DR OMA; EFAIDIR; -.
DR PhylomeDB; Q0WL80; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q0WL80; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WL80; baseline and differential.
DR Genevisible; Q0WL80; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR GO; GO:0009751; P:response to salicylic acid; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1613
FT /note="UDP-glucose:glycoprotein glucosyltransferase"
FT /id="PRO_0000412589"
FT REGION 1578..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1261
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041721"
FT MUTAGEN 306
FT /note="E->K: In psl2-2; loss of response to the PAMP
FT elf18."
FT /evidence="ECO:0000269|PubMed:19763087"
FT MUTAGEN 1309
FT /note="G->E: In ebs1-4; loss of function."
FT /evidence="ECO:0000269|PubMed:17588517"
FT MUTAGEN 1497
FT /note="D->N: In psl2-1;; loss of response to the PAMP
FT elf18."
FT /evidence="ECO:0000269|PubMed:19763087"
FT MUTAGEN 1500
FT /note="L->F: In ebs1-3; loss of function."
FT /evidence="ECO:0000269|PubMed:17588517"
SQ SEQUENCE 1613 AA; 181805 MW; 62E25666F0240900 CRC64;
MGTTTNLRSW LYLILLFIVV VGVNAQNRRP KNVQVAVKAK WQGTPLLLEA GELISKESKQ
LFWEFTDAWL GSDGDDSDCK SARDCLLKIS KQASTLLAQP VASLFHFSLT LRSASPRLVL
YRQLADESLS SFPHGDDPSA TGCCWVDTGS SLFYDVADLQ SWLASAPAVG DAVQGPELFD
FDHVHFDSRA GSPVAVLYGA VGTDCFRKFH LSLAKAAKEG KVTYVVRPVL PLGCEGKTRP
CGAIGARDNV SLAGYGVELA LKNMEYKAMD DSAIKKGITL EDPRTEDLSQ DVRGFIFSKI
LDRKPELRSE VMAFRDYLLS STVSDTLDVW ELKDLGHQTA QRIVHASDPL QSMQEINQNF
PSVVSSLSRM KLNESIKDEI LSNQRMVPPG KALLALNGAL LNIEDIDLYM LMDLAHQELS
LANHFSKLKI PDGAIRKLLL TTPLPEPDSY RVDFRSVHVT YLNNLEEDDM YKRWRSNINE
ILMPAFPGQL RYIRKNLFHA VYVIDPATAC GLESIETLRS LYENQLPVRF GVILYSTQLI
KTIENNGGQI PSSDAVTNAQ VKEDLSTMVI RLFLYIKEHH GIQTAFQFLG NLNTLRTESA
DSSEADIEQE HVDGAFVETI LPKVKTLPQD ILLKLRQEHT LKEASEASSM FVFKLGLAKL
KCSFLMNGLV FDSVEEETLL NAMNEELPKI QEQVYYGQIE SHTKVLDKLL SESGLSRYNP
QIISGGKNKP RFVSLASSTR KGESMLNDVN YLHSPETSED VKYVTHLLAA DVATKKGMKL
LHEGVRYLIG GSKSARLGVL FSSSQNADPH SLLFIKFFEK TASSFSHKEK VLYFLDKLCL
FYEREYLLKT SVESASSQMF IDKVLELADE YGLSSKAYRS CLVESVDEEL LKRLTKVAQF
LSWELGLESD ANAIISNGRV IFPVDERTFL GQDLHLLESM EFNQRVKPVQ EIIEGIEWQD
VDPDLLTSKY FSDVFMFVSS AMATRDRSSE SARFEVLNSE YSAVLLGNEN ATIHIDAVID
PLSPTGQKLA SLLQVLQKHV QTSMRIVLNP MSSLVDIPLK NYYRYVLPNT DDYSSTGFDV
DGPKAFFANM PLSKTLTMNL DVPEPWLVEP VIAIHDLDNI LLENLGDTTT LQAVFEVESL
VLTGHCAEKD HEAPRGLQLI LGTKNRPHLV DTLVMANLGY WQMKVSPGVW YLQLAPGRSS
ELYALKGGND GSQDQSSLKR ITIDDLRGKV VHLEVVKRKG KEHEKLLVPS DGDDAVQQNK
EGSWNSNFLK WASGFVGGRQ QSMKGGPDKE HEKGGRQGKT INIFSIASGH LYERFLKIMI
LSVLKNTNRP VKFWFIKNYL SPQFKDVIPH MAQEYNFEYE LITYKWPSWL HKQKEKQRII
WAYKILFLDV IFPLSLEKVI FVDADQIIRT DMGELYDMDI KGRPLAYTPF CDNNREMDGY
KFWKQGFWKE HLRGRPYHIS ALYVVDLVKF RETAAGDNLR VFYETLSKDP NSLSNLDQDL
PNYAQHTVPI FSLPQEWLWC ESWCGNATKA KARTIDLCNN PMTKEPKLQG ARRIVTEWPD
LDLEARKFTA KILGEDVELN EPVAAPATDK PNPLPSNDIS EDTEQDLESK AEL
