PLGT3_MOUSE
ID PLGT3_MOUSE Reviewed; 503 AA.
AC G5E897; Q8C6F3;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein O-glucosyltransferase 3 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q7Z4H8};
DE AltName: Full=KDEL motif-containing protein 2 {ECO:0000312|MGI:MGI:1923765};
DE AltName: Full=Protein O-xylosyltransferase POGLUT3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q7Z4H8};
DE Flags: Precursor;
GN Name=Poglut3; Synonyms=Kdelc2 {ECO:0000312|MGI:MGI:1923765};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-503.
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein glucosyltransferase that catalyzes the transfer of
CC glucose from UDP-glucose to a serine residue within the consensus
CC sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of
CC xylose from UDP-xylose but less efficiently. Specifically targets
CC extracellular EGF repeats of proteins such as NOTCH1, NOTCH3, FBN1,
CC FBN2 and LTBP1. May regulate the transport of NOTCH1 and NOTCH3 to the
CC plasma membrane and thereby the Notch signaling pathway.
CC {ECO:0000250|UniProtKB:Q7Z4H8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-glucose = 3-O-
CC (beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:58116, Rhea:RHEA-COMP:14610, Rhea:RHEA-COMP:16010,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:140576;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4H8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-
CC (beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:62016, Rhea:RHEA-COMP:16010, Rhea:RHEA-COMP:16011,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132085;
CC Evidence={ECO:0000250|UniProtKB:Q7Z4H8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q7Z4H8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the KDELC family. {ECO:0000305}.
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DR EMBL; AC079869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL25792.1; -; Genomic_DNA.
DR EMBL; AK075811; BAC35979.1; -; mRNA.
DR CCDS; CCDS23182.1; -.
DR RefSeq; NP_997610.1; NM_212445.2.
DR AlphaFoldDB; G5E897; -.
DR SMR; G5E897; -.
DR STRING; 10090.ENSMUSP00000039313; -.
DR GlyConnect; 2637; 1 N-Linked glycan (1 site).
DR GlyGen; G5E897; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; G5E897; -.
DR PhosphoSitePlus; G5E897; -.
DR EPD; G5E897; -.
DR MaxQB; G5E897; -.
DR PaxDb; G5E897; -.
DR PeptideAtlas; G5E897; -.
DR PRIDE; G5E897; -.
DR ProteomicsDB; 338485; -.
DR Antibodypedia; 50833; 59 antibodies from 15 providers.
DR DNASU; 68304; -.
DR Ensembl; ENSMUST00000037853; ENSMUSP00000039313; ENSMUSG00000034487.
DR GeneID; 68304; -.
DR KEGG; mmu:68304; -.
DR UCSC; uc009pmb.1; mouse.
DR CTD; 143888; -.
DR MGI; MGI:1923765; Poglut3.
DR VEuPathDB; HostDB:ENSMUSG00000034487; -.
DR eggNOG; KOG2458; Eukaryota.
DR GeneTree; ENSGT00940000159028; -.
DR HOGENOM; CLU_041919_0_0_1; -.
DR InParanoid; G5E897; -.
DR OMA; PVISWCG; -.
DR OrthoDB; 547457at2759; -.
DR PhylomeDB; G5E897; -.
DR TreeFam; TF323280; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 68304; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Poglut3; mouse.
DR PRO; PR:G5E897; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; G5E897; protein.
DR Bgee; ENSMUSG00000034487; Expressed in ascending aorta and 190 other tissues.
DR ExpressionAtlas; G5E897; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0140561; F:EGF-domain serine glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0140562; F:EGF-domain serine xylosyltransferase activity; IEA:RHEA.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR006598; CAP10.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..503
FT /note="Protein O-glucosyltransferase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5015091896"
FT REPEAT 19..129
FT /note="Filamin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00087"
FT MOTIF 500..503
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 503 AA; 57686 MW; 1BB9DDE7C2E1EDA0 CRC64;
MQALPLGLQL ALLVAAGAGA RVSAPRSLAW GPGLQAAAVL PVRYFFLQSV DSDGRNFTSS
PPGQTQFKVV VKSLSPKELV RIYVPKPLDR NDGTFLVRYR MHETAHKGLK IEILHGSEHV
AHSPYILKGP VYHEYCDCPE DDPQVWQETL SCPASEPQIE QDFVSFPSIN LQQMLKEVPT
RFGDERGAVV HYTILNNHIY RRSLGKYTDF KMFSDEILLS LARKVTLPDL EFYINLGDWP
LEHRKVNDTP GPIPIISWCG SLDSRDIILP TYDVTHSTLE AMRGVTNDLL SVQGNTGPSW
INKTEKAFFR GRDSREERLQ LVLLSKENPQ LLDAGITGYF FFQEKEKELG KAKLMGFFDF
FKYKYQVNVD GTVAAYRYPY LMLGDSLVLK QESPYYEHFY VALKPWKHYV PIKRNLGDLL
EKVKWAKEND EEAKKIAKEG QLTARDLLQP PRLYCYYYRV LQKYAERQAS KPMIRDGMEL
VPQPDDGTSI CQCHRRRPER EEL
