ID PGLT1_MOUSE Reviewed; 392 AA. AC Q8BYB9; Q8R0H7; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 27-MAR-2024, entry version 150. DE RecName: Full=Protein O-glucosyltransferase 1 {ECO:0000305}; DE EC=2.4.1.376 {ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}; DE AltName: Full=CAP10-like 46 kDa protein; DE AltName: Full=KTEL motif-containing protein 1; DE AltName: Full=O-glucosyltransferase Rumi homolog {ECO:0000303|PubMed:21490058}; DE Short=Rumi {ECO:0000303|PubMed:21490058}; DE AltName: Full=Protein O-xylosyltransferase POGLUT1; DE EC=2.4.2.63 {ECO:0000269|PubMed:21949356}; DE AltName: Full=Wing-shaped neural plate protein {ECO:0000303|PubMed:26496195}; DE Short=Wsnp {ECO:0000303|PubMed:26496195}; DE Flags: Precursor; GN Name=Poglut1 {ECO:0000312|MGI:MGI:2444232}; Synonyms=Clp46, Ktelc1; 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 MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Testis, and Thymus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, Spleen, and Testis; 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). RN [4] RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=21490058; DOI=10.1242/dev.060020; RA Fernandez-Valdivia R., Takeuchi H., Samarghandi A., Lopez M., Leonardi J., RA Haltiwanger R.S., Jafar-Nejad H.; RT "Regulation of mammalian Notch signaling and embryonic development by the RT protein O-glucosyltransferase Rumi."; RL Development 138:1925-1934(2011). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 389-LYS--LEU-392. RX PubMed=21949356; DOI=10.1073/pnas.1109696108; RA Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A., RA Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A., RA Jafar-Nejad H., Haltiwanger R.S.; RT "Rumi functions as both a protein O-glucosyltransferase and a protein O- RT xylosyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=26496195; DOI=10.1371/journal.pgen.1005551; RA Ramkumar N., Harvey B.M., Lee J.D., Alcorn H.L., Silva-Gagliardi N.F., RA McGlade C.J., Bestor T.H., Wijnholds J., Haltiwanger R.S., Anderson K.V.; RT "Protein O-glucosyltransferase 1 (POGLUT1) promotes mouse gastrulation RT through modification of the apical polarity protein CRUMBS2."; RL PLoS Genet. 11:E1005551-E1005551(2015). CC -!- FUNCTION: Dual specificity glycosyltransferase that catalyzes the CC transfer of glucose and xylose from UDP-glucose and UDP-xylose, CC respectively, to a serine residue found in the consensus sequence of C- CC X-S-X-P-C (PubMed:21949356, PubMed:26496195). Specifically targets CC extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 CC (PubMed:21949356, PubMed:26496195). Acts as a positive regulator of CC Notch signaling by mediating O-glucosylation of Notch, leading to CC regulate muscle development (By similarity). Notch glucosylation does CC not affect Notch ligand binding (By similarity). Required during early CC development to promote gastrulation: acts by mediating O-glucosylation CC of CRB2, which is required for CRB2 localization to the cell membrane CC (PubMed:26496195). {ECO:0000250|UniProtKB:Q8NBL1, CC ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}. 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; EC=2.4.2.63; CC Evidence={ECO:0000269|PubMed:21949356}; 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; EC=2.4.1.376; CC Evidence={ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:26496195}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000250|UniProtKB:Q8NBL1}. CC -!- TISSUE SPECIFICITY: Widely expressed in newborn and adult tissues (at CC protein level). {ECO:0000269|PubMed:21490058, CC ECO:0000269|PubMed:26496195}. CC -!- DISRUPTION PHENOTYPE: Mutant embryos die at or before 9.5 dpc. At 7.0 CC to 7.5 dpc, they cannot be morphologically distinguished from wild-type CC littermates (PubMed:21490058, PubMed:26496195). At 8.0 dpc, mutant CC embryos exhibit an abnormally expanded neural plate that does not fold CC properly, absence of heart rudiments and posterior axis truncation CC (PubMed:21490058). Defects are caused by a deficit of mesoderm caused CC by impaired gastrulation. {ECO:0000269|PubMed:21490058, CC ECO:0000269|PubMed:26496195}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family. CC {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; AK031608; BAC27475.1; -; mRNA. DR EMBL; AK035948; BAC29255.1; -; mRNA. DR EMBL; AK036224; BAC29351.1; -; mRNA. DR EMBL; AK041321; BAC30905.1; -; mRNA. DR EMBL; BC026809; AAH26809.1; -; mRNA. DR CCDS; CCDS28170.1; -. DR RefSeq; NP_759012.1; NM_172380.4. DR AlphaFoldDB; Q8BYB9; -. DR SMR; Q8BYB9; -. DR BioGRID; 230254; 3. DR STRING; 10090.ENSMUSP00000038166; -. DR CAZy; GT90; Glycosyltransferase Family 90. DR GlyConnect; 2636; 6 N-Linked glycans (2 sites). DR GlyCosmos; Q8BYB9; 3 sites, 6 glycans. DR GlyGen; Q8BYB9; 3 sites, 6 N-linked glycans (2 sites). DR iPTMnet; Q8BYB9; -. DR PhosphoSitePlus; Q8BYB9; -. DR SwissPalm; Q8BYB9; -. DR EPD; Q8BYB9; -. DR MaxQB; Q8BYB9; -. DR PaxDb; 10090-ENSMUSP00000038166; -. DR PeptideAtlas; Q8BYB9; -. DR ProteomicsDB; 289475; -. DR Pumba; Q8BYB9; -. DR Antibodypedia; 49938; 128 antibodies from 23 providers. DR DNASU; 224143; -. DR Ensembl; ENSMUST00000036210.7; ENSMUSP00000038166.7; ENSMUSG00000034064.15. DR GeneID; 224143; -. DR KEGG; mmu:224143; -. DR UCSC; uc007zfc.2; mouse. DR AGR; MGI:2444232; -. DR CTD; 56983; -. DR MGI; MGI:2444232; Poglut1. DR VEuPathDB; HostDB:ENSMUSG00000034064; -. DR eggNOG; KOG2458; Eukaryota. DR GeneTree; ENSGT00940000158283; -. DR HOGENOM; CLU_041919_1_0_1; -. DR InParanoid; Q8BYB9; -. DR OMA; LEDHCQY; -. DR OrthoDB; 1826823at2759; -. DR PhylomeDB; Q8BYB9; -. DR TreeFam; TF323280; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 224143; 1 hit in 74 CRISPR screens. DR ChiTaRS; Poglut1; mouse. DR PRO; PR:Q8BYB9; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q8BYB9; Protein. DR Bgee; ENSMUSG00000034064; Expressed in humerus cartilage element and 244 other cell types or tissues. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB. DR GO; GO:0140561; F:EGF-domain serine glucosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0140562; F:EGF-domain serine xylosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046527; F:glucosyltransferase activity; IMP:MGI. DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB. DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:MGI. DR GO; GO:0048318; P:axial mesoderm development; IMP:MGI. DR GO; GO:0072359; P:circulatory system development; IMP:MGI. DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW. DR GO; GO:0060537; P:muscle tissue development; ISS:UniProtKB. DR GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI. DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IMP:UniProtKB. DR GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB. DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:MGI. DR GO; GO:0001756; P:somitogenesis; IMP:MGI. DR InterPro; IPR006598; CAP10. DR PANTHER; PTHR12203; KDEL LYS-ASP-GLU-LEU CONTAINING - RELATED; 1. DR PANTHER; PTHR12203:SF35; PROTEIN O-GLUCOSYLTRANSFERASE 1; 1. DR Pfam; PF05686; Glyco_transf_90; 1. DR SMART; SM00672; CAP10; 1. DR Genevisible; Q8BYB9; MM. PE 1: Evidence at protein level; KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Gastrulation; KW Glycoprotein; Glycosyltransferase; Reference proteome; Signal; Transferase. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..392 FT /note="Protein O-glucosyltransferase 1" FT /id="PRO_0000246686" FT REGION 103..107 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT REGION 172..178 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT MOTIF 389..392 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT ACT_SITE 133 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q8T045" FT BINDING 177 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT BINDING 212 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT BINDING 218 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT BINDING 274..279 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT SITE 132 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT SITE 240 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 373 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 49..56 FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT DISULFID 54..357 FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT DISULFID 102..108 FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT DISULFID 263..286 FT /evidence="ECO:0000250|UniProtKB:Q8NBL1" FT MUTAGEN 389..392 FT /note="Missing: Significantly more secreted than FT wild-type." FT /evidence="ECO:0000269|PubMed:21949356" FT CONFLICT 53 FT /note="N -> S (in Ref. 1; BAC30905)" FT /evidence="ECO:0000305" SQ SEQUENCE 392 AA; 46379 MW; CAAD9133E47D3EF0 CRC64; MERRAGSRLR AWMLLLLLCP VQGRQKDSGS KWKVFLDQIN RALENYEPCS SQNCSCYHGV IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ IIKNRLFRED DCMFPSRCSG VEHFILEVIH RLPDMEMVIN VRDYPQVPKW MEPTIPVFSF SKTSEYHDIM YPAWTFWEGG PAVWPLYPTG LGRWDLFRED LLRSAAQWPW EKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ AWKSMKDTLG KPAAKDVHLI DHCKYRYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWVEF FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDIAQEIAK RGSQFIINHL QMDDITCYWE NLLTDYSKFL SYNVTRRKDY YQIVPRRLKT EL //