PGLT1_MOUSE
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 03-AUG-2022, entry version 141.
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 GlyGen; Q8BYB9; 3 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q8BYB9; -.
DR PhosphoSitePlus; Q8BYB9; -.
DR EPD; Q8BYB9; -.
DR MaxQB; Q8BYB9; -.
DR PaxDb; Q8BYB9; -.
DR PeptideAtlas; Q8BYB9; -.
DR PRIDE; Q8BYB9; -.
DR ProteomicsDB; 289475; -.
DR Antibodypedia; 49938; 107 antibodies from 22 providers.
DR DNASU; 224143; -.
DR Ensembl; ENSMUST00000036210; ENSMUSP00000038166; ENSMUSG00000034064.
DR GeneID; 224143; -.
DR KEGG; mmu:224143; -.
DR UCSC; uc007zfc.2; mouse.
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; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
DR PhylomeDB; Q8BYB9; -.
DR TreeFam; TF323280; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 224143; 1 hit in 69 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 241 other tissues.
DR Genevisible; Q8BYB9; MM.
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 Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
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 wild-
FT 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
