ID PGLT1_HUMAN Reviewed; 392 AA. AC Q8NBL1; B2RD13; Q53GJ4; Q8N2T1; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=Protein O-glucosyltransferase 1 {ECO:0000305}; DE EC=2.4.1.376 {ECO:0000269|PubMed:21490058, ECO:0000269|PubMed:21949356}; DE AltName: Full=CAP10-like 46 kDa protein {ECO:0000303|PubMed:16524674}; DE Short=hCLP46 {ECO:0000303|PubMed:16524674}; DE AltName: Full=KTEL motif-containing protein 1; DE AltName: Full=Myelodysplastic syndromes relative protein; DE AltName: Full=O-glucosyltransferase Rumi homolog {ECO:0000303|PubMed:21490058}; DE Short=hRumi {ECO:0000303|PubMed:21490058}; DE AltName: Full=Protein O-xylosyltransferase POGLUT1 {ECO:0000305}; DE EC=2.4.2.63 {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:28775322}; DE Flags: Precursor; GN Name=POGLUT1 {ECO:0000312|HGNC:HGNC:22954}; GN Synonyms=C3orf9 {ECO:0000312|HGNC:HGNC:22954}, CLP46 GN {ECO:0000303|PubMed:16524674}, KTELC1, MDSRP; GN ORFNames=MDS010, UNQ490/PRO1006 {ECO:0000303|PubMed:12975309}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Hematopoietic stem cell; RX PubMed=16524674; DOI=10.1016/j.gene.2005.08.027; RA Teng Y., Liu Q., Ma J., Liu F., Han Z., Wang Y., Wang W.; RT "Cloning, expression and characterization of a novel human CAP10-like gene RT hCLP46 from CD34+ stem/progenitor cells."; RL Gene 371:7-15(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-75 AND THR-229. RC TISSUE=Fetal brain, and Hypothalamus; 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 [9] RP PROTEIN SEQUENCE OF 24-38. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [10] RP FUNCTION, AND MUTAGENESIS OF GLY-169. 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 [11] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21081508; DOI=10.1093/glycob/cwq187; RA Wu Z.L., Ethen C.M., Prather B., Machacek M., Jiang W.; RT "Universal phosphatase-coupled glycosyltransferase assay."; RL Glycobiology 21:727-733(2011). RN [12] RP FUNCTION. 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 [13] RP INVOLVEMENT IN DDD4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=24387993; DOI=10.1016/j.ajhg.2013.12.003; RA Basmanav F.B., Oprisoreanu A.M., Pasternack S.M., Thiele H., Fritz G., RA Wenzel J., Grosser L., Wehner M., Wolf S., Fagerberg C., Bygum A., RA Altmuller J., Rutten A., Parmentier L., El Shabrawi-Caelen L., Hafner C., RA Nurnberg P., Kruse R., Schoch S., Hanneken S., Betz R.C.; RT "Mutations in POGLUT1, encoding protein O-glucosyltransferase 1, cause RT autosomal-dominant Dowling-Degos disease."; RL Am. J. Hum. Genet. 94:135-143(2014). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN LGMDR21, VARIANT LGMDR21 RP GLU-233, AND CHARACTERIZATION OF VARIANT LGMDR21 GLU-233. RX PubMed=27807076; DOI=10.15252/emmm.201505815; RA Servian-Morilla E., Takeuchi H., Lee T.V., Clarimon J., Mavillard F., RA Area-Gomez E., Rivas E., Nieto-Gonzalez J.L., Rivero M.C., RA Cabrera-Serrano M., Gomez-Sanchez L., Martinez-Lopez J.A., Estrada B., RA Marquez C., Morgado Y., Suarez-Calvet X., Pita G., Bigot A., Gallardo E., RA Fernandez-Chacon R., Hirano M., Haltiwanger R.S., Jafar-Nejad H., RA Paradas C.; RT "A POGLUT1 mutation causes a muscular dystrophy with reduced Notch RT signaling and satellite cell loss."; RL EMBO Mol. Med. 8:1289-1309(2016). RN [15] {ECO:0007744|PDB:5L0R, ECO:0007744|PDB:5L0S, ECO:0007744|PDB:5L0T, ECO:0007744|PDB:5L0U, ECO:0007744|PDB:5L0V, ECO:0007744|PDB:5UB5} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 29-385 IN COMPLEXES WITH RP UDP-GLUCOSE ANALOG AND PEPTIDE SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, RP PATHWAY, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-40; ASN-53; ASN-204 AND RP ASN-373. RX PubMed=28775322; DOI=10.1038/s41467-017-00255-7; RA Li Z., Fischer M., Satkunarajah M., Zhou D., Withers S.G., Rini J.M.; RT "Structural basis of Notch O-glucosylation and O-xylosylation by mammalian RT protein-O-glucosyltransferase 1 (POGLUT1)."; RL Nat. Commun. 8:185-185(2017). RN [16] RP VARIANTS DDD4 GLU-170; 218-ARG--LEU-392 DEL AND TYR-286. RX PubMed=27479915; DOI=10.1111/bjd.14914; RA Wilson N.J., Cole C., Kroboth K., Hunter W.N., Mann J.A., McLean W.H., RA Kernland Lang K., Beltraminelli H., Sabroe R.A., Tiffin N., Sobey G.J., RA Borradori L., Simpson E., Smith F.J.; RT "Mutations in POGLUT1 in Galli-Galli/Dowling-Degos disease."; RL Br. J. Dermatol. 176:270-274(2017). 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:21081508, PubMed:21490058, PubMed:21949356, CC PubMed:27807076, PubMed:28775322). Specifically targets extracellular CC EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 CC (PubMed:21081508, PubMed:21490058, PubMed:21949356, PubMed:27807076, CC PubMed:28775322). Acts as a positive regulator of Notch signaling by CC mediating O-glucosylation of Notch, leading to regulate muscle CC development (PubMed:27807076). Notch glucosylation does not affect CC Notch ligand binding (PubMed:21490058). 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 (By similarity). {ECO:0000250|UniProtKB:Q8BYB9, CC ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, CC ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:27807076, CC ECO:0000269|PubMed:28775322}. 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:21081508, ECO:0000269|PubMed:28775322}; 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:21490058, ECO:0000269|PubMed:21949356}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=72 uM for UDP-Glc {ECO:0000269|PubMed:21081508}; CC Vmax=7.6 pmol/min/ug enzyme {ECO:0000269|PubMed:21081508}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:21490058, CC ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:28775322}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:16524674, ECO:0000269|PubMed:24387993, CC ECO:0000269|PubMed:27807076}. CC -!- TISSUE SPECIFICITY: Expressed in most adult tissues at different CC intensities. Abundantly expressed in liver. Expressed also in brain, CC heart, skeletal muscle, spleen, kidney, placenta, lung and peripheral CC blood leukocyte. Not detectable in colon, thymus and small intestine. CC Expressed in the epidermis, especially in the upper parts, stratum CC spinosum and stratum granulosum (at protein level). CC {ECO:0000269|PubMed:16524674, ECO:0000269|PubMed:24387993}. CC -!- DISEASE: Dowling-Degos disease 4 (DDD4) [MIM:615696]: A form of CC Dowling-Degos disease, a genodermatosis manifesting with postpubertal CC reticulate hyperpigmentation that is progressive and disfiguring, and CC small hyperkeratotic dark brown papules that affect mainly the flexures CC and great skin folds. Patients usually show no abnormalities of the CC hair or nails. DDD4 is characterized by prominent involvement of non- CC flexural skin areas. {ECO:0000269|PubMed:24387993, CC ECO:0000269|PubMed:27479915}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 21 CC (LGMDR21) [MIM:617232]: A form of autosomal recessive limb-girdle CC muscular dystrophy, a degenerative myopathy characterized by slowly CC progressive wasting and weakness of the proximal muscles of arms and CC legs around the pelvic or shoulder girdles, elevated creatine kinase CC levels and dystrophic features on muscle biopsy. LGMDR21 is CC characterized by young-adult onset. {ECO:0000269|PubMed:27807076}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. 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; AY298903; AAP56253.1; -; mRNA. DR EMBL; AY358581; AAQ88944.1; -; mRNA. DR EMBL; AK075444; BAC11625.1; -; mRNA. DR EMBL; AK222937; BAD96657.1; -; mRNA. DR EMBL; AK315367; BAG37760.1; -; mRNA. DR EMBL; AC074271; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC073352; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79570.1; -; Genomic_DNA. DR EMBL; BC030614; AAH30614.1; -; mRNA. DR EMBL; BC048810; AAH48810.1; -; mRNA. DR CCDS; CCDS2988.1; -. DR RefSeq; NP_689518.1; NM_152305.2. DR PDB; 5L0R; X-ray; 1.50 A; A=29-385. DR PDB; 5L0S; X-ray; 1.45 A; A=29-385. DR PDB; 5L0T; X-ray; 1.43 A; A=29-385. DR PDB; 5L0U; X-ray; 1.80 A; A=29-385. DR PDB; 5L0V; X-ray; 1.30 A; A=29-385. DR PDB; 5UB5; X-ray; 2.09 A; A=29-385. DR PDBsum; 5L0R; -. DR PDBsum; 5L0S; -. DR PDBsum; 5L0T; -. DR PDBsum; 5L0U; -. DR PDBsum; 5L0V; -. DR PDBsum; 5UB5; -. DR AlphaFoldDB; Q8NBL1; -. DR SMR; Q8NBL1; -. DR BioGRID; 121300; 154. DR IntAct; Q8NBL1; 23. DR STRING; 9606.ENSP00000295588; -. DR CAZy; GT90; Glycosyltransferase Family 90. DR GlyConnect; 1663; 2 N-Linked glycans (1 site). DR GlyCosmos; Q8NBL1; 4 sites, 2 glycans. DR GlyGen; Q8NBL1; 5 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q8NBL1; -. DR PhosphoSitePlus; Q8NBL1; -. DR BioMuta; POGLUT1; -. DR DMDM; 74730148; -. DR CPTAC; CPTAC-2230; -. DR EPD; Q8NBL1; -. DR jPOST; Q8NBL1; -. DR MassIVE; Q8NBL1; -. DR MaxQB; Q8NBL1; -. DR PaxDb; 9606-ENSP00000295588; -. DR PeptideAtlas; Q8NBL1; -. DR ProteomicsDB; 72789; -. DR Pumba; Q8NBL1; -. DR Antibodypedia; 49938; 128 antibodies from 23 providers. DR DNASU; 56983; -. DR Ensembl; ENST00000295588.9; ENSP00000295588.4; ENSG00000163389.12. DR GeneID; 56983; -. DR KEGG; hsa:56983; -. DR MANE-Select; ENST00000295588.9; ENSP00000295588.4; NM_152305.3; NP_689518.1. DR UCSC; uc003ecm.4; human. DR AGR; HGNC:22954; -. DR CTD; 56983; -. DR DisGeNET; 56983; -. DR GeneCards; POGLUT1; -. DR HGNC; HGNC:22954; POGLUT1. DR HPA; ENSG00000163389; Low tissue specificity. DR MalaCards; POGLUT1; -. DR MIM; 615618; gene. DR MIM; 615696; phenotype. DR MIM; 617232; phenotype. DR neXtProt; NX_Q8NBL1; -. DR OpenTargets; ENSG00000163389; -. DR Orphanet; 79145; Dowling-Degos disease. DR Orphanet; 480682; POGLUT1-related limb-girdle muscular dystrophy R21. DR PharmGKB; PA162393771; -. DR VEuPathDB; HostDB:ENSG00000163389; -. DR eggNOG; KOG2458; Eukaryota. DR GeneTree; ENSGT00940000158283; -. DR HOGENOM; CLU_041919_1_0_1; -. DR InParanoid; Q8NBL1; -. DR OMA; LEDHCQY; -. DR OrthoDB; 1826823at2759; -. DR PhylomeDB; Q8NBL1; -. DR TreeFam; TF323280; -. DR BRENDA; 2.4.1.376; 2681. DR BRENDA; 2.4.2.63; 2681. DR PathwayCommons; Q8NBL1; -. DR Reactome; R-HSA-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum. DR SABIO-RK; Q8NBL1; -. DR SignaLink; Q8NBL1; -. DR SIGNOR; Q8NBL1; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 56983; 16 hits in 1153 CRISPR screens. DR ChiTaRS; POGLUT1; human. DR GenomeRNAi; 56983; -. DR Pharos; Q8NBL1; Tbio. DR PRO; PR:Q8NBL1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8NBL1; Protein. DR Bgee; ENSG00000163389; Expressed in seminal vesicle and 170 other cell types or tissues. DR ExpressionAtlas; Q8NBL1; baseline and differential. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA: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; IDA:MGI. DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB. DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IMP:UniProtKB. DR GO; GO:0048318; P:axial mesoderm development; IEA:Ensembl. DR GO; GO:0072359; P:circulatory system development; IEA:Ensembl. DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW. DR GO; GO:0060537; P:muscle tissue development; IMP:UniProtKB. DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI. DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB. DR GO; GO:0010470; P:regulation of gastrulation; ISS:UniProtKB. DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl. 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; Q8NBL1; HS. PE 1: Evidence at protein level; KW 3D-structure; Developmental protein; Direct protein sequencing; KW Disease variant; Disulfide bond; Endoplasmic reticulum; Gastrulation; KW Glycoprotein; Glycosyltransferase; Limb-girdle muscular dystrophy; KW Reference proteome; Signal; Transferase. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 24..392 FT /note="Protein O-glucosyltransferase 1" FT /id="PRO_0000246685" FT REGION 103..107 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:28775322" FT REGION 172..178 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:28775322" 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:0000305|PubMed:28775322" FT BINDING 177 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0U" FT BINDING 212 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0U" FT BINDING 218 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0U" FT BINDING 274..279 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0U" FT SITE 132 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:28775322" FT SITE 240 FT /note="Interaction with the consensus sequence C-X-S-X- FT [PA]-C in peptide substrates" FT /evidence="ECO:0000269|PubMed:28775322" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0V" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0V" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0V" FT CARBOHYD 373 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0V" FT DISULFID 49..56 FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0R, ECO:0007744|PDB:5L0S, FT ECO:0007744|PDB:5L0T, ECO:0007744|PDB:5L0U, FT ECO:0007744|PDB:5L0V, ECO:0007744|PDB:5UB5" FT DISULFID 54..357 FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0R, ECO:0007744|PDB:5L0S, FT ECO:0007744|PDB:5L0T, ECO:0007744|PDB:5L0U, FT ECO:0007744|PDB:5L0V, ECO:0007744|PDB:5UB5" FT DISULFID 102..108 FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0R, ECO:0007744|PDB:5L0S, FT ECO:0007744|PDB:5L0T, ECO:0007744|PDB:5L0U, FT ECO:0007744|PDB:5L0V, ECO:0007744|PDB:5UB5" FT DISULFID 263..286 FT /evidence="ECO:0000269|PubMed:28775322, FT ECO:0007744|PDB:5L0R, ECO:0007744|PDB:5L0S, FT ECO:0007744|PDB:5L0T, ECO:0007744|PDB:5L0U, FT ECO:0007744|PDB:5L0V, ECO:0007744|PDB:5UB5" FT VARIANT 75 FT /note="K -> R (in dbSNP:rs11556605)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027041" FT VARIANT 170 FT /note="G -> E (in DDD4; dbSNP:rs1454300079)" FT /evidence="ECO:0000269|PubMed:27479915" FT /id="VAR_077954" FT VARIANT 218..392 FT /note="Missing (in DDD4)" FT /evidence="ECO:0000269|PubMed:27479915" FT /id="VAR_077955" FT VARIANT 229 FT /note="P -> T (in dbSNP:rs17852785)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_027042" FT VARIANT 233 FT /note="D -> E (in LGMDR21; reduced glucosyltransferase and FT xylosyltransferase activities; impaired Notch signaling; FT dbSNP:rs550944082)" FT /evidence="ECO:0000269|PubMed:27807076" FT /id="VAR_077956" FT VARIANT 286 FT /note="C -> Y (in DDD4)" FT /evidence="ECO:0000269|PubMed:27479915" FT /id="VAR_077957" FT MUTAGEN 169 FT /note="G->E: Loss of O-glucosyltransferase activity." FT /evidence="ECO:0000269|PubMed:21490058" FT CONFLICT 287 FT /note="G -> D (in Ref. 5; BAD96657)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="S -> P (in Ref. 5; BAD96657)" FT /evidence="ECO:0000305" FT HELIX 33..45 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 54..57 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 74..82 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 105..118 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:5L0T" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5L0V" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 184..197 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 203..211 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 219..227 FT /evidence="ECO:0007829|PDB:5L0V" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 279..285 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:5L0V" FT TURN 307..309 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 310..314 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 321..330 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 332..349 FT /evidence="ECO:0007829|PDB:5L0V" FT HELIX 352..367 FT /evidence="ECO:0007829|PDB:5L0V" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:5L0V" SQ SEQUENCE 392 AA; 46189 MW; 25B0370757A6B224 CRC64; MEWWASSPLR LWLLLFLLPS AQGRQKESGS KWKVFIDQIN RSLENYEPCS SQNCSCYHGV IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ ITKNRLYREN DCMFPSRCSG VEHFILEVIG RLPDMEMVIN VRDYPQVPKW MEPAIPVFSF SKTSEYHDIM YPAWTFWEGG PAVWPIYPTG LGRWDLFRED LVRSAAQWPW KKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ AWKSMKDTLG KPAAKDVHLV DHCKYKYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWLEF FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDVAQEIAE RGSQFIRNHL QMDDITCYWE NLLSEYSKFL SYNVTRRKGY DQIIPKMLKT EL //