PGLT1_HUMAN
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 03-AUG-2022, entry version 165.
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},
GN CLP46 {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}.
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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; 135.
DR IntAct; Q8NBL1; 23.
DR STRING; 9606.ENSP00000295588; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR GlyConnect; 1663; 2 N-Linked glycans (1 site).
DR GlyGen; Q8NBL1; 4 sites, 2 N-linked glycans (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; Q8NBL1; -.
DR PeptideAtlas; Q8NBL1; -.
DR PRIDE; Q8NBL1; -.
DR ProteomicsDB; 72789; -.
DR Antibodypedia; 49938; 107 antibodies from 22 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 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; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
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 SignaLink; Q8NBL1; -.
DR SIGNOR; Q8NBL1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 56983; 15 hits in 1077 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 168 other tissues.
DR ExpressionAtlas; Q8NBL1; baseline and differential.
DR Genevisible; Q8NBL1; HS.
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 Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
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
