ID PLGT2_MOUSE Reviewed; 502 AA. AC Q9JHP7; Q8BPU6; Q8C528; Q8R591; Q9D8P1; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 145. DE RecName: Full=Protein O-glucosyltransferase 2 {ECO:0000305}; DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q6UW63}; DE AltName: Full=Endoplasmic reticulum resident protein 58; DE Short=ER protein 58; DE Short=ERp58; DE AltName: Full=KDEL motif-containing protein 1 {ECO:0000312|MGI:MGI:1919300}; DE AltName: Full=Protein O-xylosyltransferase POGLUT2 {ECO:0000305}; DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q6UW63}; DE Flags: Precursor; GN Name=Poglut2; Synonyms=Ep58, Kdelc1 {ECO:0000312|MGI:MGI:1919300}; 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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TOPOLOGY, RP GLYCOSYLATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryonic carcinoma; RX PubMed=11167020; DOI=10.1016/s0378-1119(00)00499-6; RA Kimata Y., Ooboki K., Nomura-Furuwatari C., Hosoda A., Tsuru A., Kohno K.; RT "Identification of a novel mammalian endoplasmic reticulum-resident KDEL RT protein using an EST database motif search."; RL Gene 261:321-327(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Cerebellum, Dendritic cell, Eye, Pancreas, 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=Czech II; TISSUE=Mammary tumor; 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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). 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:Q6UW63}. 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:Q6UW63}; 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:Q6UW63}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000250|UniProtKB:Q6UW63}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138, ECO:0000269|PubMed:11167020}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9JHP7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JHP7-2; Sequence=VSP_019936; CC Name=3; CC IsoId=Q9JHP7-3; Sequence=VSP_019935; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11167020}. CC -!- DEVELOPMENTAL STAGE: Expressed in various fetal tissues. CC {ECO:0000269|PubMed:11167020}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11167020}. CC -!- SIMILARITY: Belongs to the KDELC family. {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; AJ404004; CAC00650.1; -; mRNA. DR EMBL; AK007835; BAB25294.1; -; mRNA. DR EMBL; AK035899; BAC29235.1; -; mRNA. DR EMBL; AK053315; BAC35341.1; -; mRNA. DR EMBL; AK079701; BAC37727.1; -; mRNA. DR EMBL; AK170300; BAE41698.1; -; mRNA. DR EMBL; BC023141; AAH23141.1; -; mRNA. DR CCDS; CCDS14929.1; -. [Q9JHP7-1] DR RefSeq; NP_076134.1; NM_023645.3. [Q9JHP7-1] DR RefSeq; XP_006496352.1; XM_006496289.3. DR AlphaFoldDB; Q9JHP7; -. DR SMR; Q9JHP7; -. DR BioGRID; 215118; 3. DR IntAct; Q9JHP7; 1. DR MINT; Q9JHP7; -. DR STRING; 10090.ENSMUSP00000064500; -. DR CAZy; GT90; Glycosyltransferase Family 90. DR GlyConnect; 2449; 2 N-Linked glycans (1 site). DR GlyCosmos; Q9JHP7; 3 sites, 2 glycans. DR GlyGen; Q9JHP7; 3 sites, 2 N-linked glycans (1 site). DR iPTMnet; Q9JHP7; -. DR PhosphoSitePlus; Q9JHP7; -. DR SwissPalm; Q9JHP7; -. DR EPD; Q9JHP7; -. DR MaxQB; Q9JHP7; -. DR PaxDb; 10090-ENSMUSP00000064500; -. DR PeptideAtlas; Q9JHP7; -. DR ProteomicsDB; 263424; -. [Q9JHP7-1] DR ProteomicsDB; 263425; -. [Q9JHP7-2] DR ProteomicsDB; 263426; -. [Q9JHP7-3] DR Pumba; Q9JHP7; -. DR Antibodypedia; 54168; 162 antibodies from 14 providers. DR DNASU; 72050; -. DR Ensembl; ENSMUST00000027213.14; ENSMUSP00000027213.8; ENSMUSG00000026047.14. [Q9JHP7-2] DR Ensembl; ENSMUST00000065767.9; ENSMUSP00000064500.3; ENSMUSG00000026047.14. [Q9JHP7-1] DR GeneID; 72050; -. DR KEGG; mmu:72050; -. DR UCSC; uc007awb.1; mouse. [Q9JHP7-1] DR UCSC; uc011wkc.1; mouse. [Q9JHP7-2] DR AGR; MGI:1919300; -. DR CTD; 79070; -. DR MGI; MGI:1919300; Poglut2. DR VEuPathDB; HostDB:ENSMUSG00000026047; -. DR eggNOG; KOG2458; Eukaryota. DR GeneTree; ENSGT00940000158318; -. DR HOGENOM; CLU_041919_0_0_1; -. DR InParanoid; Q9JHP7; -. DR OMA; MFMDATL; -. DR OrthoDB; 1826823at2759; -. DR PhylomeDB; Q9JHP7; -. DR TreeFam; TF323280; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 72050; 4 hits in 78 CRISPR screens. DR ChiTaRS; Poglut2; mouse. DR PRO; PR:Q9JHP7; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q9JHP7; Protein. DR Bgee; ENSMUSG00000026047; Expressed in embryonic facial prominence and 73 other cell types or tissues. DR ExpressionAtlas; Q9JHP7; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. 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; Immunoglobulins; 1. DR InterPro; IPR006598; CAP10. DR InterPro; IPR017868; Filamin/ABP280_repeat-like. DR InterPro; IPR001298; Filamin/ABP280_rpt. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR12203; KDEL LYS-ASP-GLU-LEU CONTAINING - RELATED; 1. DR PANTHER; PTHR12203:SF21; PROTEIN O-GLUCOSYLTRANSFERASE 2; 1. DR Pfam; PF00630; Filamin; 1. DR Pfam; PF05686; Glyco_transf_90; 1. DR SMART; SM00672; CAP10; 1. DR SMART; SM00557; IG_FLMN; 1. DR SUPFAM; SSF81296; E set domains; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS50194; FILAMIN_REPEAT; 1. DR Genevisible; Q9JHP7; MM. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; KW Glycosyltransferase; Reference proteome; Signal; Transferase. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..502 FT /note="Protein O-glucosyltransferase 2" FT /id="PRO_0000247164" FT REPEAT 24..130 FT /note="Filamin" FT MOTIF 499..502 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT CARBOHYD 152 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 283..502 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019935" FT VAR_SEQ 362..431 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_019936" FT CONFLICT 47 FT /note="A -> V (in Ref. 2; BAB25294)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="K -> E (in Ref. 2; BAC35341)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="R -> H (in Ref. 2; BAC37727)" FT /evidence="ECO:0000305" FT CONFLICT 436 FT /note="A -> T (in Ref. 2; BAC37727)" FT /evidence="ECO:0000305" SQ SEQUENCE 502 AA; 57985 MW; FFE80DF36765DB7E CRC64; MFSISLLSCL FLGTVPALAQ TGGERRLSPE KSEIWGPGLK AHVVLPARYF YIRAVDTSGE QFTSSPGEKV FQVKISAPDE QFTRVGVQVL DRKDGSFIVR YRMYASYRNL KIEVKHHGQH VAESPYVLRG PVYHENCDCP LEDSAAWLRE MNCSETISQI QKDLAHFPTV DPEKIAAEIP KRFGQRQSLC HYTLKDNKVY IKTHGEHVGF RIFMDAILLS LTRKVRMPDV EFFVNLGDWP LEKKKSNSNI QPIFSWCGST ESRDIVMPTY DLTDSVLETM GRVSLDMMSV QANTGPPWES KNSTAVWRGR DSRKERLELV KLSRKHPELI DAAFTNFFFF KHDESLYGPI VKHISFFDFF KHKYQINIDG TVAAYRLPYL LVGDSVVLKQ DSIYYEHFYN ELQPWKHYIP VKSNLSDLLE KLKWAKEHDA EAKKIAKAGQ EFARNNLMGD DIFCYYFKLF QGYANLQVSE PQIREGMKRV EPQSEDDLFP CTCHRRKAKD EL //