PLGT2_MOUSE
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 03-AUG-2022, entry version 139.
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}.
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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 GlyGen; Q9JHP7; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9JHP7; -.
DR PhosphoSitePlus; Q9JHP7; -.
DR EPD; Q9JHP7; -.
DR MaxQB; Q9JHP7; -.
DR PaxDb; Q9JHP7; -.
DR PeptideAtlas; Q9JHP7; -.
DR PRIDE; Q9JHP7; -.
DR ProteomicsDB; 263424; -. [Q9JHP7-1]
DR ProteomicsDB; 263425; -. [Q9JHP7-2]
DR ProteomicsDB; 263426; -. [Q9JHP7-3]
DR Antibodypedia; 54168; 130 antibodies from 13 providers.
DR DNASU; 72050; -.
DR Ensembl; ENSMUST00000027213; ENSMUSP00000027213; ENSMUSG00000026047. [Q9JHP7-2]
DR Ensembl; ENSMUST00000065767; ENSMUSP00000064500; ENSMUSG00000026047. [Q9JHP7-1]
DR GeneID; 72050; -.
DR KEGG; mmu:72050; -.
DR UCSC; uc007awb.1; mouse. [Q9JHP7-1]
DR UCSC; uc011wkc.1; mouse. [Q9JHP7-2]
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; 547457at2759; -.
DR PhylomeDB; Q9JHP7; -.
DR TreeFam; TF323280; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 72050; 4 hits in 73 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 70 other tissues.
DR ExpressionAtlas; Q9JHP7; baseline and differential.
DR Genevisible; Q9JHP7; MM.
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; -; 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 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; SSF81296; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
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
