PLGT2_HUMAN
ID PLGT2_HUMAN Reviewed; 502 AA.
AC Q6UW63; Q53HL3; Q9BVD2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein O-glucosyltransferase 2 {ECO:0000305|PubMed:30127001};
DE EC=2.4.1.- {ECO:0000269|PubMed:30127001};
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|HGNC:HGNC:19350};
DE AltName: Full=Protein O-xylosyltransferase POGLUT2 {ECO:0000305|PubMed:30127001};
DE EC=2.4.2.- {ECO:0000269|PubMed:30127001};
DE Flags: Precursor;
GN Name=POGLUT2 {ECO:0000303|PubMed:30127001, ECO:0000312|HGNC:HGNC:19350};
GN Synonyms=EP58, KDELC1 {ECO:0000312|HGNC:HGNC:19350};
GN ORFNames=UNQ1910/PRO4357;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary arterial endothelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-114.
RC TISSUE=Cervix carcinoma;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RX PubMed=30127001; DOI=10.1073/pnas.1804005115;
RA Takeuchi H., Schneider M., Williamson D.B., Ito A., Takeuchi M.,
RA Handford P.A., Haltiwanger R.S.;
RT "Two novel protein O-glucosyltransferases that modify sites distinct from
RT POGLUT1 and affect Notch trafficking and signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E8395-E8402(2018).
RN [7]
RP FUNCTION.
RX PubMed=34411563; DOI=10.1016/j.jbc.2021.101055;
RA Williamson D.B., Sohn C.J., Ito A., Haltiwanger R.S.;
RT "POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2,
RT and LTBP1 and promote secretion of fibrillin-1.";
RL J. Biol. Chem. 297:101055-101055(2021).
RN [8]
RP STRUCTURE BY NMR OF 20-130.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the filamin domain from human BK158_1 protein.";
RL Submitted (SEP-2006) to the PDB data bank.
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 (PubMed:30127001). Can also
CC catalyze the transfer of xylose from UDP-xylose but less efficiently
CC (PubMed:30127001). Specifically targets extracellular EGF repeats of
CC proteins such as NOTCH1, NOTCH3, FBN1, FBN2 and LTBP1 (PubMed:30127001,
CC PubMed:34411563). May regulate the transport of NOTCH1 and NOTCH3 to
CC the plasma membrane and thereby the Notch signaling pathway
CC (PubMed:30127001). {ECO:0000269|PubMed:30127001,
CC ECO:0000269|PubMed:34411563}.
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:0000269|PubMed:30127001};
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:0000269|PubMed:30127001};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:30127001}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9JHP7}.
CC -!- SIMILARITY: Belongs to the KDELC family. {ECO:0000305}.
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DR EMBL; AY358959; AAQ89318.1; -; mRNA.
DR EMBL; AK222567; BAD96287.1; -; mRNA.
DR EMBL; AL157769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001297; AAH01297.1; -; mRNA.
DR CCDS; CCDS9504.1; -.
DR RefSeq; NP_001305661.1; NM_001318732.1.
DR RefSeq; NP_076994.2; NM_024089.2.
DR PDB; 2DI7; NMR; -; A=20-130.
DR PDBsum; 2DI7; -.
DR AlphaFoldDB; Q6UW63; -.
DR BMRB; Q6UW63; -.
DR SMR; Q6UW63; -.
DR BioGRID; 122521; 129.
DR IntAct; Q6UW63; 8.
DR STRING; 9606.ENSP00000365172; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR GlyConnect; 1430; 2 N-Linked glycans (1 site).
DR GlyGen; Q6UW63; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q6UW63; -.
DR PhosphoSitePlus; Q6UW63; -.
DR BioMuta; KDELC1; -.
DR DMDM; 74749382; -.
DR EPD; Q6UW63; -.
DR jPOST; Q6UW63; -.
DR MassIVE; Q6UW63; -.
DR MaxQB; Q6UW63; -.
DR PaxDb; Q6UW63; -.
DR PeptideAtlas; Q6UW63; -.
DR PRIDE; Q6UW63; -.
DR ProteomicsDB; 67452; -.
DR Antibodypedia; 54168; 130 antibodies from 13 providers.
DR DNASU; 79070; -.
DR Ensembl; ENST00000376004.5; ENSP00000365172.4; ENSG00000134901.13.
DR GeneID; 79070; -.
DR KEGG; hsa:79070; -.
DR MANE-Select; ENST00000376004.5; ENSP00000365172.4; NM_024089.3; NP_076994.2.
DR UCSC; uc001vpq.5; human.
DR CTD; 79070; -.
DR DisGeNET; 79070; -.
DR GeneCards; POGLUT2; -.
DR HGNC; HGNC:19350; POGLUT2.
DR HPA; ENSG00000134901; Low tissue specificity.
DR MIM; 611613; gene.
DR neXtProt; NX_Q6UW63; -.
DR OpenTargets; ENSG00000134901; -.
DR PharmGKB; PA134974174; -.
DR VEuPathDB; HostDB:ENSG00000134901; -.
DR eggNOG; KOG2458; Eukaryota.
DR GeneTree; ENSGT00940000158318; -.
DR HOGENOM; CLU_041919_0_0_1; -.
DR InParanoid; Q6UW63; -.
DR OMA; MFMDATL; -.
DR OrthoDB; 547457at2759; -.
DR PhylomeDB; Q6UW63; -.
DR TreeFam; TF323280; -.
DR PathwayCommons; Q6UW63; -.
DR SignaLink; Q6UW63; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79070; 23 hits in 1081 CRISPR screens.
DR ChiTaRS; KDELC1; human.
DR EvolutionaryTrace; Q6UW63; -.
DR GenomeRNAi; 79070; -.
DR Pharos; Q6UW63; Tbio.
DR PRO; PR:Q6UW63; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6UW63; protein.
DR Bgee; ENSG00000134901; Expressed in stromal cell of endometrium and 150 other tissues.
DR Genevisible; Q6UW63; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA: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 3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW 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_0000247163"
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 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 VARIANT 114
FT /note="I -> V (in dbSNP:rs1047740)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027080"
FT CONFLICT 109
FT /note="N -> S (in Ref. 2; BAD96287)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="D -> G (in Ref. 2; BAD96287)"
FT /evidence="ECO:0000305"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2DI7"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2DI7"
SQ SEQUENCE 502 AA; 58043 MW; 82633729E373E116 CRC64;
MFGTLLLYCF FLATVPALAE TGGERQLSPE KSEIWGPGLK ADVVLPARYF YIQAVDTSGN
KFTSSPGEKV FQVKVSAPEE QFTRVGVQVL DRKDGSFIVR YRMYASYKNL KVEIKFQGQH
VAKSPYILKG PVYHENCDCP LQDSAAWLRE MNCPETIAQI QRDLAHFPAV DPEKIAVEIP
KRFGQRQSLC HYTLKDNKVY IKTHGEHVGF RIFMDAILLS LTRKVKMPDV ELFVNLGDWP
LEKKKSNSNI HPIFSWCGST DSKDIVMPTY DLTDSVLETM GRVSLDMMSV QANTGPPWES
KNSTAVWRGR DSRKERLELV KLSRKHPELI DAAFTNFFFF KHDENLYGPI VKHISFFDFF
KHKYQINIDG TVAAYRLPYL LVGDSVVLKQ DSIYYEHFYN ELQPWKHYIP VKSNLSDLLE
KLKWAKDHDE EAKKIAKAGQ EFARNNLMGD DIFCYYFKLF QEYANLQVSE PQIREGMKRV
EPQTEDDLFP CTCHRKKTKD EL
