PLGT3_RAT
ID PLGT3_RAT Reviewed; 508 AA.
AC Q566E5; Q497C8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein O-glucosyltransferase 3 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q7Z4H8};
DE AltName: Full=KDEL motif-containing protein 2 {ECO:0000312|RGD:1562027};
DE AltName: Full=Protein O-xylosyltransferase POGLUT3 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q7Z4H8};
DE Flags: Precursor;
GN Name=Poglut3; Synonyms=Kdelc2 {ECO:0000312|RGD:1562027};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Prostate;
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).
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:Q7Z4H8}.
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:Q7Z4H8};
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:Q7Z4H8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q7Z4H8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the KDELC family. {ECO:0000305}.
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DR EMBL; BC093594; AAH93594.1; -; mRNA.
DR EMBL; BC100617; AAI00618.1; -; mRNA.
DR RefSeq; NP_001020294.3; NM_001025123.3.
DR AlphaFoldDB; Q566E5; -.
DR SMR; Q566E5; -.
DR STRING; 10116.ENSRNOP00000009497; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR GlyGen; Q566E5; 1 site.
DR PhosphoSitePlus; Q566E5; -.
DR jPOST; Q566E5; -.
DR PaxDb; Q566E5; -.
DR PRIDE; Q566E5; -.
DR Ensembl; ENSRNOT00000009497; ENSRNOP00000009497; ENSRNOG00000007177.
DR GeneID; 315664; -.
DR KEGG; rno:315664; -.
DR UCSC; RGD:1562027; rat.
DR CTD; 143888; -.
DR RGD; 1562027; Poglut3.
DR eggNOG; KOG2458; Eukaryota.
DR GeneTree; ENSGT00940000159028; -.
DR HOGENOM; CLU_041919_0_0_1; -.
DR InParanoid; Q566E5; -.
DR OMA; PVISWCG; -.
DR OrthoDB; 547457at2759; -.
DR PhylomeDB; Q566E5; -.
DR TreeFam; TF323280; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q566E5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000007177; Expressed in ovary and 20 other tissues.
DR Genevisible; Q566E5; RN.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..508
FT /note="Protein O-glucosyltransferase 3"
FT /id="PRO_0000247197"
FT REPEAT 25..134
FT /note="Filamin"
FT REGION 480..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 505..508
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 496
FT /note="R -> C (in Ref. 1; AAI00618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 58701 MW; E04AB38138CC5DF9 CRC64;
MLGVRRALLL PPLQLALLVA AGTGARVSAP RSLAWGPGLH ADAVLPVRYF FLQSVDSDGR
NFTSSPPGQT QFKVVVKSLS PKELVRIYVP KPLDRNDGTF LVRYRMHETV HEGLKIEILY
GGEHVAQSPY ILKGPVYHEY CDCPEDDPQA WQKTLSCPAN EPQIEQDFIS FPSINLQQML
KEVPKRFGDE RGAIVHYTIL NNHIYRRSLG KYTDFKMFSD EILLSLARKV TLPDLEFYIN
LGDWPLEHRK VNDTPGPIPI ISWCGSLDSR DIILPTYDVT HSTLEAMRGV TNDLLSVQGN
TGPSWINKTE KAFFRGRDSR EERLQLVLLS KENPQLLDAG ITGYFFFQEK EKELGKAKLM
GFFDFFKYKY QVNVDGTVAA YRYPYLMLGD SLVLKQESPY YEHFYVELRP WKHYVPIKRN
LSDLLEKVKW AKENDEEAKR IAKEGQLTAR DLLQPPRLYC YYYRVLQKYA ERQVSKPMIR
DGMERVPQPD DSTSVRQCHR KRPEREEL
