PGLT1_BOVIN
ID PGLT1_BOVIN Reviewed; 392 AA.
AC Q5E9Q1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein O-glucosyltransferase 1;
DE EC=2.4.1.376 {ECO:0000250|UniProtKB:Q8NBL1};
DE AltName: Full=CAP10-like 46 kDa protein;
DE AltName: Full=KTEL motif-containing protein 1;
DE AltName: Full=O-glucosyltransferase Rumi homolog;
DE Short=Rumi;
DE AltName: Full=Protein O-xylosyltransferase;
DE EC=2.4.2.63 {ECO:0000250|UniProtKB:Q8NBL1};
DE Flags: Precursor;
GN Name=POGLUT1; Synonyms=CLP46, KTELC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. Specifically targets extracellular EGF repeats of protein
CC such as CRB2, F7, F9 and NOTCH2 (By similarity). Acts as a positive
CC regulator of Notch signaling by mediating O-glucosylation of Notch,
CC leading to regulate muscle development (By similarity). Notch
CC glucosylation does not affect Notch ligand binding (By similarity).
CC Required during early development to promote gastrulation: acts by
CC mediating O-glucosylation of CRB2, which is required for CRB2
CC localization to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q8BYB9, ECO:0000250|UniProtKB:Q8NBL1}.
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:0000250|UniProtKB:Q8NBL1};
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:0000250|UniProtKB:Q8NBL1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8BYB9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q8NBL1}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
CC {ECO:0000305}.
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DR EMBL; BT020869; AAX08886.1; -; mRNA.
DR RefSeq; NP_001014903.1; NM_001014903.1.
DR AlphaFoldDB; Q5E9Q1; -.
DR SMR; Q5E9Q1; -.
DR STRING; 9913.ENSBTAP00000011287; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR PaxDb; Q5E9Q1; -.
DR PRIDE; Q5E9Q1; -.
DR Ensembl; ENSBTAT00000011287; ENSBTAP00000011287; ENSBTAG00000008562.
DR GeneID; 511862; -.
DR KEGG; bta:511862; -.
DR CTD; 56983; -.
DR VEuPathDB; HostDB:ENSBTAG00000008562; -.
DR VGNC; VGNC:33108; POGLUT1.
DR eggNOG; KOG2458; Eukaryota.
DR GeneTree; ENSGT00940000158283; -.
DR HOGENOM; CLU_041919_1_0_1; -.
DR InParanoid; Q5E9Q1; -.
DR OMA; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
DR TreeFam; TF323280; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000008562; Expressed in cumulus cell and 108 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS: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; 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: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; ISS:UniProtKB.
DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS: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 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Gastrulation;
KW Glycoprotein; Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..392
FT /note="Protein O-glucosyltransferase 1"
FT /id="PRO_0000246684"
FT REGION 103..107
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT REGION 172..178
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
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:0000250|UniProtKB:Q8T045"
FT BINDING 177
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT BINDING 212
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT BINDING 218
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT BINDING 274..279
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT SITE 132
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT SITE 240
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..56
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT DISULFID 54..357
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT DISULFID 102..108
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
FT DISULFID 263..286
FT /evidence="ECO:0000250|UniProtKB:Q8NBL1"
SQ SEQUENCE 392 AA; 46009 MW; 59FF5C0B59429DEC CRC64;
MELGVSSQLW LWLLLLLLPP VPGREKESGS KWKVFIDQIN RALENYEPCS SPNCSCYHGV
IEEDLTPFRG GISRKMMAEV VRRKLGTHYQ IIKNRLYRES DCMFPSRCSG VEHFILEVIG
RLPDMEMVIN VRDYPQVPKW MEPAIPIFSF SKTLEYHDIM YPAWTFWEGG PAVWPIYPMG
LGRWDLFRED LVRSAAQWPW KKKNSTAYFR GSRTSPERDP LILLSRKNPK LVDAEYTKNQ
AWKSMKDTLG KPAAKDVHLV DHCKYKYLFN FRGVAASFRF KHLFLCGSLV FHVGDEWLEF
FYPQLKPWVH YIPVKTDLSN VQELLQFVKA NDDVAQEIAE RGSQFILNHL KMDDITCYWE
NLLTEYSKFL SYNVTRRKGY DQIVPKILKI EL
