GCNT3_XENLA
ID GCNT3_XENLA Reviewed; 443 AA.
AC Q5U258;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3;
DE EC=2.4.1.102 {ECO:0000250|UniProtKB:O95395};
DE EC=2.4.1.148 {ECO:0000250|UniProtKB:O95395};
DE EC=2.4.1.150 {ECO:0000250|UniProtKB:O95395};
DE AltName: Full=C2GnT-mucin type;
DE Short=C2GnT-M;
GN Name=gcnt3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosyltransferase that can synthesize all known mucin beta
CC 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan
CC branching, 2 important steps in mucin-type biosynthesis. Has also I-
CC branching enzyme activity by converting linear into branched poly-N-
CC acetyllactosaminoglycans. {ECO:0000250|UniProtKB:O95395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-
CC COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102;
CC Evidence={ECO:0000250|UniProtKB:O95395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923,
CC Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607;
CC EC=2.4.1.102; Evidence={ECO:0000250|UniProtKB:O95395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-
CC D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-
CC (1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372;
CC EC=2.4.1.150; Evidence={ECO:0000250|UniProtKB:O95395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56188, Rhea:RHEA-COMP:11691,
CC Rhea:RHEA-COMP:14412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:87079, ChEBI:CHEBI:139581;
CC EC=2.4.1.148; Evidence={ECO:0000250|UniProtKB:O95395};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-
CC beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-
CC threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56192, Rhea:RHEA-
CC COMP:11692, Rhea:RHEA-COMP:14413, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:87080,
CC ChEBI:CHEBI:139580; EC=2.4.1.148;
CC Evidence={ECO:0000250|UniProtKB:O95395};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
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DR EMBL; BC086270; AAH86270.1; -; mRNA.
DR RefSeq; NP_001088629.1; NM_001095160.1.
DR AlphaFoldDB; Q5U258; -.
DR SMR; Q5U258; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GeneID; 495681; -.
DR KEGG; xla:495681; -.
DR CTD; 495681; -.
DR Xenbase; XB-GENE-5887147; gcnt3.L.
DR OMA; AYTIITH; -.
DR OrthoDB; 868849at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 495681; Expressed in kidney and 3 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106325; F:acetylgalactosaminyl-O-glycosyl-seryl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106326; F:acetylgalactosaminyl-O-glycosyl-threonyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-
FT 1,6-N-acetylglucosaminyltransferase 3"
FT /id="PRO_0000288550"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..228
FT /evidence="ECO:0000250"
FT DISULFID 162..385
FT /evidence="ECO:0000250"
FT DISULFID 183..210
FT /evidence="ECO:0000250"
FT DISULFID 394..426
FT /evidence="ECO:0000250"
SQ SEQUENCE 443 AA; 51202 MW; 403A28322EC561A7 CRC64;
MSLMAHVRRK LCRGHLLRCT LPLTLLLFLT VGLKHLAIDC NLAHNNDIPM GSCMASYYTA
LNLSAPGEKN CHRIIQGDTE EARRALLDNL MVKKRRLVAT DGDYINATSD CKFFRERRKY
ITFSLSQVEQ DFPIAYSMVI HDNIEMFERL LRAVYTPHNI YCVHVDKKSP ESFQQAARAI
TSCFDNVFVA SKLESVVYAS WRRVQADLNC MEDLLQSNVQ WRYLINTCGT DFPIKTNAEM
VKALKSLNGH NSMESEIPPN YKKRRWEYHF ELKEDSNKIV QTNTRKKPSP LPVPVFSGNA
YIVVTRNFVN SLFVNPTAKK FIMWAKDTYS PDEYMWATLH RFAEMPGHMP AHQKYDTSDI
NAIARLVKWQ SLEGDMNKGA PYIPCTGTHR RQVCVYGTGD LNWMVQQHHF FANKFDPKVD
DNAIQCLEEY LRYKTFHPTE NVA
