ID GCNT3_BOSMU Reviewed; 440 AA. AC Q866Z5; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 67. 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 Bos mutus grunniens (Wild yak) (Bos grunniens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=30521; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12525612; DOI=10.1128/jvi.77.3.1784-1792.2003; RA Markine-Goriaynoff N., Georgin J.-P., Goltz M., Zimmermann W., Broll H., RA Wamwayi H.M., Pastoret P.-P., Sharp P.M., Vanderplasschen A.; RT "The core 2 beta-1,6-N-acetylglucosaminyltransferase-mucin encoded by RT bovine herpesvirus 4 was acquired from an ancestor of the African RT buffalo."; RL J. Virol. 77:1784-1792(2003). 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, leading to introduce the blood group I CC antigen during embryonic development. {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 -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF465336; AAO22163.1; -; Genomic_DNA. DR AlphaFoldDB; Q866Z5; -. DR SMR; Q866Z5; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q866Z5; 1 site, No reported glycans. DR Ensembl; ENSBGRT00000015812.1; ENSBGRP00000013705.1; ENSBGRG00000008683.1. DR GeneTree; ENSGT00940000159331; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000694520; Chromosome 11. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. 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:0050892; P:intestinal absorption; IEA:Ensembl. DR GO; GO:0060993; P:kidney morphogenesis; IEA:Ensembl. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR GO; GO:0048729; P:tissue morphogenesis; IEA:Ensembl. DR InterPro; IPR003406; Glyco_trans_14. DR PANTHER; PTHR19297:SF81; BETA-1,3-GALACTOSYL-O-GLYCOSYL-GLYCOPROTEIN BETA-1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE 3; 1. DR PANTHER; PTHR19297; GLYCOSYLTRANSFERASE 14 FAMILY MEMBER; 1. DR Pfam; PF02485; Branch; 1. PE 3: Inferred from homology; KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..440 FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein FT beta-1,6-N-acetylglucosaminyltransferase 3" FT /id="PRO_0000288542" FT TOPO_DOM 1..12 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 13..30 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 31..440 FT /note="Lumenal" FT /evidence="ECO:0000255" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 73..230 FT /evidence="ECO:0000250" FT DISULFID 164..384 FT /evidence="ECO:0000250" FT DISULFID 185..212 FT /evidence="ECO:0000250" FT DISULFID 393..425 FT /evidence="ECO:0000250" SQ SEQUENCE 440 AA; 50909 MW; EF7A85AE17A5A289 CRC64; MKMTGWKKKL CRGHHLWALG CYSLLAVVAL RLSLRLKCDV DSLDLESRDF QSQRCRDVLY KNLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRLP FTDTYYLNIT RDCEQFKAQR KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA EMVLALKMLN GKNSMESEIP SEYKKNRWKY RYEVTDRLYL TSKMKDPPPD NLPMFTGNAY FVASRAFVQH VLENPKSQRL IEWVKDTYSP DEHLWATLQR APWMPGSVPY HPKYHISDMT AIARLVKWQG HEGDVSMGAP YAPCSGIHQR AICIYGAGDL HWILQNHHLL ANKFDPRVDD NVLQCLEEYL RHKAIYGTEL //