ID GCNT3_SYNCA Reviewed; 440 AA. AC Q866Z4; Q1M0V7; Q1M0V9; Q1M0W3; 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 Syncerus caffer (African buffalo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Syncerus. OX NCBI_TaxID=9970; 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Dewals B., Markine-Goriaynoff N., de Fays K., Minner F., Daix V., RA Vercammen F., Gaillard C., Sharp P.M., Vanderplasschen A.; RT "Phylogeographical analysis of bovine herpesvirus 4: demonstration that RT inter-strain recombination events took place after acquisition of the Bo17 RT gene from an ancestor of the African buffalo."; RL Submitted (DEC-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, 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; AF465337; AAO22164.1; -; Genomic_DNA. DR EMBL; AY847314; AAY21833.1; -; Genomic_DNA. DR EMBL; AY847315; AAY21834.1; -; Genomic_DNA. DR EMBL; AY847316; AAY21835.1; -; Genomic_DNA. DR EMBL; AY847317; AAY21836.1; -; Genomic_DNA. DR EMBL; AY847318; AAY21837.1; -; Genomic_DNA. DR EMBL; AY847319; AAY21838.1; -; Genomic_DNA. DR EMBL; AY847320; AAY21839.1; -; Genomic_DNA. DR AlphaFoldDB; Q866Z4; -. DR SMR; Q866Z4; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q866Z4; 1 site, No reported glycans. DR UniPathway; UPA00378; -. 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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. 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; Signal-anchor; Transferase; Transmembrane; 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_0000288549" 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; 51079 MW; 480A0D5847B5843B CRC64; MKMTGWKKKL CRGHHLWALG CYMLLAVVAL RLSLRLKCDV DSLDLESRDF QSQRCRDILY KNLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRLP FTDTYYLNIT RDCERFKAQR KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA EMVLALKMLN GKNSMESEIP SEYKKNRWKY RYEVTDRLYL TSKMKDPPPD NLPMFTGNAY FVASRAFVQH VLENPKSQRL IEWVKDTYSP DEHLWATLQR APWMPGSVPY HPKYHISDMT AIARLVKWQD HEGDVSMGAP YAPCSGIHQR AICIYGAGDL YWILQNHHLL ANKFDPRVDD NVLQCLEEYL RHKAIYGTEL //