ID GCNT3_BHV4L Reviewed; 440 AA. AC Q805R1; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 70. DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase; DE EC=2.4.1.102 {ECO:0000250|UniProtKB:Q9IZK2}; DE EC=2.4.1.148 {ECO:0000250|UniProtKB:Q9IZK2}; DE EC=2.4.1.150 {ECO:0000250|UniProtKB:Q9IZK2}; DE AltName: Full=C2GnT-mucin type; DE Short=C2GnT-M; GN Name=Bo17; OS Bovine herpesvirus 4 (strain LVR140) (BoHV-4) (Movar virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Rhadinovirus; OC Rhadinovirus bovinegamma4. OX NCBI_TaxID=436506; OH NCBI_TaxID=9913; Bos taurus (Bovine). 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: Non-essential glycosyltransferase that can synthesize all CC known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 CC O-glycan branching, 2 important steps in mucin-type biosynthesis. Has CC also I-branching enzyme activity by converting linear into branched CC poly-N-acetyllactosaminoglycans. Contributes to the post-translational CC modifications of structural proteins. 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:Q9IZK2}; 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:Q9IZK2}; 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:Q9IZK2}; 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:Q9IZK2}; 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:Q9IZK2}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000250}; CC Single-pass type II membrane protein {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expressed during BHV-4 replication (at protein CC level). CC -!- MISCELLANEOUS: Was acquired from an ancestor of the African buffalo CC around 1.5 million years ago. 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; AF465330; AAO22157.1; -; Genomic_DNA. DR EMBL; AF465331; AAO22158.1; -; Genomic_DNA. DR SMR; Q805R1; -. DR CAZy; GT14; Glycosyltransferase Family 14. DR GlyCosmos; Q805R1; 2 sites, No reported glycans. DR UniPathway; UPA00378; -. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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 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 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Glycosyltransferase; Host Golgi apparatus; KW Host membrane; Membrane; 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" FT /id="PRO_0000288553" FT TOPO_DOM 1..9 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 10..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 72 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine; by host" 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; 50720 MW; 1B79C51ADC85633D CRC64; MKMAGWKKKL CPGHHLWALG CYMLLAVVSL RLSLRFKCDV DSLDLESRDF QSQHCRDMLY NSLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRPP LTDTYYLNIT RDCERFKAQR KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VSWKYLLNTC GTDFPIKTNA EMVLALKMLK GKNSMESEVP SESKKNRWKY RYEVTDTLYP TSKMKDPPPD NLPMFTGNAY FVASRAFVQH VLDNPKSQIL VEWVKDTYSP DEHLWATLQR APWMPGSVPS HPKYHISDMT AIARLVKWQY HEGDVSMGAP YAPCSGIHRR AICIYGAGDL YWILQNHHLL ANKFDPRVDD NVLQCLEEYL RHKAIYGTEL //