GCNT3_BHV4D
ID GCNT3_BHV4D Reviewed; 440 AA.
AC Q99CW3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 10-FEB-2021, entry version 74.
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 DN-599) (BoHV-4) (Movar virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10355;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9689; Panthera leo (Lion).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11152491; DOI=10.1128/jvi.75.3.1186-1194.2001;
RA Zimmermann W., Broll H., Ehlers B., Buhk H.-J., Rosenthal A., Goltz M.;
RT "Genome sequence of bovine herpesvirus 4, a bovine Rhadinovirus, and
RT identification of an origin of DNA replication.";
RL J. Virol. 75:1186-1194(2001).
RN [2]
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; AF318573; AAK07999.1; -; Genomic_DNA.
DR EMBL; AF465332; AAO22159.1; -; Genomic_DNA.
DR RefSeq; NP_076572.1; NC_002665.1.
DR SMR; Q99CW3; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PRIDE; Q99CW3; -.
DR GeneID; 1684881; -.
DR KEGG; vg:1684881; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0044178; C:host cell 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 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 beta-
FT 1,6-N-acetylglucosaminyltransferase"
FT /id="PRO_0000288552"
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 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; 50764 MW; C88B3EAB8FDB8DD9 CRC64;
MKMAGWKKKL CRGHHLWALG CYMLLAVVSL RLSLRFKCDV DSLDLESRDF QSQHCRDMLY
NSLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRSP LTGTYYLNIT RDCERFKAQR
KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK
AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA
EMVLALKMLK GKNSMESEVP SESKKNRWKY RYEVTDTLYP TSKMKDPPPD NLPMFTGNAY
FVASRAFVQH VLDNPKSQRL VEWVKDTYSP DEHLWATLQR APWMPGSVPS HPKYHISDMT
AIARLVKWQY HEGDVSMGAP YAPCSGIHRR AICIYGAGDL YWILQNHHLL ANKFDPRVDD
NVLQCLEEYL RHKAIYGTEL
