GCNT3_BHV4V
ID GCNT3_BHV4V Reviewed; 440 AA.
AC Q9IZK2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, 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:0000269|PubMed:10811884};
DE EC=2.4.1.148 {ECO:0000269|PubMed:10811884};
DE EC=2.4.1.150 {ECO:0000269|PubMed:10811884};
DE AltName: Full=BORFF3-4;
DE AltName: Full=C2GnT-mucin type;
DE Short=C2GnT-M;
GN Name=Bo17;
OS Bovine herpesvirus 4 (strain V. test) (BoHV-4) (Movar virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=436507;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10811884; DOI=10.1073/pnas.100058897;
RA Vanderplasschen A., Markine-Goriaynoff N., Lomonte P., Suzuki M.,
RA Hiraoka N., Yeh J.-C., Bureau F., Willems L., Thiry E., Fukuda M.,
RA Pastoret P.-P.;
RT "A multipotential beta -1,6-N-acetylglucosaminyl-transferase is encoded by
RT bovine herpesvirus type 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5756-5761(2000).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14769893; DOI=10.1099/vir.0.19715-0;
RA Markine-Goriaynoff N., Gillet L., Karlsen O.A., Haarr L., Minner F.,
RA Pastoret P.-P., Fukuda M., Vanderplasschen A.;
RT "The core 2 beta-1,6-N-acetylglucosaminyltransferase-M encoded by bovine
RT herpesvirus 4 is not essential for virus replication despite contributing
RT to post-translational modifications of structural proteins.";
RL J. Gen. Virol. 85:355-367(2004).
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. {ECO:0000269|PubMed:10811884,
CC ECO:0000269|PubMed:14769893}.
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:0000269|PubMed:10811884};
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:0000269|PubMed:10811884};
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:0000269|PubMed:10811884};
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:0000269|PubMed:10811884};
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:0000269|PubMed:10811884};
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). {ECO:0000269|PubMed:10811884, ECO:0000269|PubMed:14769893}.
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}.
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DR EMBL; AF231105; AAF72001.1; -; Genomic_DNA.
DR SMR; Q9IZK2; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR BRENDA; 2.4.1.102; 923.
DR BRENDA; 2.4.1.148; 923.
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_0000288554"
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; 50702 MW; 71B9C3B6B4A949BD 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 TSKIKDPPPD NLPMFTGNAY
FVASRAFVQH VLDNPKSQIL VEWVKDTYSP DEHLWATLQR APWMPGSVPS HPKYHISDMT
AIARLVKWQY HEGDVSMGAP YAPCSGIHRR AICIYGAGDL YWILQNHHLL ANKFDPRVDD
NVLQCLEEYL RHKAIYGTEL
