GCNT3_BUBBU
ID GCNT3_BUBBU Reviewed; 440 AA.
AC Q1M0V6; Q1M0W4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 58.
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 Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Murrah, River-type, and Swamp-type;
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}.
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DR EMBL; AY847312; AAY21831.1; -; Genomic_DNA.
DR EMBL; AY847313; AAY21832.1; -; Genomic_DNA.
DR EMBL; AY847321; AAY21840.1; -; Genomic_DNA.
DR RefSeq; XP_006072400.1; XM_006072338.1.
DR AlphaFoldDB; Q1M0V6; -.
DR SMR; Q1M0V6; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GeneID; 102398238; -.
DR KEGG; bbub:102398238; -.
DR CTD; 9245; -.
DR OrthoDB; 868849at2759; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0000139; C: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 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 beta-
FT 1,6-N-acetylglucosaminyltransferase 3"
FT /id="PRO_0000288544"
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"
FT VARIANT 115
FT /note="R -> Q (in strain: River-type)"
SQ SEQUENCE 440 AA; 51008 MW; 8F25E256DC7A5291 CRC64;
MKMTGWKKKL CRGHHLWALG CYMLLAVVAL RLSLRLKCDV DSLDLESRDF QSQRCRDVLY
KNLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRLP FTDTYYLNIT RDCERFKAQR
KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPEAFKEAVK
AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA
EMVLALKMLN GKNSMESEIP SEYKKNRWKY RYEVTDRLYL TSKMKDPPPD NLPMFTGNAY
FVASRAFVQH VLENPKSQRL IEWVKDTYSP DEHLWATLQR APWMPGSVPY HPKYHISDMT
AIARLVKWQN HEGDVSMGAP YAPCSGIHQR AICIYGAGDL HWILQNHHLL ANKFDPRVDD
NVLQCLEEYL RHKAIYGTEL
