GCNT3_BOVIN
ID GCNT3_BOVIN Reviewed; 440 AA.
AC Q7YQE1; Q7YQF8; Q866Z3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 AltName: Full=Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase;
DE AltName: Full=bC2GnT-M;
DE Short=C2GnT-M;
GN Name=GCNT3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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 / MRNA].
RC TISSUE=Colon, and Tracheal epithelium;
RX PubMed=14592928; DOI=10.1165/rcmb.2003-0202oc;
RA Choi K.H., Osorio F.A., Cheng P.-W.;
RT "Mucin biosynthesis: bovine C2GnT-M gene, tissue-specific expression, and
RT herpes virus-4 homologue.";
RL Am. J. Respir. Cell Mol. Biol. 30:710-719(2004).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION.
RX PubMed=15226299; DOI=10.1074/jbc.m401046200;
RA Singh J., Khan G.A., Kinarsky L., Cheng H., Wilken J., Choi K.H.,
RA Bedows E., Sherman S., Cheng P.-W.;
RT "Identification of disulfide bonds among the nine core 2 N-
RT acetylglucosaminyltransferase-M cysteines conserved in the mucin beta6-N-
RT acetylglucosaminyltransferase family.";
RL J. Biol. Chem. 279:38969-38977(2004).
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 -!- TISSUE SPECIFICITY: Primarily expressed in mucus-secreting tissues.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:15226299}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
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DR EMBL; AF465338; AAO22165.1; -; Genomic_DNA.
DR EMBL; AY283763; AAP76324.1; -; mRNA.
DR EMBL; AY283764; AAP76325.1; -; mRNA.
DR EMBL; AY283765; AAP76326.1; -; mRNA.
DR EMBL; AY283766; AAP76327.1; -; mRNA.
DR EMBL; AY283767; AAP76328.1; -; Genomic_DNA.
DR RefSeq; NP_991378.1; NM_205809.1.
DR RefSeq; XP_005211713.1; XM_005211656.3.
DR RefSeq; XP_010807543.1; XM_010809241.2.
DR AlphaFoldDB; Q7YQE1; -.
DR SMR; Q7YQE1; -.
DR STRING; 9913.ENSBTAP00000012427; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR PaxDb; Q7YQE1; -.
DR PRIDE; Q7YQE1; -.
DR Ensembl; ENSBTAT00000012427; ENSBTAP00000012427; ENSBTAG00000009443.
DR Ensembl; ENSBTAT00000079217; ENSBTAP00000064426; ENSBTAG00000009443.
DR GeneID; 404167; -.
DR KEGG; bta:404167; -.
DR CTD; 9245; -.
DR VEuPathDB; HostDB:ENSBTAG00000009443; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000159331; -.
DR HOGENOM; CLU_032341_1_2_1; -.
DR InParanoid; Q7YQE1; -.
DR OMA; IHQRAVC; -.
DR OrthoDB; 868849at2759; -.
DR TreeFam; TF315534; -.
DR Reactome; R-BTA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000009443; Expressed in abomasum and 93 other tissues.
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:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
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:0050892; P:intestinal absorption; IEA:Ensembl.
DR GO; GO:0060993; P:kidney morphogenesis; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0048729; P:tissue morphogenesis; IEA:Ensembl.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW 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_0000288543"
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"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..230
FT /evidence="ECO:0000269|PubMed:15226299"
FT DISULFID 164..384
FT /evidence="ECO:0000269|PubMed:15226299"
FT DISULFID 185..212
FT /evidence="ECO:0000269|PubMed:15226299"
FT DISULFID 393..425
FT /evidence="ECO:0000269|PubMed:15226299"
FT CONFLICT 72
FT /note="N -> S (in Ref. 1; AAO22165)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Y -> S (in Ref. 2; AAP76324/AAP76326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50953 MW; 94D0EF6A08D9DA10 CRC64;
MKMTGWKKKL CRGHHLWALG CYMLLAVVAL RLSLRLKCDV DSLDLESRDF QSQRCRDVLY
KNLKLPAKRS INCSGITRGD QEAVVQALLD NLEVKKKRLP FTDTYYLNIT RDCEQFKAQR
KFIQFPLSKE ELDFPIAYSM VVHEKIENFE RLLRAVYAPQ NIYCVHVDVK SPETFKEAVK
AIISCFPNVF MASKLVPVVY ASWSRVQADL NCMEDLLQSS VPWKYLLNTC GTDFPIKTNA
EMVLALKMLN GKNSMESEIP SEYKKNRWKY RYEVTDRLYL TSKMKDPPPD NLPMFTGNAY
FVASRAFVQH VLENPKSQRL IEWVKDTYSP DEHLWATLQR APWMPGSVPY HPKYHISDMT
AIARLVKWQG HEGDVSMGAP YAPCSGIHQR AICIYGAGDL HWILQNHHLL ANKFDPRVDD
NVLQCLEEYL RHKAIYGTEL
